Purified recombinant Human MMP2 protein Expression System: E.coli Bioactivity: MMP-2 activity was measured by its ability to cleave a chromogenic peptide MMP-2 substrate at room temperature. At an MMP-2 concentration of 2.5 µg/mL, 50 % cleavage was achieved at an incubation time of approximately 25 minutes.
Crystallography grade
MMP2
Spezies: Human
Wirt: Insektenzellen
Recombinant
>95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
WB, SDS, ELISA, Crys
Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-2 is a secreted collagenase with specificity toward Type IV, V, VII, and X collagens. Alternative Names: Matrix metalloproteinase-2 protein, MMP-2 protein, MMP2, Gelatinase A protein, MMP 2, MMP-2, MMP 2 protein, TBE-1 protein, MMP-2 protein