1. Recombinant Proteins
  2. Cytokines and Growth Factors
  3. TGF-beta Superfamily
  4. Bone Morphogenetic Proteins (BMPs)
  5. Bone Morphogenetic Protein 1

Bone Morphogenetic Protein 1

Bone morphogenetic protein 1 (BMP-1) also known as metalloprotease, belonging to the BMP-1/tolloidlike proteinases (BTP) family[1][2]. BTPs are known to be involved in the control of muscle growth and homeostasis and in wound healing and tissue repair, and BMP-1 is a signature extracellular matrix (ECM) proteins associated with the high metastatic potential of breast tumors[3]. BMP-1 regulates morphogenesis by processing precursors to mature functional extracellular matrix (ECM) proteins and several growth factors including TGFβ, BMP2, BMP4 and GFD8[4]. BMP-1 is the dominant C-proteinase in postnatal lung fibroblasts and mediates cleavage of COOH-terminal propeptide of type I procollagen (CICP) with the main action site of extracellular space[1]. BMP-1 maintains appropriate levels of procollagen I and its activated products, acts as an essential part for maintaining periodontal homeostasis and normal cementum formation[2]. The cleavage of thrombospondin-1 (TSP-1), an ECM protein classified as “matricellular” for its ability to regulate cell-matrix interactions, results BMP-1 overexpression. However BMP-1 can both trigger the disruption of cell adhesion and stimulate TGF-β signaling in TSP-1-rich microenvironments, which promote the differentiation of primary human keratocytes into myofibroblasts[3]. Thereby, BMP-1 participates in several developmental and physiological processes such as cartilage and bone formation, muscle growth and homeostasis[2][3]. Mutations of BMP-1 gene cause osteogenesis imperfecta in human, a bone disorder characterized by brittle bones that are prone to fracture, or phenotypes of periodontal disease and skin fragility in mice[3]. BMP-1-3 is a novel systemic regulator of bone repair. BMP-1-3 isoform of the BMP-1 gene circulates in the human plasma and enhances bone healing. In vitro BMP-1-3 increases the expression of collagen type I and osteocalcin in MC3T3-E(1) osteoblast like cells, and enhances the formation of mineralized bone nodules from bone marrow mesenchymal stem cells[4].

Cat. No. Product Name / Synonyms Species Source
  • HY-P7668
    PRCP Protein, Human (HEK293, His)

    Lysosomal Pro-X Carboxypeptidase; Angiotensinase C; Lysosomal Carboxypeptidase C; Proline Carboxypeptidase; Prolylcarboxypeptidase; PRCP; PCP

    Human HEK293
    PRCP protein acts as an enzyme that cleaves the C-terminal amino acid linked to proline in peptides, including angiotensin II, III and des-Arg9-bradykinin. Although some substrates retain enzymatic activity even at neutral pH, this cleavage activity is noteworthy because it occurs at acidic pH. PRCP Protein, Human (HEK293, His) is the recombinant human-derived PRCP protein, expressed by HEK293 , with C-6*His labeled tag. The total length of PRCP Protein, Human (HEK293, His) is 475 a.a., with molecular weight of 60-90 kDa.
  • HY-P72106
    BMP-1 Protein, Human (His)

    BMP 1; BMP-1; BMP1; BMP1_HUMAN; Bone morphogenetic protein 1; Mammalian tolloid protein; mTld; OI13; PCOLC; PCP; PCP2; Procollagen C endopeptidase; Procollagen C proteinase; Procollagen C-proteinase; TLD; Tolloid; Drosophila; homolog of

    Human E. coli
    Bone morphogenetic protein 1 (BMP-1), also known as metalloproteinases, belongs to the BMP-1/tolloidlike proteinases (BTP) family. BMP-1 is also a signature extracellular matrix (ECM) protein associated with high metastatic potential in breast tumors. BMP-1 processes growth factors, including TGF-β, BMP-2, BMP-4, and GFD8, regulates morphogenesis, and mediates the cleavage of COOH-terminal propeptide of type I procollagen (CICP) in the extracellular space. The total length of human BMP-1 protein is 986 amino acids (M1-K986), with 4 glycosylation domains. BMP-1 Protein, Human (His) has a total length of 866 amino acids (A121-K986), is expressed in E. coli cells with a N-terminal *His-tag.
Cat. No. Product Name Effect Purity