Matrix metalloproteinase 7 (MMP7), also known as matrilysin, is a member of the zinc-dependent endopeptidase family involved in extracellular matrix (ECM) remodeling. It primarily degrades components like elastin, fibronectin, and proteoglycans, playing roles in tissue repair, inflammation, and cancer progression. MMP7 is secreted as an inactive zymogen and activated via proteolytic cleavage. Unlike other MMPs, it lacks a hemopexin domain, contributing to its compact structure and substrate specificity.
MMP7 antibodies are essential tools for detecting and quantifying MMP7 expression in research and diagnostics. They are widely used in techniques such as Western blotting, immunohistochemistry, and ELISA to study MMP7's involvement in pathological processes. Elevated MMP7 levels are linked to tumor invasion, metastasis, and poor prognosis in cancers (e.g., colorectal, pancreatic, and breast cancers), as well as fibrotic and inflammatory diseases.
Clinically, MMP7 antibodies aid in developing therapeutic strategies, including inhibitory drugs or antibody-based therapies targeting MMP7 overexpression. However, challenges remain due to MMP7's dual role in both promoting disease and maintaining tissue homeostasis. Ongoing research focuses on understanding its regulatory mechanisms and context-dependent functions to refine therapeutic targeting.