Recombinant Human MMP-3
Catalog Number : 420-03
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-3 degrades fibronectin, laminin, collagens III, IV, and X, and cartilage proteoglycans. Recombinant human MMP-3 is a 42.8 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (378 amino acids).
Above 98% as determined by SDS-PAGE Analysis.
MMP-3 activity was measured by its ability to cleave a chromogenic peptide MMP-3 substrate at room temperature. At a MMP-3 concentration of 2.5 μg/ml, 50% cleavage was achieved at an incubation time of approximately 75 minutes.
MRTFPGIPK WRKTHLTYR IVNYTPDLP KDAVDSAVE KALKVWEEV TPLTFSRLY EGEADIMIS FAVREHGDF YPFDGPGNV LAHAYAPGP GINGDAHFD DDEQWTKDT TGTNLFLVA AHEIGHSLG LFHSANTEA LMYPLYHSL TDLTRFRLS QDDINGIQS LYGPPPDSP ETPLVPTEP VPPEPGTPA NCDPALSFD AVSTLRGEI LIFKDRHFW RKSLRKLEP ELHLISSFW PSLPSGVDA AYEVTSKDL VFIFKGNQF WAIRGNEVR AGYPRGIHT LGFPPTVRK IDAAISDKE KNKTYFFVE DKYWRFDEK RNSMEPGFP KQIAEDFPG IDSKIDAVF EEFGFFYFF TGSSQLEFD PNAKKVTHT LKSNSWLNC
|Research Interest:||Cancer, Angiogenesis, Bone Biology|
|Protein Cross Reactivity:||NULL|