Mouse Bone morphogenetic protein 1(BMP1) ELISA kit

Metalloprotease that plays key roles in regulating the formation of the extracellular matrix (ECM) via processing of various precursor proteins into mature functional enzymes or structural proteins. Thereby participates in several developmental and physiological processes such as cartilage and bone formation, muscle growth and homeostasis, wound healing and tissue repair. Roles in ECM formation include cleavage of the C-terminal propeptides from procollagens such as procollagen I, II and III or the proteolytic activation of the enzyme lysyl oxidase LOX, necessary to formation of covalent cross-links in collagen and elastic fibers. Additional substrates include matricellular thrombospondin-1/THBS1 whose cleavage leads to cell adhesion disruption and TGF-beta activation.

1. Biochemical studies identify a Bmp-mTORC1-Hif1a signaling cascade resulting in upregulation of Glut1 in chondrocytes that is essential for murine skeletal development. PMID: 30446646
2. Loss of BMP1-like proteinase activity is shown to result in markedly thinned and fragile skin with unusually densely packed collagen fibrils and delayed wound healing. PMID: 27363389
3. plays crucial role in maintaining extracellular matrix homeostasis essential to root formation and dentin mineralization PMID: 27847137
4. Bone morphogenetic protein and retinoic acid synergistically specify female germ-cell fate in mice. PMID: 28928204
5. the proteinases encoded by Bmp1 and Tll1 genes play essential roles in the development and maintenance of mouse dentin and periodontal ligaments. PMID: 28000152
6. The presented data demonstrate Bmp1/Tll1 products to be of profound importance to bone growth and modeling. PMID: 24419319
7. Bone morphogenetic protein-1 processes insulin-like growth factor-binding protein 3. PMID: 21697095
8. during endochondral ossification, BMP and TGFbeta signaling can have antagonistic effects on chondrocyte proliferation and differentiation in vivo PMID: 21297990
9. BMP-1 protein was expressed in type I and IIa but not in IIb muscle fibers. BMP-1 mRNA levels were unaffected by either food deprivation or hindlimb suspension. PMID: 20658214
10. periostin supported BMP-1-mediated proteolytic activation of LOX on the extracellular matrix, which promoted collagen cross-linking. PMID: 20181949
11. products of Bmp1 and Tll1 are responsible for in vivo cleavage of Chordin in mammals PMID: 12808086
12. processing of the prodomain of OGN by BMP-1 potentiates the ability of OGN to modulate the formation of collagen fibrils PMID: 15292192
13. BMP1 cleaves LTBP1 at two specific sites, liberating the large latent complex from the extracellular matrix and resulting in consequent activation of TGFbeta1 via cleavage of its prodomain, latency-associated peptide, by non-BMP1-like proteinases. PMID: 17015622
14. BMP signaling promotes the generation of astrocytes and mature, myelinating oligodendrocytes in vivo but does not affect oligodendrocyte precursor development, thus suggesting tight regulation of BMP signaling to ensure proper gliogenesis PMID: 17391983
15. Bmp1 processes prl to a 17-kDa anti-angiogenic factor. PMID: 17548836
16. proteolytic cleavage of the propeptide by BMP-1/TLD proteases plays a critical role in the activation of latent myostatin in vivo PMID: 18286185
17. FN binds BMP1-like proteinases in vivo and that FN is an important determinant of the in vivo activity levels of BMP1-like proteinases. PMID: 19617627

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Golgi apparatus, trans-Golgi network. Secreted, extracellular space, extracellular matrix. Secreted. Note=Co-localizes with POSTN in the Golgi.

Peptidase M12A family

At high levels in embryonic maternal deciduum and floor plate region of the neural tube. Less in developing membranous and endochondral bone, submucosa of intestine, dermis of skin and the mesenchyme of spleen and lung.

KEGG: mmu:12153

STRING: 10090.ENSMUSP00000022693

UniGene: Mm.27757