Human BMPR‑IB/ALK‑6 APC‑conjugated Antibody

Cellular responses to bone morphogenetic proteins (BMPs) have been shown to be mediated by the formation of hetero-oligomeric complexes of the type I and type II serine/threonine kinase receptors. BMP receptor IB (BMPR-IB), also known as activin receptor-like kinase (ALK)-6, is one of seven known type I serine/threonine kinases that are required for the signal transduction of TGF-beta family cytokines. In contrast to the TGF-beta receptor system in which the type I receptor does not bind TGF-beta in the absence of the type II receptor, type I receptors involved in BMP signaling (including BMPR-IA, BMPR-IB/ALK-6, and ActR-I/ALK-2) can independently bind the various BMP family proteins in the absence of type II receptors. Recombinant soluble BMPR-IB binds BMP-4 with high-affinity in solution and is a potent BMP-4 antagonist in vitro. BMPR-IB is expressed in various tissues during embryogenesis. In adult tissues, BMPR-IB is only found in the brain. The extracellular domain of BMPR-IB shares little amino acid sequence identity with the other mammalian ALK type I receptor kinases, but the cysteine residues are conserved. Human and mouse BMPR-IB are highly conserved and share 98% amino acid sequence identity.