A recombinant partial protein sequence (within amino acids 1-200) from the human protein was used as the immunogen for the PDGFRA antibody.
Platelet-derived growth factor (PDGF) is a mitogen for mesenchyme- and glia-derived cells. PDGF consists of two chains, A and B, which dimerize to form functionally distinct isoforms, PGDF-AA, PDGF-AB and PDGF-BB. These three isoforms bind with different affinities to two receptor types, PDGFR-a and -beta, which are endowed with protein tyrosine kinase domains. PDGFR-a can bind to both A and B subunits of PDGF, while PDGFR-beta can only bind the B subunit. Ligand binding promotes either homo- or heterodimerization of the PDGF receptors in a specific manner. PDGF-AA induces the dimerization of two a receptors, PDGF-AB induces dimerization of aa and abeta and PDGF-BB induces the formation of three types of dimers, aa, abeta and betabeta. Translocation of the PDGFR-beta gene with the Tel gene is linked to chronic myelomonocytic leukemia (CMML), a myelodysplastic syndrome, and demonstrates the oncogenic potential of the PDGF receptors.
