ProSpec-EGF (Leu 21) Human

Description

Catalogue number

CYT-466

Synonyms

Urogastrone, URG, EGF.

Introduction

Description

EGF 21-Leu Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6205 Dalton.
The EGF 21-Leu is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with no additives.

Solubility

It is recommended to reconstitute the lyophilized Epidermal Growth Factor 21-Leu in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

The sequence of the first five N-terminal amino acids was determined and was found to be Asn-Ser-Asp-Ser-Glu.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

Usage

Prospec’s products are furnished for LABORATORY RESEARCH USE ONLY.They may not be used as drugs,agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGF Human

Description

Catalogue number

CYT-217

Synonyms

Urogastrone, URG, EGF.

Introduction

Description

Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution containing PBS pH-7.4.

Solubility

It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by: Analysis by HPLC. Analysis by -PAGE.

Amino acid sequence

NECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0×10⁷ IU/mg.

References

1.Title:Activation of the Hedgehog pathway in pilocytic astrocytomas.
Publication:Neuro Oncol 12 : 790-798. doi: 10.1093/neuonc/noq026 First published online: March 11, 2010
Link:http://neurooncology.oxfordjournals.org/content/12/8/790.full

2.Title:Evaluation of bioactivity and effect of polymeric stabilizers during heat treatment for the unfolded fraction of human epidermal growth factor.
Publication:SEN’I GAKKAISHI vol.67,nov.8
Link:http://www.jstage.jst.go.jp/article/fiber/67/8/185/_pdf

3.Title:GPR56 is essential for testis development and male fertility in mice.
Publication:Article first published online: 27 OCT 2010 DOI: 10.1002/dvdy.22468
Link:http://onlinelibrary.wiley.com/doi/10.1002/dvdy.22468/full

4.Title:Changing the Receptor Specificity of Anthrax Toxin.
Publication:doi: 10.1128/?mBio.00088-12 1 May 2012 mBio vol. 3 no. 3 e00088-12
Link:http://mbio.asm.org/content/3/3/e00088-12.full

5.Title:Characterization of Non-Specific Cytotoxic Cell Receptor Protein 1: A New Member of the Lectin-Type Subfamily of F-Box Proteins.
Publication:Kallio H, Tolvanen M, J?nis J, Pan P-w, Laurila E, et al. Characterization of Non-Specific Cytotoxic Cell Receptor Protein 1: A New Member of the Lectin-Type Subfamily of F-Box Proteins. PLoS ONE 6: e27152. doi:10.1371/journal.pone.0027152
Link:http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0027152

6. Title: Cancer-Associated Carbonic Anhydrases IX and XII: Effect of Growth Factors on Gene Expression in Human Cancer Cell Lines.

Publication: Journal of Cancer Molecules 5: 73-78, 2010.

Link: http://mupnet.com/JOCM%205%2073-78.pdf

7. Title: EGR-1 activation by EGF inhibits MMP-9 expression and lymphoma growth

Publication: Blood 116.5 : 759-766.
Link: http://www.bloodjournal.org/content/116/5/759.long?sso-checked=true

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGF Human, Pichia

Description

Catalogue number

CYT-332

Synonyms

Urogastrone, URG, EGF.

Introduction

Description

Epidermal Growth Factor Human Recombinant produced in Pichia Pastoris is a single, glycosylated, polypeptide chain containing 51 amino acids and having a molecular mass of 6KDa.
The EGF is purified by proprietary chromatographic techniques.

Source

Pichia Pastoris.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a filtered concentrated solution in PBS, pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below
-18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

NECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

Biological Activity

The ED₅₀, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is < 0.1 ng/ml corresponding to a specific activity of 1 x 10⁷Units/mg.

Usage

Prospec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGF Long Human

Description

Catalogue number

CYT-798

Synonyms

Urogastrone, URG, EGF.

Introduction

Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.

Description

Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa.
The EGF Long is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.

Solubility

It is recommended to reconstitute the lyophilized EGF Long in sterile 100mM AcOH not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized EGF Long although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF Long should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR

Biological Activity

The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶ IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGF Mouse

Description

Catalogue number

CYT-554

Synonyms

Urogastrone, URG, EGF.

Introduction

Description

Epidermal Growth Factor Mouse purified from submaxillary gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.1 kDa.
The EGF is purified by proprietary chromatographic techniques.

Source

Mouse Submaxillary Gland.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution containing 0.01M sodium acetate buffer.

Solubility

It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Epidermal Growth Factor Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Biological Activity

The biological activity is measured in a proliferation assay using BALB/MK cells.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGF Mouse Protein

Description

Catalogue number

CYT-326

Synonyms

Urogastrone, URG, EGF.

Introduction

Description

Epidermal Growth Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids including 3 intramolecular disulfide-bonds and having a molecular mass of 6 kDa.
The EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized with no additives.

Solubility

It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Purity

Greater than 98.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR.

Biological Activity

The activity is determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells and is typically less than 0.1ng/ml.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGF Mouse, Biotin

Description

Catalogue number

CYT-841

Synonyms

Urogastrone, URG, EGF.

Introduction

Description

EGF Mouse Recombinant, Biotin produced in E.Coli is a non-glycosylated polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. This version of EGF has a N terminal leader sequence hosting a biotin conjugation. There are 0.5 biotins for each EGF protein.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

The protein solution contains sterile PBS.

Stability

Should be stored at 4°C.
Please do not freeze.

Purity

Greater than 95.0% as determined by analysis by -PAGE.

Amino acid sequence

MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1×10⁶units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGF Mouse, His

Description

Catalogue number

CYT-138

Synonyms

Urogastrone, URG, EGF.

Introduction

Description

EGF mouse Recombinant produced in E. coli is a single polypeptide chain containing 77 amino acids and having a molecular mass of 8.6kDa.
EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

The EGF solution contains 20mM Tris-HCl buffer , 100mM NaCl, 2mM DTT and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 90% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGF Mouse, His Active

Description

Catalogue number

CYT-1054

Synonyms

AI790464, Pro-epidermal growth factor, URG.

Introduction

Pro-Epidermal Growth Factor Isoform 1 or EGF, is a globular peptide which includes three intra molecular disulfide bonds. This protein acts as a growth factor that mediates the growth and proliferation of different epithelial & epidermal cells. Among other processes that EGF is part of are inhibition of gastric secretion and wound healing. EGF is a ligand for class I tyrosine kinase receptor .

Description

EGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.6kDa.EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

EGF protein solution contains 10% glycerol, 20mM Tris-HCl , 0.1M NaCl & 2mM DTT.

Stability

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

Measured in a cell proliferation assay using mouse Balb/3T3 cell. The ED50 for this effect less or equal to 1ng/ml.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.

Usage

Prospec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGF Rat

Description

Catalogue number

CYT-669

Synonyms

Urogastrone, URG, EGF.

Introduction

Description

Epidermal Growth Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6151 Dalton.
The Rat EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Rat EGF was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized Rat EGF in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Rat EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat EGF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.

Biological Activity

The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGF Rat Protein

Description

Catalogue number

CYT-556

Synonyms

Urogastrone, URG, EGF.

Introduction

Description

Epidermal Growth Factor Rat purified from submandibular gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.15 kDa.
The EGF is purified by proprietary chromatographic techniques.

Source

Adult Male Rat Submandibular Glands.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution containing 0.01M sodium acetate buffer.

Solubility

It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below
-18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 99.0% as determined by Analysis by RP-HPLC.
Analysis by -PAGE.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EGFL6 Human

Description

Catalogue number

CYT-974

Synonyms

EGF Like Domain Multiple 6, MAM and EGF Domains-Containing Gene Protein, MAM and EGF Domain Containing, EGF-Like Protein 6, MAEG, EGF Repeat-Containing Protein 6, W80, EGFL6.

Introduction

Epidermal Growth Factorlike Domain Multiple 6 belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors.

Description

EGF Like Domain Multiple 6 Human Recombinant produced in HEK cells is a polypeptide chain starting at amino acid Asn at position 22 to amino acid Arg at position 363, fused to an FC, 6 x His-tag at C-terminus, containing a total of 348 amino acids and having a predicted molecular mass of 40-55kDa. The EGFL6 is purified by proprietary chromatographic techniques.

Source

HEK .

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The EGFL6 protein was lyophilized from a 0.2µm filtered solution in 20mM MES and 500mM NaCl, pH 6.0 with 5% Trehalose.

Solubility

It is recommended to reconstitute the lyophilized EGFL6 in sterile PBS at 500µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized EGFL6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGFL6 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Biological Activity

EGFL6 activity is determined by its ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The expected ED50 for this effect is 1-5 μg/ml.

ProSpec-EGFL6 Mouse

Description

Catalogue number

CYT-1105

Synonyms

Epidermal growth factor-like protein 6, EGF-L6, Egfl6, Maeg.

Introduction

Description

EGFL6 Mouse Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 273 amino acids and having a molecular mass of 31.1kDa .
EGFL6 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

EGFL6 protein solution contains Phosphate Buffered Saline containing 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

ADLTMKKKVK LKMVTPRPAS TRVPKVNLPY SSEEGVSRGR NYDGEQKKKE EGKRERLEEE
KGEKTLRNEV EQERTLRGDV FSPKVNEAED LDLVYVQRKE LNSKLKHKDL NISVDCSFDL
GVCDWKQDRE DDFDWHPADR DNDVGYYMAV PALAGHKKNI GRLKLLLPNL TPQSNFCLLF
DYRLAGDKVG KLRVFVKNSN NALAWEETKN EDGRWRTGKI QLYQGIDTTK SVIFEAERGK GKTGEIAVDG VLLVSGLCPD DFLSVEGHHH HHH.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-HB-EGF Human

Description

Catalogue number

CYT-119

Synonyms

HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

Introduction

HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC , fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

Description

HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa.

The HB-EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution containing 10mM sodium phosphate pH-7.5.

Solubility

It is recommended to reconstitute the lyophilized Human HB-EGF in sterile 18M-cm H₂O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Human HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC

KYVKELRAPS CICHPGYHGE RCHGLSL.

Biological Activity

The ED₅₀ was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 10⁶units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-HB-EGF Human, His

Description

Catalogue number

CYT-761

Synonyms

Proheparin-binding EGF-like growth factor, HBEGF, DTR, DTS, HEGFL, HB-EGF, Heparin-binding EGF-like growth factor, Diphtheria toxin receptor, DT-R, DTSF.

Introduction

HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC , fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind heparin and heparin sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

Description

HB-EGF His Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 109 amino acids and having a molecular mass of 12.1kDa.
HB-EGF His is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

The HB-EGF His solution contains 20mM Tris-HCl buffer , 0.2M NaCl, 2mM DTT and 50% glycerol.

Stability

Purity

Greater than 85% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGSDLQEADL DLLRVTLSSK PQALATPNKE EHGKRKKKGK GLGKKRDPCL RKYKDFCIHG ECKYVKELRA PSCICHPGYH GERCHGLSL.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-HB-EGF Mouse

Description

Catalogue number

CYT-068

Synonyms

DTR, HEGFL, diphtheria toxin receptor, DTSF.

Introduction

HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC , fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

Description

HB-EGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.8 kDa.
The HB-EGF is purified by proprietary chromatographic techniques

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was filtered and lyophilized from a concentrated solution containing 10mM PB and 500mM NaCl, pH7.4.

Solubility

It is recommended to reconstitute the lyophilized Mouse HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Mouse HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 97.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

DLEGTDLNLF KVAFSSKPQG LATPSKERNG KKKKKGKGLG KKRDPCLRKY KDYCIHGECR YLQEFRTPSC KCLPGYHGHR CHGLTL.

Biological Activity

The ED50 was determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×10⁶ units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-HB-EGF Rat

Description

Catalogue number

CYT-170

Synonyms

Proheparin-binding EGF-like growth factor, Heparin-binding EGF-like growth factor, HB-EGF, HBEGF, Dtr, Hegfl, GFHB.

Introduction

HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC , fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind heparin and heparin sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

Description

HB-EGF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa.
The HB-EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was filtered and lyophilized from a concentrated solution containing PBS, 300mM NaCl, pH 7.4 and 5% trehalose.

Solubility

It is recommended to reconstitute the lyophilized Rat HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Rat HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

DLEGTDLDLF KVAFSSKPQA LATPGKEKNG KKKRKGKGLG KKRDPCLKKY KDYCIHGECR YLKELRIPSC HCLPGYHGQR CHGLTL.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×10⁶ units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPGN Human

Description

Catalogue number

CYT-601

Synonyms

EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

Introduction

EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.

Description

Epigen Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 7.9 kDa.
Epigen is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

EPGN was lyophilized from 20mM PBS buffer pH-7.4 containing 130mM sodium chloride.

Solubility

It is recommended to reconstitute the lyophilized Epigen in sterile 18MΩ-cm H₂O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Epigen although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution EPGN should be stored at 4C between 2-7 days and for future use below -18C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPGN Human, His

Description

Catalogue number

CYT-794

Synonyms

EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

Introduction

Description

EPGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids and having a molecular mass of 12.1kDa.

EPGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

EPGN protein solution containing 20mM Tris-HCl buffer , 10% glycerol and 0.4M Urea.

Stability

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K

Usage

Prospec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPGN Human, Sf9

Description

Catalogue number

CYT-1038

Synonyms

Epithelial mitogen, EPG, Epithelial Mitogen Homolog , Epithelial Mitogen Homolog, ALGV3072, PRO9904, Epigen, EPGN.

Introduction

Description

EPGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 10.8kDa .
EPGN is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

EPGN protein solution contains Phosphate Buffered Saline and 10% glycerol

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

ADPAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE KHHHHHH.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPO a Fc Human

Description

Catalogue number

CYT-325

Synonyms

EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

Introduction

This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

Description

Erythropoietin-alpha Fc-Chimera Human Recombinant is produced in Chinese hamster ovary cells by recombinant DNA technology is a dimeric, glycosilated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing -PAGE.

Source

Chinese Hamster Ovary Cells.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Each mg of lyophilized powder contains 1x PBS pH-7.4.

Solubility

It is recommended to reconstitute the lyophilized Erythropoietin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Erythropoietin-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPO-alpha should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 10⁵ IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPO a Human

Description

Catalogue number

CYT-201

Synonyms

Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.

Introduction

Description

Erythropoietin-alpha Human Recombinant is produced in Chinese hamster ovary cells by recombinant DNA technology is a single, polypeptide chain containing 166 amino acids and having a predicted molecular mass of 21,000 Dalton and apparent glycosylated molecular mass of 36-40kDa. EPO-a is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Each mg of lyophilized powder contains 0.59 mg sodium citrate, 0.58 mg sodium chloride and 0.006 mg citric acid.

Solubility

It is recommended to reconstitute the lyophilized EPO-alpha in sterile 18MΩ-cm H₂O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Purity

Greater than 98.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDR.

Biological Activity

The Specific Activity was measured by Normocyth -aemic mice and was found to be 150,000 IU/mg.

References

1.Title:Zinc Transporters ZnT1 , Zip8 , and Zip10 in Mouse Red Blood Cells Are Differentially Regulated during Erythroid Development and by Dietary Zinc Deficiency^1–3
Publication:Journal of Nutrition, doi:10.3945/jn.108.093575
Vol. 138, No. 11, 2076-2083, November 2008
© 2008 American Society for Nutrition J. Nutr. 138:2076-2083, November 2008
Link:http://jn.nutrition.org/content/138/11/2076.full

2.Title:Systemically delivered Erythropoietin transiently enhances adult hippocampal neurogenesis.
Publication:Article first published online: 7 MAY 2007 DOI:10.1111/j.1471-4159.2007.04684.x Journal of Neurochemistry Volume 102, Issue 6, pages 1953–1965, September 2007.
Link:http://onlinelibrary.wiley.com/doi/10.1111/j.1471-4159.2007.04684.x/full

3.Title:ZINC TRANSPORTER EXPRESSION IN MATURE RED BLOOD CELLS AND
DIFFERENTIATING ERYTHROID PROGENITOR CELLS.
Publication:UNIVERSITY OF FLORIDA
© 2007 Moon-Suhn Ryu
Link:http://ufdcimages.uflib.ufl.edu/UF/E0/02/14/46/00001/ryu_m.pdf

4.Title:Cell Therapy with Human Renal Cell Cultures Containing Erythropoietin-Positive Cells Improves Chronic Kidney Injury.
Publication:First Published Online May 3, 2012 doi: 10.5966/sctm.2011-0048 Stem Cells Trans Med May 2012 vol. 1 no. 5 373-383
Link:http://stemcellstm.alphamedpress.org/content/1/5/373.full

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPO a Human, HEK

Description

Catalogue number

CYT-083

Synonyms

Erythropoietin-Alpha, EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

Introduction

Description

EPO-a Human Recombinant produced in HEK cells is a glycosylated monomer, having a total molecular weight of 36kDa.
The EPO-alpha is purified by proprietary chromatographic techniques.

Source

HEK.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The EPO-alpha was lyophilized from 1mg/ml in 1xPBS.

Solubility

It is recommended to reconstitute the lyophilized EPO-alpha in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized EPO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPO-alpha should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95% as obsereved by -PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells and is typically 0.5-2.5ng/ml, corresponding to a specific activity of 400,000-2,000,000 units/mg.

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPO a Human, His

Description

Catalogue number

CYT-791

Synonyms

Erythropoietin, EP, INN=Epoetin, EPO a, Erythropoietin-alpha, EPO.

Introduction

EPO a is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. EPO a is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. EPO a also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

Description

EPO a Human Recombinant produced in Baculovirus is a single, glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of 19.5kDa.
EPO a is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile Filtered clear solution.

Formulation

EPO a protein solution contains Phosphate-Buffered Saline and 10% glycerol.

Stability

Purity

Greater than 95% as determined by -PAGE.

Amino acid sequence

APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

Biological Activity

The ED50 range is ≤0.5ng/ml and measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPO a Human, Sf9

Description

Catalogue number

CYT-934

Synonyms

Erythropoietin, Epoetin, MVCD2, EP, Erythropoietin-Alpha, EPO-a, EPO-alpha.

Introduction

Description

Erythropoietin-alpha Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of 19.5kDa .
EPO-a is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

EPO a protein solution contains phosphate buffered saline and 10% glycerol.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED₅₀ for this effect is ≤ 0.5 ng/ml.

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPO Mouse

Description

Catalogue number

CYT-1171

Synonyms

Erythropoietin, erythropoietin isoform 1 precursor, Epo.

Introduction

Erythropoietin or EPO is a hormone , part of the type I cytokine group of proteins. EPO is found mainly in the kidney tissue, produced from fibroblast-like cortical interstitial cells near the proximal tubules. EPO is also present in the blood, where it acts as red cell production regulator, by the promotion of differentiation of erythroid and thereby starts hemoglobin synthesis. Furthermore, EPO has neuroprotective activity towards brain injuries & anti-apoptotic activity in different tissues.

Description

EPO Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa.
EPO is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

EPO Mouse protein contains 10% glycerol and Phosphate-Buffered Saline .

Stability

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

Amino acid sequence

ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPO Rat

Description

Catalogue number

CYT-1187

Synonyms

Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.

Introduction

Description

EPO Rat Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 19.6 kDa. EPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

EPO protein contains Phosphate-Buffered Saline and 10% glycerol.

Stability

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

Amino acid sequence

DGSAPPRLIC DSRVLERYIL EAKEAENVTM GCAEGPRLSE NITVPDTKVN FYAWKRMKVE EQAVEVWQGL SLLSEAILQA QALQANSSQP PESLQLHIDK AISGLRSLTS LLRVLGAQKE LMSPPDATQA APLRTLTADT FCKLFRVYSN FLRGKLKLYT GEACRRGDRH HHHHH.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPOR Human

Description

Catalogue number

CYT-929

Synonyms

Erythropoietin Receptor, EPO-R, EPOR.

Introduction

Erythropoietin receptor, also known as EPOR arbitrates erythropoietin-induced erythroblast proliferation as well as differentiation. During EPO binding, EPOR activates Jak2 tyrosine kinase which activates various intracellular pathways including: Ras/MAP kinase, phosphatidylinositol 3-kinase and STAT transcription factors. Furthermore, stimulated EPOR has a function in erythroid cell survival. Mutations in EPOR may possibly produce erythroleukemia and familial erythrocytosis. In addition, dysregulation of EPOR can affect on the growth of selected tumors.

Description

EPOR Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids and having a molecular mass of 25.6kDa. . EPOR is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile Filtered clear solution.

Formulation

EPOR protein solution containing Phosphate Buffered Saline and 10% glycerol.

Stability

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.

Usage

ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-EPOR Human, Active

Description

Catalogue number

CYT-997

Synonyms

EPO-R, EPOR, Erythropoietin Receptor.

Introduction

Description

EPOR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids and having a molecular mass of 25.6kDa .
EPOR is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile Filtered clear solution.

Formulation

EPOR protein solution contains Phosphate Buffered Saline and 10% glycerol.

Stability

Purity

Greater than 95.0% as determined by analysis by -PAGE.

Biological Activity

Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.

Amino acid sequence

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-aFGF Bovine

Description

Catalogue number

CYT-613

Synonyms

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Introduction

Acidic fibroblast growth factor is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

Description

Fibroblast Growth Factor-acidic Bovine purified from Bovine Brain contains a 17 kDa and a 20 kDa polypeptide chain. The 17 kDa peptide is derived from the 20K peptide by restricted proteolysis. . The FGF acidic is purified by proprietary chromatographic techniques.

Source

Bovine Brain.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Each 5µg aFGF were lyophilized from 0.5ml solution containing 1mM sodium phosphate, pH 7 after filtration over a low binding membrane.

Solubility

It is recommended to reconstitute the lyophilized aFGF in sterile 50mM Na2HPO4 pH-7, and 0.5% albumin. The Recommended concentration in cell culture: 1-20ng/ml.

Stability

Lyophilized aFGF although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution aFGF should be stored at 4°C between 2-3 weeks and for future use below -18°C.
Please prevent freeze-thaw cycles.

Purity

Greater than 90%.

Biological Activity

Stimulates growth of bovine capillary endothelial cells by 3-5 fold over 5% calf serum at 10-25ng/ml FGF.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 1 Human

Description

Catalogue number

CYT-264

Synonyms

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Introduction

Acidic fibroblast growth factor is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis.
Three alternatively spliced variants encoding different isoforms have been described.
The hep-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

Description

Fibroblast Growth Factor-acidic Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of approximately 15.8kDa.
The FGF acidic is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated sterile solution containing PBS, pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-acidic in sterile 18MΩ-cm H2O at 4 degrees Celsius at a concentration of 0.1mg-0.25mg per 1ml. Allow sample to sit for 5 min. at 4 degrees, spin to remove precipitant.

Stability

Lyophilized Fibroblast Growth Factor-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-a should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles.

Purity

Greater than 95.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

MFNLPPGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SVGEVYIKST ETGQYLAMDT DGLLYGSQTP NEECLFLERL EENHYNTYIS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

Biological Activity

The ED₅₀, calculated by the dose-dependant proliferation of mouse BALB/c 3T3 cells is <0.5 ng/ml, corresponding to a specific activity of > 2,000,000IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 1 Human, Sf9

Description

Catalogue number

CYT-364

Synonyms

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Introduction

Acidic fibroblast growth factor is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

Description

Fibroblast Growth Factor-1 Human Recombinant produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of 15803 Dalton.
The FGF-a is purified by proprietary chromatographic techniques.

Source

Baculovirus.

Physical Appearance

Sterile Filtered liquid formulation.

Formulation

The sterile protein solution contains 20mM Tris HCl pH=7.9, 100mM KCl, 0.2mM DTT and 20% glycerol.

Stability

Purity

Greater than 95.0% as determined by Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

The sequence of the first five N-terminal amino acids as determined and was found to be Met-Phe-Asn-Leu-Pro.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors is <10 ng/ml, corresponding to a specific activity of 100,000IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 1 Mouse

Description

Catalogue number

CYT-528

Synonyms

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Introduction

Description

Fibroblast Growth Factor-acidic Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids and having a molecular mass of 15.9kDa.

The FGF acidic is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.5.

Solubility

It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-acidic in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5×10⁶IU/mg.

References

Title: Differentiation of human embryonic stem cells into bipotent mesenchymal stem cells
Publications: Stem cells 24.8 : 1914-1922.
Link: http://onlinelibrary.wiley.com/doi/10.1634/stemcells.2005-0648/epdf

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 1 Mouse, His

Description

Catalogue number

CYT-072

Synonyms

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Introduction

Acidic fibroblast growth factor is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

Description

FGF-1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 18kDa .
FGF-1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered colorless clear solution.

Formulation

FGF-1 protein solution containing 20mM Tris-HCl buffer , 1mM DTT, 30% glycerol and 0.1M NaCl.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs,agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 1 Rat

Description

Catalogue number

CYT-075

Synonyms

Fibroblast growth factor 1, FGF-1, Acidic fibroblast growth factor, aFGF, binding growth factor 1, HBGF-1, Fgf1, Fgfa, HBGF1.

Introduction

Description

Fibroblast Growth Factor-acidic Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids and having a molecular mass of 15.9 kDa.
The FGF acidic is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized at a concentration of 1 mg/ml in 5mM Na₂PO₄, pH-7.5 and 50mM NaCl.

Solubility

It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-acidic in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Purity

Greater than 98.0% as determined by -PAGE.

Amino acid sequence

MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

Biological Activity

The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5×10⁶IU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 15 Mouse

Description

Catalogue number

CYT-027

Synonyms

Fibroblast Growth Factor 15, FGF19.

Introduction

FGF-15 takes part in the suppression of bile acid biosynthesis by down-regulation of CYP7A1 expression. FGF-15 is expressed in the developing brain.

Description

FGF-15 Protein is 23.78 kDa protein containing 203 amino acid residues including a 10 a.a. N-Terminal His-tag.

Source

E. coli

Physical Appearance

Filtered colorless solution.

Formulation

The FGF-15 filtered solution in 20mM TRIS and 50mM NaCl, pH 8.5.

Stability

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

MKHHHHHHAS RPLAQQSQSV SDEDPLFLYG WGKITRLQYL YSAGPYVSNC FLRIRSDGSV DCEEDQNERN LLEFRAVALK TIAIKDVSSV RYLCMSADGK IYGLIRYSEE DCTFREEMDC LGYNQYRSMK HHLHIIFIQA KPREQLQDQK PSNFIPVFHR SFFETGDQLR SKMFSLPLES DSMDPFRMVE DVDHLVKSPS FQK.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 18 Human

Description

Catalogue number

CYT-120

Synonyms

Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.

Introduction

Fibroblast growth factor 18 is a member of the large FGF family which has at least 23 members. FGF18 is a binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.

Description

FGF-18 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 21.1kDa. The FGF-18 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

FGF-18 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized FGF-18 in sterile 18MΩ-cm H₂O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized FGF-18 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-18 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

AEENVDFRIH VENQTRARDD VSRKQLRLYQ LYSRTSGKHI QVLGRRISAR GEDGDKYAQL LVETDTFGSQ VRIKGKETEF YLCMNRKGKL VGKPDGTSKE CVFIEKVLEN NYTALMSAKY SGWYVGFTKK GRPRKGPKTR ENQQDVHFMK RYPKGQPELQ KPFKYTTVTK RSRRIRPTHP A.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×10⁶ units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 18 Human, His

Description

Catalogue number

CYT-935

Synonyms

Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.

Introduction

Description

FGF18 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 22.3kDa.

Source

Escherichia Coli.

Physical Appearance

Filtered White lyophilized powder.

Formulation

FGF18 was filtered and lyophilized in phosphate buffered saline and 5% w/v trehalose.

Solubility

It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. FGF18 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

Stability

Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

Amino acid sequence

MKHHHHHHASEENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQPELQK PFKYTTVTKR SRRIRPTHPA.

Purity

Purity as determined by densitometric image analysis is greater than 95%.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 18 Mouse

Description

Catalogue number

CYT-064

Synonyms

Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

Introduction

Fibroblast growth factor 18 is a member of the large FGF family which has at least 23 members. FGF18 is a heparin binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.

Description

FGF-18 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 21kDa.
The FGF-18 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

FGF-18 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized FGF-18 in sterile 18M-cm H₂O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Purity

Greater than 95.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×10⁶ units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 19 Human

Description

Catalogue number

CYT-700

Synonyms

Fibroblast growth factor 19, FGF-19, FGF19.

Introduction

The FGFs are a family of more than 20 small secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors 1, 2, or 3. A fourth closely related tyrosine kinase receptor was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors : FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and INS desensitization and to improve INS, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

Description

FGF19 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 21.8 kDa.
The FGF-19 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Filtered white lyophilized powder.

Formulation

Filtered and lyophilized from 1mg/ml in 1xPBS, pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized FGF-19 in sterile 18M-cm H₂O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized FGF-19 Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-19 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Biological Activity

The ED50 as determined by the dose-dependent stimulation of the proliferation of balb/c 3T3 cells is 100-150ng/ml.

Purity

Greater than 95.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

MRPLAFSDAG PHVHYGWGDP IRLRHLYTSG PHGLSSCFLR IRADGVVDCA RGQSAHSLLE IKAVALRTVA IKGVHSVRYL CMGADGKMQG LLQYSEEDCA FEEEIRPDGY NVYRSEKHRL PVSLSSAKQR QLYKNRGFLP LSHFLPMLPM VPEEPEDLRG HLESDMFSSP LETDSMDPFG LVTGLEAVRS PSFEK.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs,agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 19 Human, His

Description

Catalogue number

CYT-279

Synonyms

Fibroblast growth factor 19, FGF-19.

Introduction

The FGFs are a family of more than 20 small secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors 1, 2, or 3. A fourth closely related tyrosine kinase receptor was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors : FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and insulin desensitization and to improve insulin, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

Description

Fibroblast Growth Factor-19 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 206 amino acids and having a molecular mass of 23 kDa. The amino acid sequence of the recombinant human FGF19 is 100% homologous to the amino acid sequence of the human FGF19 without signal sequence and contains his tag at N-terminal. The FGF-19 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Filtered white lyophilized powder.

Formulation

Filtered and lyophilized from 0.5mg/ml in 20mM TRIS, 20mM NaCl, pH 7.5.

Solubility

Add deionized water to a working concentration approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.

Stability

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

MRGSHHHHHH GMASLAFSDA GPHVHYGWGD PIRLRHLYTS GPHGLSSCFL RIRADGVVDC ARGQSAHSLLEIKAVALRTV AIKGVHSVRY LCMGADGKMQ GLLQYSEEDC AFEEEIRPDG YNVYRSEKHR LPVSLSSAKQ RQLYKNRGFL PLSHFLPMLP MVPEEPEDLR GHLESDMFSS PLETDSMDPF GLVTGLEAVR SPSFEK.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs,agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 2 Bovine

Description

Catalogue number

CYT-560

Synonyms

HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b.

Introduction

FGF-basic is a member of the fibroblast growth factor family. FGF family members bind heparin and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from AUG and non-AUG initiation codons resulting in five different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.
The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. there are differences in the tissue distribution and concentration of these 2 growth factors.

Description

FGF-2 Bovine purified from bovine pituitary is a single, glycosylated, polypeptide chain having a molecular mass of 16kDa.
The basic-FGF is purified by proprietary chromatographic techniques.

Source

Bovine Pituitary.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The FGF-basic Bovine was lyophilized from a concentrated sterile solution containing 50mM Na2HPO4, pH-7.5 & 0.5% HSA.

Solubility

It is recommended to reconstitute the lyophilized FGF-2 Bovine in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized FGF2 Bovine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C.
Upon reconstitution FGF-b Bovine should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

The recommended concentration in responsive cells is 0.1 to 2ng/ml.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 2 Human

Description

Catalogue number

CYT-218

Synonyms

Prostatropin, FGF-basic, Basic FGF, HBGF-2, FGF-2, FGF-b.

Introduction

Basic fibroblast growth factor is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The HPR -binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

Description

Fibroblast Growth Factor-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.2kDa.
The FGF-b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution in 20mM Tris-HCl, pH7.4 and 1M NaCl.

Solubility

It is recommended to reconstitute the lyophilized Fibroblast Growth Factor Basic in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Fibroblast Growth Factor-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-b should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by Analysis by -PAGE.

Amino acid sequence

AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.

Biological Activity

The ED₅₀, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0×10⁷ Units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

References

1.Title:Activation of the Hedgehog pathway in pilocytic astrocytomas
Publication:Neuro Oncol 12 : 790-798. doi: 10.1093/neuonc/noq026 First published online: March 11, 2010
Link:http://neurooncology.oxfordjournals.org/content/12/8/790.full

2.Title:Phenotype reversion in fetal human liver epithelial cells identifies the role of an intermediate meso-endodermal stage before hepatic maturation
Publication:Advance Online Publication March 4, 2008 doi: 10.1242/?jcs.019315 April 1, 2008 J Cell Sci 121, 1002-1013.
Link:http://jcs.biologists.org/content/121/7/1002.full

3. Title:Embryonic Stem Cell-Derived Glial Precursors as a Vehicle for Sulfamidase Production in the MPS-IIIA Mouse Brain .
Publication:

Cell Transplantation

ISSN: 0963-6897

DOI: 10.3727/096368910X498944

Volume 19, Issue 8, pages 985-998

4.Title:Adult Human Dental Pulp Stem Cells Differentiate Toward Functionally Active Neurons Under Appropriate Environmental Cues.
Publication: Article first published online: 22 MAY 2008 DOI:10.1634/stemcells.2007-0979 Copyright © 2008 AlphaMed Press.
Link:http://onlinelibrary.wiley.com/doi/10.1634/stemcells.2007-0979/full

5.Title: Successful implantation of physiologically functional bioengineered mouse internal anal sphincter
Publication: American Journal of Physiology-Gastrointestinal and Liver Physiology 299.2 : G430-G439.
Link: http://ajpgi.physiology.org/content/299/2/G430

ProSpec-FGF 2 Human (147 a.a.)

Description

Catalogue number

CYT-557

Synonyms

Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

Introduction

FGF-basic is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

Description

Fibroblast Growth Factor-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16.5kDa.
The FGF2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The bFGF was lyophilized from a sterile filtered solution containing 20mM Tris-HCl, pH 7.6 and 150mM NaCl.

Solubility

It is recommended to reconstitute the lyophilized FGF-B in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized basic-FGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFb should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by -PAGE.

Amino acid sequence

MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.

Biological Activity

The ED₅₀, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0×10⁷ units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 2 Human, Plant

Description

Catalogue number

CYT-123

Synonyms

Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b, Fibroblast growth factor 2, Basic fibroblast growth factor, Heparin-binding growth factor 2.

Introduction

Basic fibroblast growth factor is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

Description

FGF-2 Human Recombinant produced in rice is a single, non-glycosylated polypeptide chain containing 146 amino acids and having a molecular mass of ~17kDa.
The FGF-b protein is purified by proprietary chromatographic techniques.

Source

Rice Grain .

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

FGF-b was lyophilized from a concentrated solution without any additives.

Solubility

It is recommended to reconstitute the lyophilized Fibroblast Growth Factor Basic in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Purity

Greater than 95.0% as determined by -PAGE.

Biological Activity

The ED₅₀, as calculated by the dose-dependent proliferation of Balb/c 3T3 cells expressing FGF receptors is <1 ng/ml, corresponding to a specific activity of >1 x10⁶ Units/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 2 Human, sf9

Description

Catalogue number

CYT-365

Synonyms

Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

Introduction

Basic fibroblast growth factor is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

Description

Fibroblast Growth Factor-2 Human Recombinant produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17353 Dalton.
The FGF-basic is purified by proprietary chromatographic techniques.

Source

Baculovirus.

Physical Appearance

Sterile Filtered liquid formulation.

Formulation

The sterile protein solution contains 20mM Tris pH=7.9, 100mM KCl, 1mM DTT and 20% glycerol.

Stability

Purity

Greater than 98.0% as determined by Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ala-Gly-Ser-Ile.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 2 Mouse

Description

Catalogue number

CYT-386

Synonyms

HBGF-2, Prostatropin, FGF-2, FGB-b.

Introduction

FGF-basic is a member of the fibroblast growth factor family. FGF family members bind and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from AUG and non-AUG initiation codons resulting in five different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.
The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. there are differences in the tissue distribution and concentration of these 2 growth factors.

Description

Fibroblast Growth Factor-basic Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.3kDa. The FGF-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

FGF-b was lyophilized from 5mM Na₂PO₄, pH7.5 and 50mM NaCl.

Solubility

It is recommended to reconstitute the lyophilized Fibroblast Growth Factor b in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Fibroblast Growth Factor-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-basic should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

MPALPEDGGA AFPPGHFKDP KRLYCKNGGF FLRIHPDGRV DGVREKSDPH VKLQLQAEER GVVSIKGVCA NRYLAMKEDG RLLASKCVTE ECFFFERLES NNYNTYRSRK YSSWYVALKR TGQYKLGSKT GPGQKAILFL PMSAKS.

Biological Activity

The activity as calculated by the dose-dependant proliferation of BALB/3T3 cells was found to be less than 1ng/ml corresponding to a specific activity of 1,000,000 units/mg.

Protein content

Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 0.885 as the extinction coefficient for a 0.1% solution. This value is calculated by the PC GENE computer analysis program of protein sequences .
2. Analysis by RP-HPLC, using a calibrated solution of FGF2 as a Reference Standard.

References

1. Title: Fibroblast Growth Factor-2 Autofeedback Regulation in Pituitary Folliculostellate TtT/GF Cells
Publication: Endocrinology 150.7 : 3252-3258.
Link: http://press.endocrine.org/doi/full/10.1210/en.2008-1625

2. Title: The Mouse Cornea as a Transplantation Site for Live Imaging of Engineered Tissue Constructs
Publication: Cold Spring Harbor Protocols 2010.4 : pdb-prot5416.
Link: http://cshprotocols.cshlp.org/content/2010/4/pdb.prot5416.full

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 2 Rat

Description

Catalogue number

CYT-608

Synonyms

HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b, Fibroblast Growth Factor-basic, Basic fibroblast growth factor, bFGF, Heparin-binding growth factor 2.

Introduction

Description

bFGF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.4 kDa.
The bFGF2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

FGF-b was lyophilized from 1mg/ml solution after extensive dialysis against 10mM Na₂PO₄, pH 7.5 and 50mM NaCl.

Solubility

It is recommended to reconstitute the lyophilized Rat bFGF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Rat bFGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat FGF-2 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 97.0% as determined by -PAGE.

Amino acid sequence

MPALPEDGGGA FPPGHFKDPK RLYCKNGGFF LRIHPDGRVD GVREKSDPHV KLQLQAEERG VVSIKGVCAN RYLAMKEDGR LLASKCVTEE CFFFERLESN NYNTYRSRKY SSWYVALKRT GQYKLGSKTG PGQKAILFLP MSAKS.

Biological Activity

The ED₅₀ range as determined by the dose-dependant proliferation of 3T3 cells was found to be less than 0.13-0.2ng/ml.

Usage

ProSpec’s products are furnished form LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 21 Bovine

Description

Catalogue number

CYT-657

Synonyms

Fibroblast growth factor 21, FGF-21, FGF21.

Introduction

The FGFs are a family of more than 20 small secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors 1, 2, or 3. A fourth closely related tyrosine kinase receptor was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors : FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and desensitization and to improve, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

Description

Fibroblast Growth Factor -21 Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids, having a molecular weight of 19.5 kDa.
The FGF-21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered white lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.4 mg/ml of NaHCO3, pH 8.

Solubility

It is recommended to reconstitute the lyophilized Bovine FGF-21 in sterile water or 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.

Stability

Lyophilized FGF-21 Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 21 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by:
Analysis by Gel Filtration.
Analysis by -PAGE.

Amino acid sequence

The sequence of the first five N-terminal amino acids was determined and was found to be Ala-His-Pro-Ile-Pro.

Protein content

Bovine FGF-21 quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.47 as the extinction coefficient for a 0.1% solution. This value is calculated by the PC GENE computer analysis program of protein sequences .
2. Analysis by RP-HPLC, using a standard solution of FGF-21 Recombinant as a Reference Standard.

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs,agricultural or pesticidal products, food additives or household chemicals.

ProSpec-FGF 21 Human

Description

Catalogue number

CYT-474

Synonyms

Fibroblast growth factor 21, FGF-21.

Introduction

The FGFs are a family of more than 20 small secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors 1, 2, or 3. A fourth closely related tyrosine kinase receptor was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors : FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and desensitization and to improve glucose and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

Description

Fibroblast Growth Factor -21 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids, having a molecular weight of 19.4 kDa.

The FGF-21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered white lyophilized powder.

Formulation

Lyophilized from PBS, pH 7.4.

Solubility

It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-21 Human Recombinant sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized FGF-21 Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 21 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.

Purity

Greater than 96.0% as determined by:
Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

HPIPDS SPLLQFGGQV RQRYLYTDDA QQTEAHLEIR EDGTVGGAAD QSPESLLQLK ALKPGVIQIL GVKTSRFLCQ RPDGALYGSL HFDPEACSFR ELLLEDGYNV YQSEAHGLPL HLPGNKSPHR DPAPRGPARF LPLPGLPPAP PEPPGILAPQ PPDVGSSDPL SMVGPSQGRS PSYAS.

Biological Activity

The ED₅₀ as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 μg/ml, corresponding to a specific activity of > 2.0 × 10³ IU/mg in the presence of 5µg/ml of rMuKlotho-β and 10µg/ml of heparin.

References

Title: Fibroblast Growth Factor 21 Action in the Brain Increases Energy Expenditure and Sensitivity in Obese Rats
Publication: Diabetes 59.7 : 1817-1824.
Link: http://diabetes.diabetesjournals.org/content/59/7/1817.full

Usage

ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

EGF Human

Catalogue number

Synonyms

Introduction

Description

Source

Physical Appearance

Formulation

Solubility

Stability

Purity

Amino acid sequence

Biological Activity

Usage

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