分类： 生长因子growth factors

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.

GH-dependant binding protein, IBP3, BP-53, IGFBP-3.

IGFBP3 is a member of the IGFBP family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with IGFALS and either IGF I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

IGFBP3 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids and having a molecular mass of 28806 Dalton.
IGFBP-3 is purified by proprietary chromatographic techniques.

It is recommended to reconstitute the lyophilized IGFBP3 in sterile 20mM AcOH not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

GASSAGLGPVVRCEPCDARALAQCAPPPAVCAELVREPGCGCCLTCALSEGQPCGIYTERCGSGL

RCQPSPDEARPLQALLDGRGLCVNASAVSRLRAYLLPAPPAPGNASESEEDRSAGSVESPSVSST

HRVSDPKFHPLHSKIIIIKKGHAKDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLN

HLKFLNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYTTKGKEDVHCYSMQSK

The ED_50, calculated by by its ability to inhibit IGF-II induced proliferation of MCF-7 is < 200ng/ml in the presence of 15ng/ml of Human IGF-II, corresponding to a specific activity of 5.0 × 10³ IU/mg.

Title:The role of IGFBP3 in the growth inhibitory actions of androgens in LNCaP human prostate cancer cells.
Publication:Article first published online: 4 OCT 2007 DOI:10.1002/ijc.23100 Copyright © 2007 Wiley-Liss, Inc.
Link:http://onlinelibrary.wiley.com/doi/10.1002/ijc.23100/full

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.

Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

Fibroblast Growth Factor 17 is a part of the fibroblast growth factor family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes includingmorphogenesis, embryonic development cell growth, , tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a part in central nervous system, bone and vascular development.

Fibroblast Growth Factor 17 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acid and having a molecular mass of approximately 22.5kDa.
FGF17 is purified by proprietary chromatographic techniques.

Escherichia Coli.

Sterile Filtered White lyophilized powder.

Lyophilized from a 0.2μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0,   0.02 % Tween-20 and 700 mM NaCl.

It is recommended to reconstitute the lyophilized Fibroblast Growth Factor 17 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Lyophilized FGF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 17 should be stored at 4°C between 2-7 days and for future use below -18°C.

Please prevent freeze-thaw cycles.

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

TQGENHPSPN FNQYVRDQGA MTDQLSRRQI REYQLYSRTS GKHVQVTGRR ISATAEDGNK FAKLIVETDT FGSRVRIKGA ESEKYICMNK RGKLIGKPSG KSKDCVFTEI VLENNYTAFQ NARHEGWFMA FTRQGRPRQA SRSRQNQREA HFIKRLYQGQ LPFPNHAERQ KQFEFVGSAP TRRTKRTRRP QSQT.

The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < 10 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg in the presence of 10 μg/ml of heparin.

The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed ‘sulfation factor,’ which later became known as somatomedin.  Three main somatomedins have been characterized: somatomedin C , somatomedin A , and somatomedin B.

IGF1 Gilthead SeabreamRecombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7545.4 Dalton, the predicted pI=7.72.
IGF-1 is purified by proprietary chromatographic techniques.

It is recommended to reconstitute the lyophilized IGF-1 in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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.

MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK

The somatomedins, or insulin-like growth factors , comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone . Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed ‘sulfation factor,’ which later became known as ‘somatomedin’ . 3 main somatomedins have been characterized: somatomedin C , somatomedin A , and somatomedin B .

IGF1 A67T Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7 kDa.

The IGF1 A67T is purified by proprietary chromatographic techniques.

IGF1 A67T Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM PB and 150 mM NaCl, pH 6.0.

It is recommended to reconstitute the lyophilized IGF1 A67T in sterile 18MΩ-cm H₂O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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.

Greater than 95.0% as determined by -PAGE.

GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPTKSA.

The somatomedins, or insulin-like growth factors , comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone . Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed ‘sulfation factor,’ which later became known as ‘somatomedin’ . 3 main somatomedins have been characterized: somatomedin C , somatomedin A , and somatomedin B .

IGF1 A70T Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7kDa.

The IGF1 A70T is purified by proprietary chromatographic techniques.

IGF1 A70T Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM PB and 150 mM NaCl, pH 6.0.

It is recommended to reconstitute the lyophilized IGF1 A70T in sterile 18MΩ-cm H₂O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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.

Greater than 95.0% as determined by -PAGE.

GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKST.

The somatomedins, or insulin-like growth factors , comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone . Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed ‘sulfation factor,’ which later became known as ‘somatomedin’ . 3 main somatomedins have been characterized: somatomedin C , somatomedin A , and somatomedin B .

IGF1 R36Q Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7kDa.

The IGF1 R36Q is purified by proprietary chromatographic techniques.

IGF1 R36Q Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM PB and 150 mM NaCl, pH 5.4.

It is recommended to reconstitute the lyophilized IGF1 R36Q in sterile 18MΩ-cm H₂O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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.

Greater than 95.0% as determined by -PAGE.

GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSQRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

The somatomedins, or insulin-like growth factors , comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone . Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed ‘sulfation factor,’ which later became known as ‘somatomedin’ . 3 main somatomedins have been characterized: somatomedin C , somatomedin A , and somatomedin B .

IGF1 V44M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7 kDa.

The IGF1 V44M is purified by proprietary chromatographic techniques.

IGF1 V44M Lyophilized from a 0.2 µm filtered concentrated solution in PBS.

It is recommended to reconstitute the lyophilized IGF1 V44M in sterile 18MΩ-cm H₂O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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.

Greater than 95.0% as determined by -PAGE.

GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIMDECCFR SCDLRRLEMY.

IGF1 N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.74kDa. The N¹⁵ is stable isotope labeled.

The IGF1 N15 is purified by proprietary chromatographic techniques.

It is recommended to reconstitute the lyophilized rbIGF-I in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed ‘sulfation factor,’ which later became known as ‘somatomedin’ . Three main somatomedins have been characterized: somatomedin C , somatomedin A , and somatomedin B .

IGF-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.7kDa.
IGF-I is purified by proprietary chromatographic techniques.

IGF-2 is a member of the INS family of polypeptide growth factors that is involved in development and growth. It is an imprinted gene and is expressed only from the paternally inherited allele. It is a candidate gene for eating disorders. There is a read-through, INS-IGF2, which aligns to this gene at the 3′ region and to the upstream INS gene at the 5′ region. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.

Insulin-Like Growth Factor- II Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids and having a molecular mass of 7.5k Dalton.                  

IGF-II is purified by proprietary chromatographic techniques.

The protein was lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid .

Greater than 95.0% as determined by -PAGE.

The activity is determined by the dose dependent proliferation of FDC-P1 cells and is typically 1.4 ng/mL corresponding to a specific activity of 7.1×10⁵units/mg.

Title: Sub-Cellular Localisation Studies May Spuriously Detect the Yes-Associated Protein, YAP
Publications:  Nucleoli Leading to Potentially Invalid Conclusions of Its Function. PLoS ONE 10.2 : e0114813.
Link: http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0114813

Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.2.

Greater than 97.0% as determined by -PAGE and HPLC.

Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN. 

Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.
ProInsulin is purified by proprietary chromatographic techniques.

Escherichia Coli.

Sterile Filtered White lyophilized powder.

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.

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

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

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

RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR. 

It is recommended to reconstitute the lyophilized Leptin-Antagonist Triple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

2. Analysis by RP-HPLC,using calibrated solution of Leptin Bovine as a Reference Standard.

2. Analysis by RP-HPLC,using calibrated solution of Leptin Chicken as a Reference Standard.

It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO₃ adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences .

2. Analysis by RP-HPLC,using calibrated solution of Leptin Horse as a Reference Standard.

Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.

Leptin N82K Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16kDa.

The Leptin N82K is purified by proprietary chromatographic techniques.

Lyophilized from a concentrated solution with 0.0045mM NaHCO₃.

It is recommended to reconstitute the lyophilized leptin N82K in sterile water or 0.4% NaHCO₃ adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Lyophilized leptin N82K although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K 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.

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

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

Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 as the extinction coefficient for a 0.1% solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences . 

Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.

Pegylated Leptin N82K Human Recombinant produced in E.Coli is  a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the -PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.

Lyophilized from a concentrated solution with 0.003mM NaHCO3 Having 35-40% protein.

It is recommended to reconstitute the lyophilized Pegylated Leptin N82K in sterile water or 0.4% NaHCO₃ adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Lyophilized Pegylated Leptin N82K although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K 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.

Greater than 99.0% as determined by:
 Gel filtration analysis.
Analysis by -PAGE.

Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. This abolishment of activity results from drastically reduced affinity toward leptin receptor.

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.870 as the extinction coefficient for a 0.1% protein solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences .  

Leptin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16 kDa. The Leptin is purified by proprietary chromatographic techniques. 

The mouse Leptin was lyophilized from a concentrated solution containing 0.0045mM NaHCO₃.

Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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.

Greater than 95.0% as determined by:
Analysis by gel filtration analysis.
Analysis by -PAGE.

AVPIQKVQDD TKTLIKTIVT RINDISHTQS VSAKQRVTGL DFIPGLHPIL SLSKMDQTLA VYQQVLTSLP SQNVLQIAND LENLRDLLHL LAFSKSCSLP QTSGLQKPES LDGVLEASLY STEVVALSRL QGSLQDILQQ LDVSPEC.

Biological activity of Mouse Leptin is performed by including proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% solution at pH-8.0. This value is calculated by the PC GENE computer analysis program of protein sequences .