Description / human MMP-1 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-1 is a secreted collagenase with specificity toward Type I, II, III, VII, and X collagens. Recombinant human MMP-1 is a 42.7 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain which is involved in substrate specificity and in binding TIMP-1.
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| Size | 2 µg |
|---|---|
| Source | E. coli |
| Biological Activity | MMP-1 activity was measured by its ability to cleave a chromogenic peptide MMP-1 substrate at room temperature. At an MMP-1 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 analysis |
| Length [aa] | 371 |
| Molecular Weight | 42.7 kDa |
| Species Reactivity | Human |
| Formulation | lyophilized |
| Protein Sequence | MFVLTEGNPR WEQTHLTYRI ENYTPDLPRA DVDHAIEKAF QLWSNVTPLT FTKVSEGQAD IMISFVRGDH RDNSPFDGPG GNLAHAFQPG PGIGGDAHFD EDERWTNNFR EYNLHRVAAH ELGHSLGLSH STDIGALMYP SYTFSGDVQL AQDDIDGIQA IYGRSQNPVQ PIGPQTPKAC DSKLTFDAIT TIRGEVMFFK DRFYMRTNPF YPEVELNFIS VFWPQLPNGL EA |
| Synonyms | Matrix metalloproteinase-1, fibroblast collagenase, interstitial collagenase |
| Uniprot ID | P03956 |
| Protein RefSeq | NP_002412.1 |
| mRNA RefSeq | NM_002421.3 |