MilliporeSigma™ anti-MT1-MMP Clone: 113-5B7,

Description

• Specifically detects MT1-MMP Clone: 113-5B7 in Human, Mouse, Rabbit, Rat samples, and it is validated for Immunofluorescence, Immunohistochemistry (Paraffin), Immunoprecipitation Matrix 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.