PDGFRα/CD140a (human, recombinant)

PDGFR2|Platelet-derived Growth Factor Receptor 2|Platelet-derived Growth Factor Receptor α|RHEPDGFRA

PDGFRα, also known as CD140a, is a type I transmembrane glycoprotein and receptor tyrosine kinase.{54656,60401} It is composed of five extracellular immunoglobulin-like (Ig-like) domains, a transmembrane domain, and an intracellular kinase domain. PDGFRα is widely expressed and functions as a homodimer or a heterodimer with PDGFRβ.{60401} Binding of the growth factor PDGF-AA or PDGF-CC induces homodimerization, while binding of PDGF-BB or PDGF-AB can induce either homodimerization or heterodimerization with PDGFRβ.{54656} In each case, binding of the ligands induces receptor autophosphorylation and a conformational change that facilitates access to the intracellular kinase domain and intracellular signaling through multiple pathways, including ERK/MAPK, PI3K/AKT/mTOR, PLC/PKC, and JAK/STAT.{54656,60401} Activating point mutations in PDGFRA, the gene encoding PDGFRα, are associated with gastrointestinal stromal tumors.{60401} PDGFRα can also fuse with FIP1L1, and the fusion protein has been found in patients with idiopathic hypereosinophilia. Cayman’s PDGFRα/CD140a (human, recombinant) protein can be used for binding activity assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of PDGFRα (amino acids 24-524) fused to human IgG1 Fc at its C-terminus, consists of 739 amino acids and has a calculated molecular weight of 82.9 kDa. As a result of glycosylation, the monomer migrates at approximately 120-130 kDa by SDS-PAGE under reducing conditions.

-80

-80

Lyophilized from sterile PBS, pH 7.4

365

≥90% estimated by SDS-PAGE