Cell-based assay to quantify human MMP9, involved in both normal and pathological tissue remodeling, immunity, and inflammation.
Cisbio's Human MMP9 assay is designed to measure the concentrations of MMP-9 (pro- and active forms) in cell culture supernatants of human origin.
Matrix metalloproteinase (MMP) 9, also known as gelatinase B, is a zinc-dependent endopeptidase secreted as an inactive proenzyme which is then activated by proteolytic cleavage. MMP9 plays a significant role in tissue repair and remodeling by degrading structural components of the extracellular matrix (ECM), such as collagens, gelatin, and elastin. This endopeptidase also has crucial functions in cell growth, migration, inflammation, and angiogenesis by processing a variety of non-ECM molecules such as cytokines and chemokines (e.g. pro-TGF-β, pro-TNF-α, CXCL1, CXCL8, IFN-β).
Its enzymatic activity is regulated by interaction with its physiological inhibitors, the tissue inhibitors of metalloproteinases TIMP1 and TIMP2, that block the access of substrates to the catalytic domain of the enzyme.
MMP-9 is mainly regulated at the level of transcription by several growth factors, cytokines, and bacterial products including LPS.
Upregulation of MMP9, leading to MMP9-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.