ProSpec-Leptin Mouse, PEG

Description

Catalogue number

CYT-591

Synonyms

OB Protein, Obesity Protein, OBS, Obesity factor.

Introduction

A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

Description

Leptin Mono-Pegylated Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus. Pegylated Mouse Leptin contains PEG 20 kDa at its N-terminus and having a molecular mass of 35.6 kDa as determined by mass spectrometry.
Since its enlarged hydrodymanic volume Pegylated Leptin runs on -PAGE as A 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein.
Pegylated Mouse Leptin half-life in circulation after SC injection was over 20 hours. Mouse Leptin was purified by proprietary chromatographic techniques according to Salomon et al Protein Expression and Purification 47, 128–136 and then pegylated.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The mouse Leptin was lyophilized from a concentrated solution containing 0.003mM NaHCO3.

Solubility

It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO3 adjusted to pH-8.5 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

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.

Purity

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

Biological Activity

Pegylated mouse Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated mouse Leptin in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect , resulting mainly from reduced food intake.

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-Leptin Ovine

Description

Catalogue number

CYT-239

Synonyms

OB Protein, Obesity Protein, OBS, Obesity factor.

Introduction

Description

Leptin Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.
The Leptin 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 0.0045mM NaHCO3.

Solubility

It is recommended to reconstitute the lyophilized Leptin 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:
Analysis by SEC-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-Val-Pro-Ile-Arg.

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Protein content

Protein quantitation was carried out by two independent methods
1. UV spectroscopy at 280 nm using the absorbency value of 0.2 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 calibrated solution of Leptin Ovine as a Reference Standard.

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-Leptin Ovine, MTS

Description

Catalogue number

CYT-531

Synonyms

OB Protein, Obesity Protein, OBS, Obesity factor.

Introduction

Description

Leptin Ovine MTS tagged Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.5 kDa.
The Leptin is purified by proprietary chromatographic techniques. The membrane translocating sequence Tag is composed of 10 amino acids Val-Leu-Leu-Pro-Val-Leu-Leu-Ala-Ala-Pro located at the N-terminus.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.02% NaHCO3.

Solubility

It is recommended to reconstitute the lyophilized Leptin in sterile 0.02% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Leptin Ovine MTS tagged 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.

Purity

Greater than 98.0% as determined by:
Analysis by SEC-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-Val-Pro-Ile-Arg.

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Protein content

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-Leptin Porcine

Description

Catalogue number

CYT-503

Synonyms

OB Protein, Obesity Protein, OBS, Obesity factor.

Introduction

Description

Leptin Porcine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and additional Ala at N-terminus, having a molecular mass of 16kDa.
The Leptin 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 0.02% NaHCO₃.

Solubility

It is recommended to reconstitute the lyophilized recombinant porcine 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.

Stability

Purity

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

Amino acid sequence

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

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Protein content

Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 0.57 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 calibrated solution of Leptin Porcine as a Reference Standard.

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-Leptin Protein

Description

Catalogue number

CYT-228

Synonyms

OB Protein, Obesity Protein, OBS, Obesity factor.

Introduction

Description

Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.
The Leptin 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 0.0045mM NaHCO3.

Solubility

The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.

Stability

Lyophilized Leptin although stable at room temperature, should be stored desiccated below 0°C. Reconstituted Leptin is best stored refrigerated at 4°C.

Purity

Greater than 95.0% as determined by:
Analysis by SEC-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-Val-Pro-Ile-Gln.

Biological Activity

Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Protein content

Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 0.878 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 Leptin as a Reference Standard.

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:Leptin and Amylin Act in an Additive Manner to Activate Overlapping Signaling Pathways in Peripheral Tissues In vitro and ex vivo studies in humans.
Publication:Published online before print September 24, 2010, doi: 10.2337/dc10-0518 Diabetes Care January 2011 vol. 34 no. 1 132-138 .
Link:http://care.diabetesjournals.org/content/34/1/132.full

2.Title:The Mammalian Target of Rapamycin as Novel Central Regulator of Puberty Onset via Modulation of Hypothalamic Kiss1 System.
Publication: Published online before print September 4, 2009, doi: 10.1210/en.2009-0096 Endocrinology November 1, 2009 vol. 150 no. 11 5016-5026
Link:http://endo.endojournals.org/content/150/11/5016.full

3.Title:p38 Mitogen-Activated Protein Kinase and Liver X Receptor-? Mediate the Leptin Effect on Sterol Regulatory Element Binding Protein-1c Expression in Hepatic Stellate Cells.
Publication:Mol Med. 2012; 18: 10–18.

Published online 2011 October 3. doi: 10.2119/molmed.2011.00243
Link:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3269638/

4. Title: PI3K integrates the effects of and leptin on large-conductance Ca2+-activated K+ channels in neuropeptide Y neurons of the hypothalamic arcuate nucleus

Publication: American Journal of Physiology-Endocrinology and Metabolism 298.2 : E193-E201.
Link: http://ajpendo.physiology.org/content/298/2/E193.shorty

ProSpec-Leptin Pufferfish

Description

Catalogue number

CYT-530

Synonyms

OB Protein, Obesity Protein, OBS, Obesity factor.

Introduction

Description

Leptin Pufferfish Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa.
Bioactive Leptin Pufferfish Recombinant was prepared according to the sequence published by Kurokawa et al. Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al , General and Comparative Endocrinology.
The Pufferfish Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The Pufferfish Leptin was lyophilized from a concentrated solution with 0.003mM NaHCO3.

Solubility

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

Stability

Lyophilized Pufferfish 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.

Purity

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

Amino acid sequence

ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE

GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE

QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC

Protein content

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 as the extinction coefficient for a 0.1% solution. This value is calculated by the PC GENE computer analysis program of protein sequences .

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.

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-Leptin qA Human

Description

Catalogue number

CYT-353

Description

Leptin Quadruple Mutant Human Recombinant is a single polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a Mw of 16 kDa, Human Leptin was mutated, resulting in L39A/D40A/F41A/I42A.
Leptin Antagonist Quadruple Mutant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Physical Appearance

White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.0045mM NaHCO3.

Solubility

It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant 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.

Stability

Lyophilized Leptin Antagonist Quadruple Mutant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein is suggested. Please prevent freeze-thaw cycles.

Purity

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

Amino acid sequence

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

Biological Activity

ProSpec’s Leptin Quadruple Antagonist Mutant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.

Protein content

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.89 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 .

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-Leptin qA Ovine

Description

Catalogue number

CYT-357

Description

Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A/I42A mutant.
Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Physical Appearance

White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.0045mM NaHCO3.

Solubility

It is recommended to reconstitute the lyophilized Leptin-Antagonist Quadruple Mutant Ovine Recombinant 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.

Stability

Lyophilized Leptin-Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 LEP-qA mutant mg/ml and up to 2mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein is suggested.
Please prevent freeze-thaw cycles.

Purity

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

Amino acid sequence

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

Biological Activity

ProSpec’s leptin qA is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of ovine leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

Protein content

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 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 .

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-Leptin Rabbit

Description

Catalogue number

CYT-507

Synonyms

OB Protein, Obesity Protein, OBS, Obesity factor.

Introduction

Description

Leptin Rabbit Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.
The Leptin 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 0.02% NaHCO₃.

Solubility

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.

Stability

Purity

Greater than 98.0% as determined by:
Analysis by SEC-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-Val-Pro-Ile-Arg.

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Protein content

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.505 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 .

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-Leptin Rat

Description

Catalogue number

CYT-227

Synonyms

OB Protein, Obesity Protein, OBS, Obesity factor.

Introduction

Description

Leptin Rat 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.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.0045mM NaHCO3.

Solubility

It is recommended to reconstitute the lyophilized Leptin 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:
Analysis by SEC-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-Val-Pro-Ile-His.

Biological Activity

Biological activity of Leptin Rat is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Protein content

Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 0.201 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 Leptin rat as a Reference Standard.

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:Expression of Hypothalamic KiSS-1 System and Rescue of Defective Responses by Kisspeptin in Streptozotocin-Induced Diabetic Male Rats.
Publication: doi: 10.2337/db05-1584 Diabetes September 2006 vol. 55 no. 9 2602-2610
Link:http://diabetes.diabetesjournals.org/content/55/9/2602.full?patientinform-links=yes&legid=diabetes;55/9/2602

2.Title:Desensitization of responses to kisspeptin in the female rat: analyses of LH and FSH secretion at different developmental and metabolic states.
Publication:Am J Physiol Endocrinol Metab 294: E1088–E1096, 2008.294: E1088–E1096, 2008. First published April 15, 2008; doi:10.1152/ajpendo.90240.2008.
Link:http://ajpendo.physiology.org/content/294/6/E1088.full.pdf

3.Title:p38 MAPK and LXR? mediate leptin effect on SREBP-1c expression in hepatic stellate cells .
Publication:
Link:http://www.molmed.org/content/papers%20in%20press/11_243_Yan.pdf

4.Title:Neuroprotection by leptin in a rat model of permanent cerebral ischemia: effects on STAT3 phosphorylation in discrete cells of the brain.
Publication:Citation: Cell Death and Disease 2, e238; doi:10.1038/cddis.2011.125
Published online 8 December 2011.
Link:http://www.nature.com/cddis/journal/v2/n12/full/cddis2011125a.html

5.Title: The mammalian target of rapamycin as novel central regulator of puberty onset via modulation of hypothalamic Kiss1 system.
Publication: Endocrinology 150.11 : 5016-5026.
Link http://press.endocrine.org/doi/full/10.1210/en.2009-0096

ProSpec-Leptin Rat, PEG

Description

Catalogue number

CYT-592

Synonyms

OB Protein, Obesity Protein, OBS, Obesity factor.

Introduction

Description

Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa as determined by mass spectometry. However due to enlarged hydrodymanic volume it runs on the -PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al Protein Expression and Purification 47, 128–136 and then pegylated.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.003mM NaHCO3.

Solubility

It is recommended to reconstitute the lyophilized pegylated Rat Leptin in sterile 0.4% NaHCO3 adjusted to pH-8.5, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

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

Purity

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

Biological Activity

Pegylated Rat Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect , resulting mainly from reduced food intake.

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-Leptin Receptor Chicken

Description

Catalogue number

CYT-509

Synonyms

OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

Introduction

Leptin Receptor is a part of the gp130 family of cytokine receptors that stimulate gene transcription by activating cytosolic STAT proteins. Leptin Receptor plays a role in the regulation of fat metabolism and in novel hematopoietic pathway that is obligatory for normal lymphopoiesis. Leptin Receptorparticipates in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus.Leptin Receptoraffectsspecifically on T lymphocyte responses.

Description

Leptin Binding Domain Chicken Recombinant also called Leptin Receptor produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids and having a molecular mass of 24.5 kDa. Chicken Leptin Receptor consists of the cytokine binding domain of leptin receptor amino acids 420-626 of chicken leptin receptor.
The Leptin Binding Domain is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered colorless solution at a concentration of 0.4 mg/ml.

Formulation

The protein was filter sterilized and stored at 4°C solution of Tris-HCl buffer, pH 9.0 with 150mM NaCl.

Stability

Sterile solutions at 0.5mg/ml or less are stable at 4°C for several months.

Purity

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

Amino acid sequence

The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Ile-Asp-Val-Asn-Ile Biological ActivityBiological Activity is evidenced by high affinity binding of mammalian leptins at 1:1 molar ratio.

Protein content

Protein quantitation was carried out by two independent methods
1. UV spectroscopy at 280 nm using the absorbency value of 2.45 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 Leptin Binding Domain as a Reference Standard.

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-Leptin Salamander

Description

Catalogue number

CYT-704

Synonyms

OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.

Introduction

Description

Leptin Salamander Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of 16kDa. The Salamander Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The Salamander Leptin was lyophilized from a concentrated solution with 0.0045mM NaHCO3.

Solubility

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

Stability

Lyophilized Salamander 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.

Purity

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

Amino acid sequence

The sequence of the ten N-terminal amino acids was determined and was found to be Ala-Ile-Met-Val-Asp-Gln-Leu-Arg-Met-Asp.

Biological Activity

By inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity in that test is similar to that of mouse leptin Protein Expression and Purifcation 47, 128–136).

Protein content

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.104 as the extinction coefficient for a 0.1% solution. This value is calculated by the PC GENE computer analysis program of protein sequences .

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-Leptin tA Human

Description

Catalogue number

CYT-352

Description

Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Physical Appearance

White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.0045mM NaHCO3.

Solubility

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

Stability

Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein is suggested.
Please prevent freeze-thaw cycles.

Purity

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

Amino acid sequence

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

Biological Activity

ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

Protein content

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 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 .

References

Title: Leptin-induced vascular smooth muscle cell proliferation via regulating cell cycle, activating ERK1/2 and NF-kB
Publication: Acta biochimica et biophysica Sinica 42.5 : 325-331.
Link: http://abbs.oxfordjournals.org/content/42/5/325.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-Leptin tA Human, PEG

Description

Catalogue number

CYT-702

Description

Pegylated Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 35.6kDa, Leptin was mutated, resulting in L39A/D40A/F41A. 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. Leptin Antagonist Triple Mutant Human Recombinant is Mono-Pegylated with 20kDa PEG and was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Physical Appearance

White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.003mM NaHCO3.

Solubility

It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant pegylated Human Recombinant 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.

Stability

Lyophilized PEG-SHLA although stable at room temperature for several weeks, should be stored desiccated below – 20C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml of PEG-SHLA and filter sterilization mLEP mutant can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein is suggested.
Please prevent freeze-thaw cycles.

Purity

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

Biological Activity

Capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated antagonist but in vivo it has profound weight gain effect , resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.

Protein content

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-Leptin tA Mouse

Description

Catalogue number

CYT-354

Description

Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, LEP was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Physical Appearance

White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.003mM NaHCO3.

Solubility

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

Stability

Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein is suggested.
Please prevent freeze-thaw cycles.

Purity

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

Amino acid sequence

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

Biological Activity

ProSpec’s Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting Leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.

Protein content

Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 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 .

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-Leptin tA Mouse, PEG

Description

Catalogue number

CYT-566

Description

Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.
The Mouse Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.
The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa.
Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Physical Appearance

White lyophilized powder.

Formulation

The Mouse Leptin triple anatagonist was lyophilized from a concentrated solution with 0.003mM NaHCO3.

Solubility

Stability

Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein is suggested.
Please prevent freeze-thaw cycles.

Purity

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

Biological Activity

Leptin Antagonist Triple Mutant Mouse Recombinant half-life in circulation after SC injection was over 20 hours.
Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Mouse Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect , resulting mainly from increased food intake.

Protein content

Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 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 .

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-Leptin tA Ovine, PEG

Description

Catalogue number

CYT-703

Description

Pegylated Leptin Antagonist Triple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 aa and an additional Ala at N-terminus and having a molecular mass of ~ 35.6 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. However due to enlarged hydrodymanic volume it runs on the SGS-Page as 48 kDa protein and in gel-filtration on Superdex 200 as over 200kDa protein. Leptin Antagonist Triple Mutant Ovine Recombinant Mono-Pegylated with 20kDa PEG and was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Physical Appearance

White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.003mM NaHCO3.

Solubility

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.

Stability

Lyophilized Leptin Antagonist Triple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution at > 0.1 Lep-tA mutant mg/ml and up to 2mM and filter sterilization Leptin mutant can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein is suggested. Please prevent freeze-thaw cycles.

Purity

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

Biological Activity

Pegylated triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated antagonist but in vivo it has profound weight gain effect , resulting mainly from increased food intake.

Protein content

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 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 .

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-Leptin tA Rat

Description

Catalogue number

CYT-355

Description

Leptin Antagonist Triple Mutant Rat Recombinant is a singly non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Physical Appearance

White lyophilized powder.

Formulation

The protein was lyophilized from a concentrated solution with 0.003mM NaHCO3.

Solubility

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

Stability

Lyophilized Leptin-Antagonist Triple Mutant Rat Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP-tA mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein is suggested.
Please prevent freeze-thaw cycles.

Purity

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

Amino acid sequence

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

Biological Activity

ProSpec’s Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

Protein content

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-Leptin tA Rat, PEG

Description

Catalogue number

CYT-567

Description

Leptin Antagonist Triple Mutant Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.
The Rat Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.
The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin triple anatagonist runs as a 48 kDa.
Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Physical Appearance

White lyophilized powder.

Formulation

The Rat Leptin triple anatagonist was lyophilized from a concentrated solution with 0.003mM NaHCO3.

Solubility

Stability

Lyophilized Leptin Antagonist Triple Mutant Rat Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein is suggested.
Please prevent freeze-thaw cycles.

Purity

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

Biological Activity

Leptin Antagonist Triple Mutant Rat Recombinant half-life in circulation after SC injection was over 20 hours.
Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Rat Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect , resulting mainly from increased food intake.

Protein content

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-MIF Human

Description

Catalogue number

CYT-575

Synonyms

Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

Introduction

The cytokine Macrophage migration inhibitory factor has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

Description

Macrophage Inducing Factor Human Recombinant produced in E. coli is a single, non-glycosylated, polypeptide chain containing 115 amino acids and having a molecular mass of 12kDa. MIF human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

1mg/ml solution containing 50mM Tris-HCl pH-8, 0.5mM DTT & 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 98.0% as determined by -PAGE.

Amino acid sequence

MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA.

References

Title: Macrophage migration inhibitory factor regulates proliferation of gastric cancer cells via the PI3K/Akt pathway
Publication: WJG 15.44 : 5541.
Link: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785056/

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-MIF Human His C

Description

Catalogue number

CYT-521

Synonyms

Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

Introduction

Description

MIF human Recombinant, fused to His-tag at C-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.
Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chaincontaining 123 amino acidsand having a molecular mass of 13.5 kDa.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered lyophilized powder.

Formulation

Human MIF was lyophilized from a 1mg/ml solution containing PBS pH-7.4.

Solubility

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

Stability

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

Measured by its ability to bind rhCD74 in a functional ELISA.

Amino acid sequence

MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPC
ALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTF
ALEHHHHHH.

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-MIF Human His N

Description

Catalogue number

CYT-431

Synonyms

Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

Introduction

Description

MIF human Recombinant, fused to His-tag at N-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.
Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chain having amino acids from 1-114 and having a molecular mass of 16.6 kDa.

Source

Escherichia Coli.

Physical Appearance

Sterile filtered colorless solution.

Formulation

1mg/ml solution containing PBS pH-7.4.

Stability

Liquid MIF although stable 4°C for 1 week, should be stored 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

MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC LHSIGKIGGA QNRSYSKLLC GLLAERLRIS PDRVYINYYD MNAANVGWNN STFA.

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-MIF Human, Active

Description

Catalogue number

CYT-596

Synonyms

Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

Introduction

Description

MIF human Recombinant was cloned into an E.coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.
Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chain containing 115 amino acids and having a molecular mass of 12.5 kDa.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Biological Activity

Human PBMCs were cultured with 0 to 1000ng/ml Human MIF. Production of IL-8 was measured via ELISA after 24 hours. The ED50 which was found to be 88-132ng/ml.

Formulation

MIF-Protein was lyophilized from 10mM sodium phosphate buffer pH-7.5.

Solubility

It is recommended to reconstitute the lyophilized MIF-Protein in sterile 18MΩ-cm H2O at a concentration between 0.1mg-1mg per 1ml.

Stability

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

MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLM
AFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVY
INYYDMNAANVGWNNSTFA.

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-MIF Human, GST

Description

Catalogue number

CYT-401

Synonyms

Macrophage Migration Inhibitory Factor , Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase, L-Dopachrome Isomerase, GLIF, MMIF, GIF, Macrophage Migration Inhibitory Factor, Glycosylation-Inhibiting Factor, EC 5.3.3.12, EC 5.3.2.1, Macrophage migration inhibitory factor.

Introduction

Description

MIF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 345 amino acids and having a molecular mass of 39.2kDa.

MIF is fused to a 230 amino acid GST-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

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

Stability

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPRGSPEFA MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA.

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-MIF Mouse

Description

Catalogue number

CYT-744

Synonyms

Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase, Glif.

Introduction

Description

MIF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa.
The MIF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a 0.2µm filtered solution containing 1mM sodium phosphate, pH 7.5.

Solubility

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

Stability

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

MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTNDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.

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-MIF Mouse, His

Description

Catalogue number

CYT-896

Synonyms

Introduction

Description

MIF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids and having a molecular mass of 14.9kDa.

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

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

MIF protein solution containing Phosphate buffered saline , 10% glycerol and 1mM DTT.

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 MGSMPMFIVN TNVPRASVPE GFLSELTQQL AQATGKPAQY IAVHVVPDQL MTFSGTNDPC ALCSLHSIGK IGGAQNRNYS KLLCGLLSDR LHISPDRVYI NYYDMNAANV GWNGSTFA.

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-MIF Rat

Description

Catalogue number

CYT-193

Synonyms

Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

Introduction

Description

MIF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa.
The MIF 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 1×PBS, pH 7.4 and 5% trehalose.

Solubility

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

Stability

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

MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTSDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.

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-MIF T.Vaginalis

Description

Catalogue number

CYT-1033

Synonyms

Introduction

Description

MIF T.Vaginalis Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 121 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 13.4kDa .

Source

Escherichia Coli.

Physical Appearance

Filtered White lyophilized powder.

Formulation

MIF T.Vaginalis filtered and lyophilized from 0.5mg/ml solution in 20 mM Tris buffer and 50 mM NaCl, pH 7.5.

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. MIF T.Vaginalis 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.

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

MPALVIKTNA KFTEEEKSKA TEELGNIVSK VLGKPISYVM VTLEDGVAVR FGGSDEKAAF MSLMSIGGLN RAVNKRASAA LTKWFTDHGF QGDRIYIVFN PKSAEDWGFN GDTFAHHHHH H.

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-MIA Human

Description

Catalogue number

CYT-310

Synonyms

Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.

Introduction

The Melanoma Inhibitory protein was identified as an inhibitor of in vitro growth of malignant melanoma cells. The protein contains a SH3 domain.
MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion. In a study of human melanoma cell lines with different metastatic capacity MIA mRNA expression appeared to be inversely correlated with pigmentation. MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas.

Description

Melanoma Inhibitory Activity Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain consisting of 108 amino having a total molecular mass of 12237 Dalton.
The MIA 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 20mM Potassium-phosphate pH=7 and 150mM potassium chloride.

Solubility

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

Stability

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

Agrees with the sequence of native MIA human with an addition N-terminal Methionine residue.
MGPMPKLADRKLCADQECSSHPISMAVALQDYMAPDCRFLTIHRGQVV
YVFSLKGRGRFLWGGSVQGDYYGDLAARLGYFPSSIVREDQTLKVDVKT
DKWDFYCQ.

Biological Activity

The biological activity is calculated by the inhibiting effect on the invasion of Mel In Tumor cells and found active in Mel In assay.

Protein content

UV spectroscopy at 280 nm using the absorption coefficient of 19300 M^-1cm^-1.

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-MIA Human, His

Description

Catalogue number

CYT-810

Synonyms

Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.

Introduction

The Melanoma Inhibitory protein was identified as an inhibitor of in vitro growth of malignant melanoma cells. The protein contains a SH3 domain.

MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion. In a study of human melanoma cell lines with different metastatic capacity MIA mRNA expression appeared to be inversely correlated with pigmentation. MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas.

Description

MIA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 128 amino acids and having a molecular mass of 14.4 kDa.

MIA is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

The MIA solution contains 20mM Tris-HCl buffer , 0.4M Urea and 10% glycerol.

Stability

Purity

Greater than 90% as determined by -PAGE.

Amino acid sequence

MGSSHHHHHH SSGLVPRGSH MGPMPKLADR KLCADQECSH PISMAVALQD YMAPDCRFLT IHRGQVVYVF SKLKGRGRLF WGGSVQGDYY GDLAARLGYF PSSIVREDQT LKPGKVDVKT DKWDFYCQ

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-MIA2 Human

Description

Catalogue number

CYT-638

Synonyms

MIA-2, MIA2, Melanoma Inhibitory Activity 2, FLJ22404.

Introduction

MIA2 performs as a tumour suppressor in hepatocellular carcinoma. MIA2is a novel acute phase protein which its expression is found in the liver and reacts to liver damage in chronic liver diseases and is considerably higher in severe fibrosis patients . MIA2 is induced by IL6, TGF-B & and conditioned medium from activated hepatic stellate cells. MIA2 is is mainly expressed in hepatocytes.

Description

MIA2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain consisting of 101 amino having a total molecular mass of 11.5 kDa.
The MIA2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

The MIA2 protein was lyophilized from a concentrated solution containing 20mM Phosphate buffer pH=7.4 and 150mM NaCl.

Solubility

It is recommended to reconstitute the lyophilized MIA2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized MIA2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIA2 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 97.0% as determined by Analysis by RP-HPLC.
Analysis by -PAGE.

Amino acid sequence

MLESTKLLAD LKKCGDLECE ALINRVSAMR DYRGPDCRYL NFTKGEEISV YVKLAGERED LWAGSKGKEF GYFPRDAVQI EEVFISEEIQ MSTKESDFLC L.

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-Myostatin Human

Description

Catalogue number

CYT-418

Synonyms

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Introduction

GDF8 is a member of the bone morphogenetic protein family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

Description

Myostatin Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 109 amino acids and having a total molecular mass of 24814 Dalton.
The GDF-8 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a concentrated solution containing no additives.

Solubility

It is recommended to reconstitute the lyophilized Myostatin in sterile 20mM HCl at 0.1 mg/ml, which can then be further diluted to other aqueous solutions.

Stability

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

The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Phe-Gly-Leu-Asp.

Biological Activity

The ED50 as determined by the inhibition of the proliferation of MPC-11 cells is < 20ng/ml, corresponding to a Specific Activity of 50,000units/mg.

Protein content

Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 1.55 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 Myostatin as a Reference Standard.

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-Myostatin Human, HEK

Description

Catalogue number

CYT-833

Synonyms

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Introduction

Description

Myostatin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 360 amino acids, having a calculated molecular mass of 41.1kDa. Myostatin is fused to a 2 aa N-terminal linker and a 6 aa His tag at N-Terminus.

Source

HEK 293.

Physical Appearance

Filtered colorless solution.

Formulation

Myostatin solution at a concentration of 0.25mg/ml in phosphate buffered saline pH 8.0 and 20% glycerol.

Stability

Amino acid sequence

HHHHHHASNE NSEQKENVEK EGLCNACTWR QNTKSSRIEA IKIQILSKLR LETAPNISKD VIRQLLPKAP PLRELIDQYD VQRDDSSDGS LEDDDYHATT ETIITMPTES DFLMQVDGKP KCCFFKFSSK IQYNKVVKAQ LWIYLRPVET PTTVFVQILR LIKPMKDGTR YTGIRSLKLD MNPGTGIWQS IDVKTVLQNW LKQPESNLGI EIKALDENGH DLAVTFPGPG EDGLNPFLEV KVTDTPKRSR RDFGLDCDEH STESRCCRYP LTVDFEAFGW DWIIAPKRYK ANYCSGECEF VFLQKYPHTH LVHQANPRGS AGPCCTPTKM SPINMLYFNG KEQIIYGKIP AMVVDRCGCS.

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.

ProSpec-Myostatin Human, His

Description

Catalogue number

CYT-445

Synonyms

GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.

Introduction

Myostatin is expressed uniquely in human skeletal muscle as a 12 kDa mature glycoprotein consisting of 113 amino acid residues and secreted into plasma. Myostatin is a member of the transforming growth factor ? superfamily of secreted growth and differentiation factors that is essential for proper regulation of skeletal muscle mass. Studies have shown that myostatin could play an important role in cardiac development and physiology.

Description

Total 152AA. M.W. 16.7kDa . N-terminal His-tag and spacer . The AA sequence of the human myostatin part of the fusion protein is corresponding to the UniProtKB/Swiss-Prot entry O14793.

Source

Escherichia Coli.

Physical Appearance

Filtered white lyophilized powder.

Formulation

Filtered and lyophilized from 0.5mg/ml in 0.05M acetate buffer, pH 4.5.

Solubility

Add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.

Stability

Purity

Greater than 95% as determined by -PAGE.

Amino acid sequence

MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDPSSRSAVR SRRDFGLDCD EHSTESRCCR YPLTVDFEAFGWDWIIAPKR YKANYCSGEC EFVFLQKYPH THLVHQANPR GSAGPCCTPT KMSPINMLYF NGKEQIIYGKIPAMVVDRCG CS.

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-Myostatin Propeptide Human

Description

Catalogue number

CYT-448

Synonyms

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Introduction

Myostatin , a member of the TGFbeta superfamily, is a potent and specific negative regulator of skeletal muscle mass. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and/or follistatin-related gene. The myostatin propeptide is known to bind and inhibit myostatin in vitro. This interaction is relevant in vivo, with a majority of myostatin in serum bound to its propeptide. The myostatin propeptide is negative regulator of myostatin in vivo.

Description

Recombinant Human Myostatin Propeptide is a 27.8kDa protein containing 244 amino acid residues of the human Myostatin Propeptide.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered white lyophilized powder.

Formulation

Lyophilized with no additives.

Solubility

It is recommended to reconstitute the lyophilized Myostatin Propeptide in sterile 20mM HCl at 0.1mg/ml, which can then be further diluted to other aqueous solutions.

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.

Purity

Greater than 95.0% as determined by -PAGE.

Amino acid sequence

MNENSEQKE NVEKEGLCNA CTWRQNTKSS RIEAIKIQIL SKLRLETAPN ISKDVIRQLL PKAPPLRELI DQYDVQRDDS SDGSLEDDDY HATTETIITM PTESDFLMQV DGKPKCCFFK FSSKIQYNKV VKAQLWIYLR PVETPTTVFV QILRLIKPMK DGTRYTGIRS LKLDMNPGTG IWQSIDVKTV LQNWLKQPES NLGIEIKALD ENGHDLAVTF PGPGEDGLNP FLEVKVTDTP KRSRR.

Biological Activity

The protein has full biological activity when compared to a standard. The activity is determined by its ability to inhibit 50ng/ml of Myostatin on MPC-11 cells and is typically 0.13-0.2 μg/ml.

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-Myostatin Propeptide Human, HEK

Description

Catalogue number

CYT-936

Synonyms

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Introduction

Description

Myostatin Propetide Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 253 amino acids, having a calculated molecular mass of 29.1kDa.
Myostatin Propetide is fused to a 10 aa C-terminal His tag.

Source

HEK 293.

Physical Appearance

Filtered colorless solution.

Formulation

Myostatin Propetide solution at a concentration of 0.25mg/ml in phosphate buffered saline pH 8.0 and 20% glycerol.

Stability

Amino acid sequence

NENSEQKENV EKEGLCNACT WRQNTKSSRI EAIKIQILSK LRLETAPNIS KDVIRQLLPK APPLRELIDQ YDVQRDDSSD GSLEDDDYHA TTETIITMPT ESDFLMQVDG KPKCCFFKFS SKIQYNKVVK AQLWIYLRPV ETPTTVFVQI LRLIKPMKDG TRYTGIRSLK LDMNPGTGIW QSIDVKTVLQ NWLKQPESNL GIEIKALDEN GHDLAVTFPG PGEDGLNPFL EVKVTDTPKR SRR HHHHHHH HHH.

Purity

Greater than 80.0% 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.

ProSpec-Noggin Human

Description

Catalogue number

CYT-475

Synonyms

SYM1, SYNS1, NOG.

Introduction

The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta superfamily signaling proteins, such as bone morphogenetic protein-4 . By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism and multiple synostoses syndrome were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

Description

Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa.

Noggin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.

Solubility

It is recommended to be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.

Stability

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

MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC.

Biological Activity

The ED₅₀ was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED₅₀ for this effect is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3×10⁵units/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-Noggin Human, HEK

Description

Catalogue number

CYT-977

Synonyms

Noggin, Symphalangism 1 , Synostoses Syndrome 1, SYNS1A, SYNS1, SYM1.

Introduction

Description

Noggin produced in HEK293 cells is a polypeptide chain containing 211 amino acids and having a molecular mass of 23.8kDa. .
Noggin is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Physical Appearance

Sterile filtered colorless solution.

Formulation

Recombinant Human Noggin hek293 derived protein is provided as a solution containing 50mM MES and 30% 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

QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSCHHHHH H.

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-Noggin Human, Sf9

Description

Catalogue number

CYT-1119

Synonyms

SYM1, SYNS1, NOG.

Introduction

Nogginwhich is encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta superfamily signaling proteins, such as bone morphogenetic protein-4 . By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may play and important role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. Noggin was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. There are several dominant human NOG mutations in unrelated families with proximal symphalangism and multiple synostoses syndrome . All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

Description

Noggin produced in Sf9 Baculovirus cells is a glycosylated homodimer containing 205 amino acids and having a molecular mass of 47.9kDa under non-reducing conditions. .
Noggin is purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20 and 5% trehalose.

Solubility

It is recommended to reconstitute the lyophilized Noggin 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:
Analysis by RP-HPLC
Analysis by -PAGE.

Amino acid sequence

Biological Activity

Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cellsans was fount to be 0.04‑0.2 μg/mL in the presence of 50 ng/mL of Recombinant Human BMP‑4.

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-Noggin Mouse

Description

Catalogue number

CYT-600

Synonyms

Noggin, SYM1, SYNS1, NOG.

Introduction

Description

Noggin Mouse Recombinant produced in E.Coli is a non-glycosylated, disulfide-linked protein consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.4 kDa .

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a 0.2μm filtered solution in 30% acetonitrile, 0.1% TFA.

Solubility

It is recommended to be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.

Stability

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

MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYD
PGFMATSPPEDRPGGGGGPAGGAEDLAELDQLLRQRPSGAMPSEIKG
LEFSEGLAQGKKQRLSKKLRRKLQMWLWSQTFCPVLYAWNDLGSRF
WPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHLTVLRWRCQRRGQR
CGWIPIQYPIISECKCSC.

Biological Activity

The ED₅₀ as determined by inhibiting BMP-4-induced alkaline phosphatase production of murine ATDC5 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 10⁵ IU/mg in the presence of 5ng/ml BMP-4.

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-NOV Human

Description

Catalogue number

CYT-805

Synonyms

Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

Introduction

Nephroblastoma Overexpressed which is encoded by the NOV gene is a part of the CCN family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.

Description

Nephroblastoma Overexpressed Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 331 amino acids and having a molecular mass of 36.2 kDa. The NOV 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 20mM Tris-HCl, pH 8.6 and 150 mM NaCl.

Solubility

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

Stability

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

MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M.

Biological Activity

Determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg. range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/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-NOV Human, HEK

Description

Catalogue number

CYT-1032

Synonyms

Introduction

Description

NOV Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain containing 331 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 36.5kDa .

Source

HEK293 cells.

Physical Appearance

Filtered White lyophilized powder.

Formulation

NOV filtered and lyophilized from 0.5mg/ml in PBS and 5 % 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. NOV is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

Stability

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

QRCPPQCPGR CPATPPTCAP GVRAVLDGCS CCLVCARQRG ESCSDLEPCD ESSGLYCDRS ADPSNQTGIC TAVEGDNCVF DGVIYRSGEK FQPSCKFQCT CRDGQIGCVP RCQLDVLLPE PNCPAPRKVE VPGECCEKWI CGPDEEDSLG GLTLAAYRPE ATLGVEV SVNCIEQTTE WTACSKSCGM GFSTRVTNRN RQCEMLKQTR LCMVRPCEQE PEQPTDKKGK KCLRTKKSLK AIHLQFKNCT SLHTYKPRFC GVCSDGRCCT PHNTKTIQAE FQCSPGQIVK KPVMVIGTCT CHTNCPKNNE AFLQELELKT TRGKMHHHHH H.

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-NOV Mouse

Description

Catalogue number

CYT-171

Synonyms

Protein NOV homolog, NovH, CCN family member 3, Nephroblastoma-overexpressed gene protein homolog, Nov, Ccn3, C130088N23Rik.

Introduction

Nephroblastoma Overexpressed is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein is comprised of 4 structural domains, which present distinct, and sometimes opposing, biological activities. An elevated expression of NOV is linked with certain tumors, including Wilm’s tumor and most nephroblastomas. On the other hand, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is associated with decreased NOV expression.

Description

NOV Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 333 amino acids and having a molecular mass of 36.4kDa.
The NOV is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

NOV protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.5 and 150mM NaCl.

Solubility

It is recommended to reconstitute the lyophilized NOV 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

QVSASLRCPS RCPPKCPSIS PTCAPGVRSV LDGCSCCPVC ARQRGESCSE MRPCDQSSGL YCDRSADPNN QTGICMVPEG DNCVFDGVIY RNGEKFEPNC QYFCTCRDGQ IGCLPRCQLD VLLPGPDCPA PRKVAVPGEC CEKWTCGSDE QGTQGTLGGL ALPAYRPEAT VGVEVSI NCIEQTTEWS ACSKSCGMGV STRVTNRNRQ CEMVKQTRLC IVRPCEQEPE EVTDKKGKKC LRTKKSLKAI HLQFENCTSL YTYKPRFCGV CSDGRCCTPH NTKTIQVEFQ CLPGEIIKKP VMVIGTCTCY SNCPQNNEAF LQDLELKTSR GEI.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 μg/ml, corresponding to a specific activity of > 1000 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-Omentin 298 a.a. Human

Description

Catalogue number

CYT-061

Synonyms

Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

Introduction

Omentin is a recently recognized gene highly localized to the mental tissue . Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

Description

Omentin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids and having a molecular mass of 33.2 kDa.
The Omentin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

Omentin protein is supplied in 20mM Tris-HCL, pH-8, 0.4M Urea and 10% Glycerol.

Stability

Purity

Greater than 90.0% as determined by -PAGE.

Amino acid sequence

MWSTDEANTY FKEWTCSSSP SLPRSCKEIK DECPSAFDGL YFLRTENGVI YQTFCDMTSG GGGWTLVASV HENDMRGKCT VGDRWSSQQG SKAVYPEGDG NWANYNTFGS AEAATSDDYK NPGYYDIQAK DLGIWHVPNK SPMQHWRNSS LLRYRTDTGF LQTLGHNLFG IYQKYPVKYG EGKCWTDNGP VIPVVYDFGD AQKTASYYSP YGQREFTAGF VQFRVFNNER AANALCAGMR VTGCNTEHHC IGGGGYFPEA SPQQCGDFSG FDWSGYGTHV GYSSSREITE AAVLLFYR

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-Omentin Human

Description

Catalogue number

CYT-301

Synonyms

Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

Introduction

Omentin is a recently recognized gene highly localized to the mental tissue . Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase INSstimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of INS presence. Its role in glucose metabolism and obesity remains to be described; an INS-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

Description

Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 313 amino acids and having a molecular mass of
35 kDa. Intelectin is purified by proprietary chromatographic techniques.

Source

E.Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Each mg of lyophilized powder contains 10mM NaP, pH-7.5 and 5:1 mannitol to protein.

Solubility

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

Stability

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

MNQLSFLLFL IATTRGWSTD EANTYFKEWTCSSSPSLPRS CKEIKDECPS AFDGLYFLRT ENGVIYQTFC DMTSGGGGWT LVASVHENDM RGKCTVGDRW SSQQGSKADY PEGDGNWANY NTFGSAEAAT SDDYKNPGYY DIQAKDLGIW HVPNKSPMQH WRNSSLLRYR TDTGFLQTLG HNLFGIYQKY PVKYGEGKCW TDNGPVIPVV YDFGDAQKTA SYYSPYGQRE FNNERAANAL CAGMRVTGCN TEHHCIGGGG YFPEASPQQC GDFSGFDWSG YGTHVGYSSS REITEAAVLLFYR.

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-Omentin Human, His

Description

Catalogue number

CYT-551

Synonyms

Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

Introduction

Description

Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 294 amino acids and having a molecular mass of 32.7 kDa.
Recombinant Human Omentin contains His tag fused at N-Terminus.
Intelectin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Each mg of lyophilized powder contains 20mM Tris & 50mM NaCl pH-8.0.

Solubility

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

Stability

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

MRGSHHHHHH GMASTDEANT YFKEWTCSSS PSLPRSCKEI KDECPSAFDG LYFLRTENGV IYQTFCDMTS GGGGWTLVAS VHENDMRGKC TVGDRWSSQQ GSKAVYPEGD GNWANYNTFG SAEAATSDDY KNPGYYDIQA KDLGIWHVPN KSPMQHWRNS SLLRYRTDTG FLQTLGHNLF GIYQKYPVKY GEGKCWTDNG PVIPVVYDFG DAQKTASYYS PYGQREFTAG FVQFRVFNNE RAANALCAGM RVTGCNTEHH CIGGGGYFPE ASPQQCGDFS GFDWSGYGTH VGYS.

Applications

Elisa
Western blot.

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-OSM Human

Description

Catalogue number

CYT-231

Synonyms

OSM, MGC20461.

Introduction

Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

Description

Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids and having a molecular mass of 26kDa.
The OSM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a concentrated solution containing PBS pH-7.4.

Solubility

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

Stability

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

AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR
ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER
SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP
PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSRRHSPH
QALRKGVRRT RPSRKGKRLM TRGQLPR.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

Protein content

Protein quantitation was carried out by two independent methods
1. UV spectroscopy at 280 nm using the absorbency value of 0.45 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 standard solution of Oncostatin as Reference.

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-OSM Human, 195 a.a

Description

Catalogue number

CYT-735

Synonyms

OSM, MGC20461, Oncostatin M.

Introduction

Description

Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids and having a molecular mass of 22kDa.
The OSM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Lyophilized from a concentrated solution containing 1xPBS pH-7.4.

Solubility

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

Stability

Purity

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

Amino acid sequence

AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSR.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of the proliferation of human TF-1 cells is < 0.2ng/ml, corresponding to a specific activity of > 5.0×10⁶ 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-OSM Human, 209 a.a

Description

Catalogue number

CYT-639

Synonyms

OSM, MGC20461, Oncostatin M.

Introduction

Description

Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids and having a molecular mass of 23.9kDa.
The Oncostatin-M is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized powder.

Formulation

Oncostatin-M was lyophilized from a concentrated solution containing 1x PBS pH-7.4.

Solubility

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

Stability

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

AAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPG
AFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDL
EKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQ
RKLEGCRFLHGYHRFMHSVGRVFKWGESPNRSRRHSPHQALRKGVRR.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 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.

Leptin Mouse, PEG

Catalogue number

Synonyms

Introduction

Description

Source

Physical Appearance

Formulation

Solubility

Stability

Purity

Biological Activity

Usage

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