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).
Source
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.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
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.
SDS-PAGE
94-124 kDa, reducing conditions
Publications
Read Publications using 385-PR/CF in the following applications:
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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