HTRF Human MMP2 assay is designed to measure the concentrations of MMP2 (pro- and active forms) in cell culture supernatants of human origin. Matrix metalloproteinase (MMP) 2, also known as gelatinase A, is a zinc-dependent endopeptidase secreted as an inactive proenzyme that is then activated by proteolytic cleavage. MMP2 plays a significant role in tissue repair and remodeling by degrading structural components of the extracellular matrix (ECM), such as collagens, gelatin, and fibronectin. This endopeptidase also plays a major role in cell growth, migration, inflammation, and angiogenesis, by processing a variety of non-ECM substrates such as cytokines and chemokines (e.g. pro-TGF-β, pro-IL-1β, pro-TNF-α, CXCL12, CCL7, CX3CL1). Its enzymatic activity is regulated by interaction with its physiological inhibitors, the tissue inhibitors of metalloproteinases TIMP1 and TIMP2, which block the access of substrates to the catalytic domain of the enzyme. MMP2 is mainly regulated at the level of transcription by several cytokines and growth factors, including TGF-β. Upregulation of MMP2, leading to MMP2-TIMP1/2 imbalances, has been linked to tissue fibrosis, cancer, diabetes, arthritis, and cardiovascular diseases. The secretion of this biomarker is therefore a common end point measured when investigating such diseases and to find new drugs.