PBS, 5% trehalose
recombinant soluble human platelet-derived growth factor receptor α expressed in Sf 21 cells.
Purified by affinity chromatography
For In vitro laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
CD140A, MGC74795, PDGFR2, RHEPDGFRA
Platelet-Derived Growth Factor (PDGF) in serum is the principal mitogen present for cells of mesenchymal origin. PDGF is localized in alpha-granules of platelets and released during clot formation. PDGF from human platelets has been purified and described as a cationic glycoprotein (pI 9.5 to 10.4) having a molecular weight of approximately 30 kD and composed of two covalently linked subunits, designated as chains A (16 kD) and B (14 kD). In platelets, approximately 70% of the PDGF is present as the AB dimer, with most of the remainder as BB.Purified human PDGF shows substantial size heterogeneity, ranging from 27 to 31 kD, probably due to the presence of isoforms, glycosylation processing, aging of the platelets, and partial proteolysis during purification. The A and B chains are 40% homologous in sequence and are encoded by distinctly different genes. Each chain contains 8 cysteine residues, which are involved in intra- and inter-chain disulfide bonds. Cleavage of these bonds by reduction causes irreversible loss of biological activity. PDGF elicits multifunctional actions with a variety of cells.Two distinct human PDGF receptors have been identified, PDGF alpha and PDGF beta, which are structurally related, consist of an extracellular region, a single transmembrane region, and an intracellular region. The three different isoforms of PDGF (PDGF-AA, PDGF-AB, and PDGF-BB) bind with different affinities to two both receptors. Ligand binding induces receptor dimerization. The A-subunit of PDGF binds to alpha-receptors, whereas the B-subunit binds to both alpha- and beta- receptors. Binding of PDGF to its receptor activates the tyrosine kinase domain and leads to enhanced phosphorylation of intracellular substrates as well as autophosphorylation of the receptor itself. Autophosphorylation is induced by allowing binding and activation of the cytoplasmic SH2-domain, which contains signal transduction molecules. Thereby, a number of different signaling pathways are initiated leading to cell growth, actin reorganization, migration and differentiation.