assay
≥95% (SDS-PAGE)
form
lyophilized
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
impurities
≤1 ng/μg Endotoxin (ng/μg PDGF-BB)
shipped in
dry ice
storage temp.
−70°C
Quality Level
General description
Recombinant, 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.
Biochem/physiol Actions
ED₅₀ = 1-5 ng/ml as determined by the dose dependent proliferation of BALB/c 3T3 cells
Physical form
Lyophilized from a sterile-filtered solution, carrier free.
Preparation Note
Reconstitute 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.
Other Notes
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.
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.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
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Paulina Villar-Fincheira et al.
Frontiers in physiology, 12, 722528-722528 (2021-10-29)
Little is known about the effects of training load on exercise-induced plasma increase of interleukin-6 (IL-6) and soluble IL-6 receptor (sIL-6R) and their relationship with vascular remodeling. We sought to evaluate the role of sIL 6R as a regulator of
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