Description / human MMP-2 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-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).
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| Size | 2 µg |
|---|---|
| Source | E. coli |
| Biological Activity | 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. |
| Purity Confirmation | > 90% by SDS-PAGE & HPLC analyses |
| Length [aa] | 552 |
| Molecular Weight | 62 kDa |
| Species Reactivity | Human |
| Formulation | lyophilized |
| Protein Sequence | MYNFFPRKPK WDKNQITYRI IGYTPDLDPE TVDDAFARAF QVWSDVTPLR FSRIHDGEAD IMINFGRWEH GDGYPFDGKD GLLAHAFAPG TGVGGDSHFD DDELWTLGEG QVVRVKYGNA DGEYCKFPFL FNGKEYNSCT DTGRSDGFLW CSTTYNFEKD GKYGFCPHEA LFTMGGNAEG QPCKFPFRFQ GTSYDSCTTE GRTDGYRWCG TTEDYDRDKK YGFCPETAMS TV |
| Synonyms | MMP2; CLG4; MONA; CLG4A; TBE-1; MMP-II |
| Uniprot ID | P08253 |
| Protein RefSeq | NP_004521.1 |
| mRNA RefSeq | NM_004530 |