MMP-1 (human, recombinant)

Collagenase-1|Fibroblast Collagenase|Interstitial Collagenase|Matrix Metalloproteinase-1

Matrix metalloproteinase-1 (MMP-1) is an endopeptidase that has a major role in tissue remodeling.{61761,61762} 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.{61761} MMP-1 is ubiquitously expressed at low levels under normal physiological conditions and localizes to the extracellular space.{61762} 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.{61761} Knockdown of MMP1 inhibits the proliferation, migration, and invasion of colorectal cancer cells.{61763} MMP1 transgenic mice exhibit increased alveolar damage following exposure to M. tuberculosis.{61764} Polymorphisms of MMP1 are associated with several diseases, including various cancers, periodontitis, and coronary artery disease.{61762} 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.

-80

-80

Lyophilized from sterile 25 mM MES, pH 5.5, with 10 mM calcium chloride, 150 mM sodium chloride, and 0.05% Brij 35

365

≥96% estimated by SDS-PAGE