Description of Target: Produced in E. coli. Active Matrix Metalloproteinase-10 (MMP-10, stromelysin-2, transin-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-10 (Phe99-Glu271, NM_2425) with a C-terminal purification tag. This comprises an active form of MMP-10 which lacks the C-terminal hemopexin domain. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected.
Key Reference: Paxillin-mediated recruitment of calcineurin to the contractile ring is required for the correct progression of cytokinesis in fission yeast: R. Martin-Garcia, et al.; Cell Rep. 25, 772 (2018)
Matrix metalloproteinase-10 is a critical effector of protein kinase Ciota-Par6alpha -mediated lung cancer: L.A. Frederick, et al.; Oncogene 27, 4841 (2008).
Molecular Weight: 19 kDa.
Product Format: Liquid. 50mM TRIS (pH 7.5) containing 5mM calcium chloride, 300mM sodium chloride, 20uM zinc chloride, 0.5% Brij-35, and 30% glycerol.
Protein Name: Stromelysin-2.
Purification: Partially purified by single-step affinity chromatography and gel filtration.
Source: E. Coli.