Description / human MMP-3 protein
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).
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| Size | 10 µg |
|---|---|
| Source | E. coli |
| Biological Activity | 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. |
| Purity Confirmation | > 98% by SDS-PAGE & HPLC analysis |
| Length [aa] | 378 |
| Molecular Weight | 42.8 kDa |
| Species Reactivity | Human |
| Formulation | lyophilized |
| Protein Sequence | MRTFPGIPKW RKTHLTYRIV NYTPDLP kDa VDSAVEKALK VWEEVTPLTF SRLYEGEADI MISFAVREHG DFYPFDGPGN VLAHAYAPGP GINGDAHFDD DEQWTKDTTG TNLFLVAAHE IGHSLGLFHS ANTEALMYPL YHSLTDLTRF RLSQDDINGI QSLYGPPPDS PETPLVPTEP VPPEPGTPAN CDPALSFDAV STLRGEILIF KDRHFWRKSL RKLEPELHLI S |
| Synonyms | MMP3; SL-1; STMY; STR1; CHDS6; MMP-3; STMY1 |
| Uniprot ID | P08254 |
| Protein RefSeq | NP_002413.1 |
| mRNA RefSeq | NM_002422.3 |