Recombinant Human PDGF R beta Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit the biological activity of PDGF-BB using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED50 for this effect is 1-3 µg/mL in the presence of 50 ng/mL Recombinant Human PDGF‑BB (Catalog # 220-BB).
Mouse myeloma cell line, NS0-derived human PDGF R beta protein
Human PDGF R beta Leu33-Phe530 (Glu241Asp) Accession # P09619
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
84 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
PDGF is a major serum mitogen that can exist as a homo or hetero-dimeric protein consisting of disulfide-linked PDGF-A and PDGF-B chains. The PDGF-AA, PDGF-BB and PDGF-AB isoforms have been shown to bind to two distinct cell surface PDGF receptors with different affinities. Where as PDGF R alpha binds all three PDGF isoforms with high affinity, PDGF R beta binds PDGF-BB only with high-affinity. Both PDGF R alpha and PDGF R beta are members of the class III subfamily of receptor tyrosine kinases (RTK) that also includes the receptors for M-CSF, SCF and Flt3 ligand. All class III RTKs are characterized by the presence of five immunoglobulin-like domains in their extracellular region and a split kinase domain in their intracellular region. PDGF binding induces receptor homo-and hetero-dimerization and signal transduction. The expression of the alpha and beta receptors is independently regulated in various cell types. Recombinant soluble PDGF R beta binds PDGF with high affinity and is potent PDGF antagonist.
Heldin, C.H. and L. Claesson-Welsh (1994) in Guidebook to Cytokines and Their Receptors, Nicola, N.A. ed. Oxford University Press, New York, p. 202.
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