MMP-1 proenzyme (human fibroblasts) | Enzo Life Sciences ALX-200-418-C005 product information

This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.

product summary

company name :

Enzo Life Sciences

other brands :

Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

product type :

protein

product name :

MMP-1 proenzyme (human fibroblasts)

catalog :

ALX-200-418-C005

quantity :

5 µg

citations: 9

Reference
Pilcher B, Dumin J, Sudbeck B, Krane S, Welgus H, Parks W. The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix. J Cell Biol. 1997;137:1445-57 pubmed
Vallon R, Muller R, Moosmayer D, Gerlach E, Angel P. The catalytic domain of activated collagenase I (MMP-1) is absolutely required for interaction with its specific inhibitor, tissue inhibitor of metalloproteinases-1 (TIMP-1). Eur J Biochem. 1997;244:81-8 pubmed
Wilhelm S, Eisen A, Teter M, Clark S, Kronberger A, Goldberg G. Human fibroblast collagenase: glycosylation and tissue-specific levels of enzyme synthesis. Proc Natl Acad Sci U S A. 1986;83:3756-60 pubmed
Hasty K, Hibbs M, Kang A, Mainardi C. Secreted forms of human neutrophil collagenase. J Biol Chem. 1986;261:5645-50 pubmed
Nagase H, Enghild J, Suzuki K, Salvesen G. Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate. Biochemistry. 1990;29:5783-9 pubmed
Suzuki K, Enghild J, Morodomi T, Salvesen G, Nagase H. Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin). Biochemistry. 1990;29:10261-70 pubmed
Nagase H, Suzuki K, Enghild J, Salvesen G. Stepwise activation mechanisms of the precursors of matrix metalloproteinases 1 (tissue collagenase) and 3 (stromelysin). Biomed Biochim Acta. 1991;50:749-54 pubmed
Knight C, Willenbrock F, Murphy G. A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases. FEBS Lett. 1992;296:263-6 pubmed
Masui Y, Takemoto T, Sakakibara S, Hori H, Nagai Y. Synthetic substrates for vertebrate collagenase. Biochem Med. 1977;17:215-21 pubmed

product information

Product ID :

ALX-200-418

Catalog Number :

ALX-200-418-C005

Product Name :

MMP-1 proenzyme (human fibroblasts)

Product Type :

Protein

Size :

5 µg

list of Pubmed id :

9182674, 9063449, 3012533, 3007518, 2383557, 2176865, 1666284, 1537400, 193489

Background :

MMP-1, the classical matrix metalloproteinase, is expressed by a large number of cell types. As an example, in basal keratinocytes migrating across the dermal matrix the enzyme is invariably expressed and cleaves fibrilliar collagen type I. It was shown that the interaction of the α2β1 integrin with dermal collagen mediates induction of MMP-1 in keratinocytes at the onset of healing and that the activity of MMP-1 is needed to initiate cell movement. The cleavage of dermal collagen provides keratinocytes with a mechanism to maintain their directionality during reepithelialization (Pilcher et al. 1997). The MMP-1 zymogens of ~56/52kDa can be activated by a stepwise mechanism through which sequential processing events occur in the propeptide region. Both proenzymes can be activated by limited digestion with trypsin or by treatment with APMA generating their respective active enzyme forms of ~46/42kDa (Wilhelm et al. 1986).

ALTnames :

Matrix metalloproteinase 1, Interstitial collagenase, Fibroblast collagenase

Purity :

≥90% (SDS-PAGE, Western blot)

Buffer :

Liquid. In 50mM TRIS-HCl, pH 7.0, 300mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ35 and 0.05% sodium azide.

Storage :

-80°C