Recombinant Human BMP-1/PCP Protein, CF

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).