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. Recombinant human MMP-2 is a 62.0 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).
Size
Various Sizes
Concentration
n/a
Applications
Cell Culture
Other Names
72 kDa type IV collagenase;3.4.24.24;72 kDa gelatinase;Gelatinase A;Matrix metalloproteinase-2;MMP-2;TBE-1;PEX;MMP2;CLG4A; Matrix metalloproteinase-2; Gelatinase A, TBE-1