BMP-1 Protein, Human (His)

Bone morphogenetic protein 1 (BMP-1), also known as metalloproteinases, belongs to the BMP-1/tolloidlike proteinases (BTP) family^[1][2]. BMP-1 is also a signature extracellular matrix (ECM) protein associated with high metastatic potential in breast tumors^[3]. BMP-1 processes growth factors, including TGF-β, BMP-2, BMP-4, and GFD8, regulates morphogenesis^[4], and mediates the cleavage of COOH-terminal propeptide of type I procollagen (CICP) in the extracellular space^[1]. 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.

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].
BMP1 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].
BMP1 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, BMP1 participates in several developmental and physiological processes such as cartilage and bone formation, muscle growth and homeostasis^[2][3].
Mutations of BMP1 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].
BMP1-3 is a novel systemic regulator of bone repair. BMP1-3 isoform of the BMP-1 gene circulates in the human plasma and enhances bone healing. In vitro BMP1-3 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].
BMP-1 is widely found in different animals, while the sequence in human is highly similar with rat (96.54%), and mouse (96.34).

BMP-1 produced by human keratocytes (185 nM; 4 hr; 37 ℃) cleaves TSP-1 whether soluble and insoluble isoform, and results in abnormal adhesion of HT1080 cells on cleaved TSP-1^[4].
BMP1-3, isoform of the Bmp-1, circulates in the human plasma and is significantly increased in patients with acute bone fracture^[5].
BMP1-3 (50 ng/mL; once every two days for three times) 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^[5].

BMP1-3 (human; 3 μg/rats and 20 μg/rabbits; i.v.; 3 times per week for 6 weeks) enhances bone healing when treated systemically to rats (250-300 g) with a long bone fracture and locally to rabbits with a critical size defect of the ulna^[5].

Measured by its ability to cleave a fluorogenic peptide substrate Mca-YVADAPK(Dnp)-OH. The specific activity is 4.879 pmol/min/µg.

Human

E. coli

N-6*His

P13497 (A121-K986)

649  [NCBI]

AATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCPACGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKLPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEAICGGDVKKDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEKPDDIKSTSSRLWLKFVSDGSINKAGFAVNFFKEVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRCEAACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCKEAGCDHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFMEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLATGSRMFLRFYSDNSVQRKGFQASHATECGGQVRADVKTKDLYSHAQFGDNNYPGGVDCEWVIVAEEGYGVELVFQTFEVEEETDCGYDYMELFDGYDSTAPRLGRYCGSGPPEEVYSAGDSVLVKFHSDDTITKKGFHLRYTSTKFQDTLHSRK

Approximately 102 kDa

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from a 0.2 μm solution of Tris-based buffer, 50% Glycerol or 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0 or PBS, 6% Trehalose, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. N'Diaye EN, et al. Extracellular BMP-1 is the major proteinase for COOH-terminal proteolysis of type I procollagen in lung fibroblasts. Am J Physiol Cell Physiol. 2021 Feb 1;320(2):C162-C174.  [Content Brief]

  [2]. Wang J, et al. Proteinase bone morphogenetic protein 1, but not tolloid-like 1, plays a dominant role in maintaining periodontal homeostasis. J Periodontol. 2021 Jul;92(7):1018-1029.  [Content Brief]

  [3]. Anastasi C, et al. BMP-1 disrupts cell adhesion and enhances TGF-β activation through cleavage of the matricellular protein thrombospondin-1. Sci Signal. 2020 Jul 7;13(639):eaba3880.  [Content Brief]

  [4]. Grgurevic L, et al. Bone morphogenetic protein (BMP)1-3 enhances bone repair. Biochem Biophys Res Commun. 2011 Apr 29;408(1):25-31.  [Content Brief]