|BMPR‑IA/ALK‑3 in Human Prostate. BMPR‑IA/ALK‑3 was detected in immersion fixed paraffin-embedded sections of human prostate using Mouse Anti-Human BMPR‑IA/ALK‑3 Monoclonal Antibody (Catalog # MAB24061) at 25 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm in epithelial cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
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% sequence identity
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