anti-MT1-MMP Clone: 113-5B7,, Mouse Monoclonal Antibody, Each

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Specifically detects MT1-MMP Clone: 113-5B7 in Human, Mouse, Rabbit, Rat samples, and it is validated for Immunofluorescence, Immunohistochemistry (Paraffin), ImmunoprecipitationMatrix metalloproteinases (MMPs) are a family of enzymes that are responsible for the degradation of extracellular matrix components. Of the sixteen proteins reported to date, ten are normally found as soluble molecules. Several of the MMP proteins have been shown to be integral membrane proteins and have been named MT-MMPs for membrane bound MMP. The MT-MMP family is now known to contain at least three members, MT1-MMP, MT2-MMP and MT3-MMP, also known as MMP14, MMP15, and MMP16 respectively. While each of these proteins contain a C-terminal transmembrane domain allowing localization to the cell surface they are independent in expression. These proteins also differ from the other members of the MMP family in that they contain an 8 amino acid insert in the catalytic domain. The MT1-MMP protein is encoded by a 4.5 kb mRNA species giving rise to a protein with a molecular weight of 60-66kDa by SDS-PAGE. MT1-MMP is responsible for cleaving progelatinase A (MMP-2, 72kDa Type IV collagenase) and progelatinase B to their active forms. MT1-MMP itself requires an activation step that is the result of the activity of the membrane plasmin cascade. MT1-MMP functions by binding TIMP-2 and then the COOH terminal end of MMP-2 resulting in a 105kDa trimer which effects the cleavage of pro-MMP-2 to the biologically active form. The order of the binding of pro-MMP-2 and TIMP-2 to MT1-MMP is critical as TIMP-2 will also inhibit the activity of MMP-2 when present in a soluble form.