MMP-1 Native Protein Summary
Description |
Collagenases are enzymes that break the peptide bonds in collagen, and are useful in structural and functional studies of collagen metabolism. Collagenase Type I has average levels of collagenase, caseinase, clostripain, and tryptic activities, and is well-suited for the digestion of fat, adrenal, and liver cells or tissues. |
Details of Functionality |
This protein was produced in an in vitro wheat germ expression system that should preserve correct conformational folding that is necessary for biological function. While it is possible that this protein could display some level of activity, the functionality of this protein has not been explicitly measured or validated. |
Source |
Clostridium histolyticum |
Protein/Peptide Type |
Native Protein |
Gene |
MMP1 |
Purity |
>90% |
Applications/Dilutions
Dilutions |
- Bioactivity
- Enzyme Activity
|
Packaging, Storage & Formulations
Storage |
Store at 4C. Do not freeze. |
Preservative |
No Preservative |
Concentration |
LYOPH |
Purity |
>90% |
Reconstitution Instructions |
Primary cell isolation, culture and tissue dissociation: Reconstitute in balanced salt solutions at concentrations from 0.05% to 0.5% (w/v). Enzymetic assay: Reconstitute in 0.05 M TES buffer with 0.36 mM CaCl2, pH 7.5 (concentration of 1.0 mg/ml) |
Notes
This product is produced by and distributed for Abnova, a company based in Taiwan.
Alternate Names for MMP-1 Native Protein
Background
Human interstitial collagenase (matrix metalloproteinase-1, MMP-1), an enzyme whose only known physiologic substrate has heretofore been believed to be the extracellular matrix molecule, collagen. Data indicate that matrix metalloproteinase-1 displays an expanded substrate repertoire that supports the existence of a new interface between connective tissue turnover and serine proteinase inhibitors (1). It has been shown that the MMP-1 functions as a protease agonist of Protease-activated receptors (PAR1) cleaving the receptor at the proper site to generate PAR1-dependent Ca2+ signals and migration. These results demonstrate that MMP-1 in the stromal-tumor microenvironment can alter the behavior of cancer cells through PAR1 to promote cell migration and invasion (2). It has also been suggested that increased levels of MMP-1 due to tobacco smoking plays a major role in the aging process of skin since MMP-1 degrades collagen, which accounts for at least 70% of the dry weight of dermis. Significantly more MMP-1 has been detected in the skin of smokers than non-smokers whereas no difference was seen for the tissue inhibitor of metalloproteinases 1 (3).
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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