|Detection of BMPR‑IA/ALK‑3 in PC‑3 Human Cell Line by Flow Cytometry. PC‑3 human prostate cancer cell line was stained with Goat Anti-Human BMPR‑IA/ALK‑3 Fluorescein‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB346F, filled histogram) or isotype control antibody (Catalog # IC108F, open histogram). View our protocol for Staining Membrane-associated Proteins.|
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 1A (BMPR-1A), also known as activin receptor-like kinase (ALK)-3, 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-IA binds BMP-4 with high-affinity in solution and is a potent BMP-4 antagonist in vitro. BMPR-IA is ubiquitously expressed during embryogenesis. In adult tissues, BMPR-IA mRNA is also widely distributed with the highest expression levels found in skeletal muscle. The extracellular domain of BMPR-IA 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-IA are highly conserved and share 98% amino acid sequence identity
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