Cayman PDGFRα/CD140a (human, recombinant)

PDGFRα, also known as CD140a, is a type I transmembrane glycoprotein and receptor tyrosine kinase.^, 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. 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. 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.^, Activating point mutations in PDGFRA, the gene encoding PDGFRα, are associated with gastrointestinal stromal tumors. 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.

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