SpecificityThere are six reported isoforms of human BMP-1 and ab38951 recognizes four of them; the 986, 823, 730 and 622 amino acid forms. The predicted MWs are 111.2, 92.7, 82.9 and 70.5 kDa respectively. This antibody recognizes an epitope that sits in the propeptide region of human BMP-1, which is proteolytically removed on activation of BMP-1.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Application notesWB: A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen. Ab38951 will detect the shorter BMP-1(kDa) as well as the longer mTld form of BMP-1(111kDa). Dilution optimised using Chromogenic detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.
RelevanceBone morphogenetic protein 1 (BMP1) was first identified in osteogenic extracts of bone. It is an extracellular zinc endopeptidase, implicated in morphogenetic processes in a broad range of species. BMP1 is a member of the astacin family of metalloproteinases. The astacin family includes BMP1, astacin, meprin A and B, tolloid-like proteins, and choriolysin. BMP1 is involved in extracellular matrix (ECM) formation, suggesting that a functional link may exist between astacin metalloproteinases, growth factors, and cell differentiation and pattern formation during development. The name PCP reflects this enzyme’s involvement in the collagen deposition of growing bone. The enzymes known as the procollagen C and N proteinases (PCP and PNP) are involved in the processing of fibrillar procollagen precursors to mature collagens, which is an essential requirement for fibril formation. PCP cleaves the C-terminus from procollagen, to allow the formation of mature, triplehelical collagen. The N-terminus is cleaved by the procollagen N-proteinase (PNP or ADAM-TS2). Defects in PNP have been linked to the skin disorder dermatosparaxis, and defects in BMP1 are thought to lead to aberrant collagen processing, and connective tissue disorders. Many forms of BMP1 have been reported, with varying truncation at the C-terminus. The long form of BMP1 is most similar to the tolloid-like proteins, which have extra EGF-like and CUB domains.