PDGFRα/CD140a (human, recombinant)

PDGFRα, also known as CD140a, is a type I transmembrane glycoprotein and receptor tyrosine kinase.^1,2 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.² 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.¹ 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.^1,2 Activating point mutations in PDGFRA, the gene encoding PDGFRα, are associated with gastrointestinal stromal tumors.² 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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1. Heldin, C.-H., and Lennartsson, J. Structural and functional properties of platelet-derived growth factor and stem cell factor receptors. Cold Spring Harb. Perspect. Biol. 5(8), a009100 (2013).

2. Roskoski, R., Jr. The role of small molecule platelet-derived growth factor receptor (PDGFR) inhibitors in the treatment of neoplastic disorders. Pharmacol. Res. 129, 65-83 (2018).