PDGFR?/CD140a (human, recombinant)

PDGFR?/CD140a (human, recombinant)

CAT N°: 31843
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From 505.00 429.25

PDGFR?, 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. PDGFR? is widely expressed and functions as a homodimer or a heterodimer with PDGFR?.{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 PDGFR?.{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 PDGFR?, are associated with gastrointestinal stromal tumors.{60401} PDGFR? can also fuse with FIP1L1, and the fusion protein has been found in patients with idiopathic hypereosinophilia. Cayman’s PDGFR?/CD140a (human, recombinant) protein can be used for binding activity assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of PDGFR? (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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