|Detection of Human BMP‑1/PCP by Western Blot. Western blot shows lysates of Jurkat human acute T cell leukemia cell line and human skin tissue. PVDF Membrane was probed with 2 µg/mL of Human BMP‑1/PCP Monoclonal Antibody (Catalog # MAB1927) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for BMP‑1/PCP at approximately 180 kDa (as indicated). This experiment was conducted under non-reducing conditions and using Immunoblot Buffer Group 1.|
Bone morphogenetic protein 1 (BMP-1), also known as procollagen C-proteinase (PCP), is a zinc protease of the astacin family (1, 2). BMP-1/PCP plays a key role in formation of extracellular matrix (ECM) by converting precursor proteins into their mature and functional forms. The precursor proteins identified as substrates for BMP-1/PCP include collagens, biglycan, laminin 5, dentin matrix protein-1, and lysyl oxidase (3). There are six alternatively spliced forms known to be derived from the BMP-1 gene, and isoform 1 consisting of residues 1 to 730 was expressed. The secreted and purified protein does not contain the signal peptide (amino acid residues 1‑22) and pro domain (residues 23‑120), but contain protease (residues 121‑321), CUB I (residues 322‑434), CUB II (residues 435‑546), EGF-like (residues 547‑588) and CUB III (residues 591‑703) domains. The pro domain is apparently cleaved by a furin-like proprotein convertase (4). The purified BMP-1/PCP is an active protease and its peptidase activity can be determined as described above. The purified BMP-1/PCP is predicted to possess procollagen C-proteinase activity because it contains the minimal domain structure required (5).
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