MMP-3

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) .

MMP3; SL-1; STMY; STR1; CHDS6; MMP-3; STMY1

4314

P08254

NP_002413.1

NM_002422.3

11q22.3

Human

Human

MRTFPGIPKW RKTHLTYRIV NYTPDLP kDa VDSAVEKALK VWEEVTPLTF SRLYEGEADI MISFAVREHG DFYPFDGPGN VLAHAYAPGP GINGDAHFDD DEQWTKDTTG TNLFLVAAHE IGHSLGLFHS ANTEALMYPL YHSLTDLTRF RLSQDDINGI QSLYGPPPDS PETPLVPTEP VPPEPGTPAN CDPALSFDAV STLRGEILIF KDRHFWRKSL RKLEPELHLI SSFWPSLPSG VDAAYEVTSK DLVFIFKGNQ FWAIRGNEVR AGYPRGIHTL GFPPTVRKID AAISDKEKNK TYFFVEDKYW RFDEKRNSME PGFPKQIAED FPGIDSKIDA VFEEFGFFYF FTGSSQLEFD PNAKKVTHTL KSNSWLNC

< 0.1 ng/µg of protein (< 1EU/µg)

> 98% by SDS-PAGE & HPLC analysis

MP-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.

378

Lyophilized

42.8 kDa

E. coli