General Notes
Mouse anti Human MMP-9 antibody, clone B10-7B9, recognizes matrix metalloproteinase 9 (MMP-9) also known as 92 kDa gelatinase and 92 kDa type IV collagenase. MMP-9 is a member of the zinc-dependent endopeptidases and is expressed in various cell types, including neutrophils, macrophages, fibroblasts and endothelial cell (Huang 2018). Expression of MMP-9 is induced by pro-inflammatory cytokines and is synthesized as a pre-proenzyme with a 19 amino acid N-terminal signal peptide. It can then be secreted by the cell into the extracellular environment where it is modified into the inactive pro-MMP9. At this point it can be activated by various proteases such as MMP-3, to generate the activated 82 kDa form (Vandooren et al. 2013). Activated MMP-9 can proteolytically cleave many extracellular matrix proteins including gelatin, collagen and elastin as part of extracellular matrix remodeling. Overexpression of MMP-9 has been observed in a range of malignant tumors and its’ extracellular matrix remodeling has been linked with mediating tumor invasion, metastasis, angiogenesis and regulating the tumor microenvironment (Huang 2018). MMP-9 has also been associated with other pathologies including autoimmune and cardiovascular diseases.The biotinylated Mouse anti Human MMP-9 antibody, clone B10-7B9 (MCA6197B) can be used as a detection antibody in a sandwich ELISA with the purified Mouse anti Human MMP-9 antibody, clone I13-2E1 (MCA6196GA) as the capture antibody.