Matrix metalloproteinase 9 (MMP-9), also known as gelatinase B, belongs to the broader family of MMPs, which, as their name suggests, are zinc-dependent enzymes whose classical substrates are extracellular matrix proteins. MMP-9 is generally secreted as an inactive 92 kD pro-form. A cysteine residue in the pro-domain coordinates with zinc in the catalytic domain to confer latency. When the pro-domain is cleaved off by other proteases, such as MMP-3, the enzyme is activated and forms its typical 82 kD mature form. Other domains on the mature form, such as fibronectin repeats and a hemopexin domain, help to determine substrate specificity. An atypical 65 kD mature form also exists that lacks the hemopexin domain.MMP-9 is secreted by many cell types, but notably neutrophils, monocytes, macrophages, endothelial cells, platelets, and tumor cells. Its substrates include not only matrix proteins such as collagenases, but also chemokines and cytokines. It is regulated at many levels- transcription, secretion, activation, sequestration, and by the presence of natural inhibitors. MMP-9 plays important roles in inflammation, wound healing, tissue remodeling, cell migration, and tumor growth and metastasis. It is a potential biomarker for many diseases and conditions, often with elevated levels seen in various cancers, inflammatory conditions, allergies, autoimmune diseases, and myocardial infarction.Interestingly, MMP-9 is the only MMP that can form homodimers, and they are biologically active. Because the dimers form at the C-terminal hemopexin domain, both pro- and mature homodimer forms can exist. MMP-9 can also interact and bind to a multitude of other proteins. For example, tissue inhibitor of metalloproteinase 1 (TIMP-1) is its natural inhibitor; other binding partners include CD44 and neutrophil gelatinase-associated lipocalin (NGAL).MMP-9 is most closely related to MMP-2, with which it shares only 46% amino acid sequence identity overall. Across species, human MMP-9 shares 82-99% amino acid sequence identity with MMP-9s of non-human primates (NHPs).BioLegend's LEGEND MAX(TM) Human MMP-9 ELISA Kit is a Sandwich Enzyme-Linked Immunosorbent Assay (ELISA) with a 96-well strip plate that is pre-coated with a monoclonal capture antibody. This kit specifically quantitates human MMP-9 from cell culture supernatant, serum, plasma, urine, saliva, and other biological fluids. It is analytically validated with ready-to-use reagents. Based on the properties of the antibodies that are utilized, this kit detects both the 92 kD pro-MMP-9 form and the mature 82 kD form, but not the 65 kD form. It can also detect both the native monomeric and dimeric pro-MMP-9 forms. This kit may be used for detecting MMP-9 in non-human primate samples.
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