| Applications | WB, IP |
| Clonality | Polyclonal |
| Host | Goat |
| Conjugate | Alexa Fluor 405 |
| Immunogen | Mouse myeloma cell line NS0-derived recombinant human BMP‑1/PCP Ala121-Gln730 Accession # NP_001190 |
| Specificity | Detects human BMP‑1/PCP direct ELISAs and Western blots. In direct ELISAs, approximately 10% cross-reactivity with recombinant human (rh) TLL-2 is observed, and less than 1% cross-reactivity with rhBMP-2, -3, -3b, -4, -5, -6, -7, -8, -9, -10, and -15 is o |
| Isotype | IgG |
| Clonality | Polyclonal |
| Host | Goat |
| Purity Statement | Antigen Affinity-purified |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
| Storage | Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied |
| Buffer | Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide |
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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