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521225 PDGF, BB Homodimer, Human, Recombinant, E. coli

MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: rhPDGF-BB

521225
  
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Overview

Replacement Information

Key Spec Table

Purity
≥95% by SDS-PAGE
Description
OverviewRecombinant, human platelet-derived growth factor (disulfide-linked dimer of two 109 amino acid B-chain monomers) expressed in E. coli. Shown to be a potent chemoattractant for neutrophils, mesenchymal and mononuclear cells. Has the same amino acid sequence as mature human PDGF-B. Rapidly activates protein kinase D in vascular smooth muscle cells.
Catalogue Number521225
Brand Family Calbiochem®
SynonymsrhPDGF-BB
References
ReferencesAbedi, H., et al. 1998. FEBS Lett. 427, 209.
Abboud, H.E., et al. 1994. J. Cell Physiol. 158, 140.
Westermark, B., and Heldin, C.-H. 1991. Cancer Res. 51, 5087.
Raines, E.W., et al. 1985. Methods Enzymol. 109, 749.
Johnson, A., et al. 1984. EMBO J. 3, 921.
Product Information
FormLyophilized
FormulationLyophilized from a sterile-filtered solution, carrier free.
Quality LevelMQ100
Applications
Biological Information
Biological activityED₅₀ = 1-5 ng/ml as determined by the dose dependent proliferation of BALB/c 3T3 cells
Purity≥95% by SDS-PAGE
Physicochemical Information
ContaminantsEndotoxin: ≤1 ng/µg PDGF-BB
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage ≤ -70°C
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 3 months at -70°C.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
521225 0

Documentation

PDGF, BB Homodimer, Human, Recombinant, E. coli SDS

Title

Safety Data Sheet (SDS) 

PDGF, BB Homodimer, Human, Recombinant, E. coli Certificates of Analysis

TitleLot Number
521225

References

Reference overview
Abedi, H., et al. 1998. FEBS Lett. 427, 209.
Abboud, H.E., et al. 1994. J. Cell Physiol. 158, 140.
Westermark, B., and Heldin, C.-H. 1991. Cancer Res. 51, 5087.
Raines, E.W., et al. 1985. Methods Enzymol. 109, 749.
Johnson, A., et al. 1984. EMBO J. 3, 921.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision01-October-2007 JSW
SynonymsrhPDGF-BB
DescriptionRecombinant, human platelet-derived growth factor (disulfide-linked dimer of two 109 amino acid B-chain monomers) expressed in E. coli. Shown to be a potent chemoattractant for neutrophils, mesenchymal, and mononuclear cells. PDGF represents one of the major mitogens present in platelets. It exerts its effects by binding to specific high-affinity dimeric receptor tyrosine kinases. Material has the same amino acid sequence as mature human PDGF-B. Two distinct PDGF receptors have been identified: the PDGFα receptor, which binds to all three forms of PDGF, and the PDGFβ receptor, which can bind only PDGF-BB and PDGF-AB.
FormLyophilized
FormulationLyophilized from a sterile-filtered solution, carrier free.
Purity≥95% by SDS-PAGE
ContaminantsEndotoxin: ≤1 ng/µg PDGF-BB
Biological activityED₅₀ = 1-5 ng/ml as determined by the dose dependent proliferation of BALB/c 3T3 cells
SolubilityReconstitute to a concentration of ≥100 µg/ml 100 mM acetic acid, 0.1% BSA. Further dilute with low endotoxin medium or buffered solution containing FBS or tissue culture grade BSA just prior to use.
Storage ≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 3 months at -70°C.
Toxicity Standard Handling
Merck USA index14, 7525
ReferencesAbedi, H., et al. 1998. FEBS Lett. 427, 209.
Abboud, H.E., et al. 1994. J. Cell Physiol. 158, 140.
Westermark, B., and Heldin, C.-H. 1991. Cancer Res. 51, 5087.
Raines, E.W., et al. 1985. Methods Enzymol. 109, 749.
Johnson, A., et al. 1984. EMBO J. 3, 921.