Matrix metalloproteinase-1 (MMP-1) is an endopeptidase that has a major role in tissue remodeling.1,2 It is composed of an N-terminal extracellular signal peptide, a prodomain containing a cysteine switch that interacts with the catalytic domain to regulate the proteolytic activity of MMP-1, a catalytic domain, and a C-terminal domain containing four hemopexin-like repeats which confer specificity for collagen.1 MMP-1 is ubiquitously expressed at low levels under normal physiological conditions and localizes to the extracellular space.2 It is primarily involved in the degradation of the extracellular matrix with type I collagen being its main substrate, but also degrades types II, III, V, IX, and X fibrillar collagens. MMP-1 also cleaves cell surface molecules such as insulin-like growth factor 1 (IGF-1) binding protein 3 (IGFBP3) and TNF-α.1 Knockdown of MMP1 inhibits the proliferation, migration, and invasion of colorectal cancer cells.3 MMP1 transgenic mice exhibit increased alveolar damage following exposure to M. tuberculosis.4 Polymorphisms of MMP1 are associated with several diseases, including various cancers, periodontitis, and coronary artery disease.2 Cayman’s MMP-1 (human, recombinant) protein can be used for enzyme activity applications. This protein consists of 461 amino acids and has a predicted N-terminus of Phe20 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 50-55 kDa.WARNING This product is not for human or veterinary use.
