- CITATIONS: 1
|Application ||IHC-P, WB, E|
|Calculated MW||111249 Da|
|Antigen Region||957-986 aa|
|Other Names||Bone morphogenetic protein 1, BMP-1, Mammalian tolloid protein, mTld, Procollagen C-proteinase, PCP, BMP1, PCOLC|
|Target/Specificity||This Bmp1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 957-986 amino acids from the C-terminal region of human Bmp1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Bmp1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Cleaves the C-terminal propeptides of procollagen I, II and III. Induces cartilage and bone formation. May participate in dorsoventral patterning during early development by cleaving chordin (CHRD). Responsible for the proteolytic activation of lysyl oxidase LOX.|
|Cellular Location||Golgi apparatus, trans-Golgi network. Secreted, extracellular space, extracellular matrix. Note=Co- localizes with POSTN in the Golgi.|
Provided below are standard protocols that you may find useful for product applications.
The BMP1 locus encodes a protein that is capable of inducing formation of cartilage in vivo. Although other bone morphogenetic proteins are members of the TGF-beta superfamily, BMP1 encodes a protein that is not closely related to other known growth factors. BMP1 protein and procollagen C proteinase (PCP), a secreted metalloprotease requiring calcium and needed for cartilage and bone formation, are identical. PCP or BMP1 protein cleaves the C-terminal propeptides of procollagen I, II, and III and its activity is increased by the procollagen C-endopeptidase enhancer protein. The BMP1 gene is expressed as alternatively spliced variants that share an N-terminal protease domain but differ in their C-terminal region.
Leighton, M., et al., J. Biol. Chem. 278(20):18478-18484 (2003).
Hartigan, N., et al., J. Biol. Chem. 278(20):18045-18049 (2003).
Garrigue-Antar, L., et al., J. Biol. Chem. 277(45):43327-43334 (2002).
Rattenholl, A., et al., J. Biol. Chem. 277(29):26372-26378 (2002).
Janitz, M., et al., J. Mol. Med. 76(2):141-146 (1998).
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