MMP 1 Human, HEK

Matrix Metalloproteinase-1 (MMP-1), also known as interstitial collagenase or fibroblast collagenase, is a member of the matrix metalloproteinase (MMP) family. These enzymes are involved in the breakdown of extracellular matrix (ECM) components, playing crucial roles in various physiological and pathological processes, including tissue remodeling, embryonic development, and disease progression such as arthritis and cancer metastasis .

MMP-1 is a zinc-dependent endopeptidase that primarily degrades interstitial collagens, including types I, II, and III . It can also degrade a broad range of other substrates such as types VII, VIII, and X collagens, casein, gelatin, myelin basic protein, L-selectin, pro-TNF, IL-1β, IGFBP-3, IGFBP-5, pro-MMP-2, and pro-MMP-9 . The enzyme is secreted as an inactive pro-protein and is activated upon cleavage by extracellular proteinases .

MMP-1 is expressed by various cell types, including fibroblasts, keratinocytes, endothelial cells, monocytes, and macrophages . Its expression is tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational modifications. Factors such as cytokines, growth factors, and mechanical stress can influence MMP-1 expression .

Human recombinant MMP-1 is often produced in HEK 293 cells, a human embryonic kidney cell line, to ensure proper post-translational modifications and biological activity . The recombinant enzyme is typically purified to high levels of purity (>95% as determined by SDS-PAGE) and is available in various forms, including lyophilized powder and buffered aqueous solutions .

Recombinant MMP-1 is widely used in research to study ECM remodeling, cell migration, and invasion. It is also utilized in assays to screen for MMP inhibitors, which are potential therapeutic agents for diseases involving excessive ECM degradation .