PDGFRβ, also known as CD140b, is a type I transmembrane glycoprotein and receptor tyrosine kinase encoded by PDGFRB in humans.1 It is composed of five extracellular immunoglobulin-like (Ig-like) domains, a transmembrane domain, and an intracellular kinase domain. PDGFRβ is ubiquitously expressed and functions as a homodimer or a heterodimer with PDGFRα. Binding of the growth factor PDGF-BB or PDGF-DD to PDGFRβ promotes homodimerization, 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.1,2,3 Knockdown of Pdgfrb decreases the number of vascular smooth muscle cells, induces CNS-specific reduction in pericytes, and is postnatally lethal in mice. De novo mutations in PDGFRB have been found in patients with novel overgrowth syndrome.4 Cayman's PDGFRβ/CD140b Extracellular Domain (human, recombinant) protein can be used for binding assays. This protein consists of 510 amino acids, has a calculated molecular weight of 57.6 kDa, and a predicted N-terminus of Leu33 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 95 to 100 kDa due to glycosylation.WARNING This product is not for human or veterinary use.
