Matrix Metalloproteinase-28 (MMP28), also known as epilysin, is a member of the MMP family of zinc-dependent endopeptidases involved in extracellular matrix (ECM) remodeling, tissue repair, and immune regulation. Unlike many MMPs, MMP28 is expressed in normal tissues, including skin, lungs, and testes, and is implicated in both physiological processes (e.g., epithelial homeostasis) and pathological conditions like fibrosis, cancer, and inflammation. Its unique structure, featuring a furin-like prodomain, allows intracellular activation, distinguishing it from other MMPs requiring extracellular proteolytic cleavage.
MMP28 antibodies are essential tools for detecting and studying the protein's expression, localization, and function. These antibodies, often polyclonal or monoclonal, target specific epitopes within MMP28's catalytic or hemopexin domains. They are widely used in techniques such as Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to investigate MMP28's role in diseases. For example, studies using MMP28 antibodies have linked its overexpression to tumor progression in certain cancers and its dysregulation to fibrotic lung diseases. Validated antibodies with high specificity are critical, as cross-reactivity with other MMPs can complicate interpretation. Ongoing research aims to clarify MMP28's dual roles in tissue repair versus pathological remodeling, highlighting the antibody's importance in mechanistic and therapeutic exploration.