MMP2 (Matrix Metalloproteinase 2), also known as gelatinase A, is a zinc-dependent endopeptidase belonging to the matrix metalloproteinase family. It plays a critical role in degrading extracellular matrix (ECM) components, particularly gelatin and type IV collagen, facilitating tissue remodeling, wound healing, and pathological processes like cancer metastasis, inflammation, and angiogenesis. MMP2 is synthesized as an inactive pro-enzyme (pro-MMP2) that requires proteolytic activation, often involving membrane-type MMPs (MT-MMPs) and tissue inhibitors of metalloproteinases (TIMPs). Dysregulation of MMP2 expression or activity is linked to tumor invasion, cardiovascular diseases, and autoimmune disorders.
MMP2 antibodies are essential tools for detecting and quantifying MMP2 in research and diagnostics. These antibodies are commonly used in techniques like Western blotting, immunohistochemistry (IHC), immunofluorescence (IF), and ELISA to study MMP2 expression patterns, localization, and activation in cells, tissues, or biological fluids. Polyclonal and monoclonal MMP2 antibodies target specific epitopes, such as the catalytic domain or propeptide region, enabling differentiation between latent and active enzyme forms. Validated antibodies are critical for ensuring specificity, as cross-reactivity with other MMPs (e.g., MMP9) can occur. Applications include investigating MMP2's role in disease mechanisms, therapeutic target validation, and biomarker studies. Proper controls, such as MMP2-knockout samples or siRNA-mediated silencing, are recommended to confirm antibody reliability.