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Product Description
MMP-13 (Collagenase-3) was first identified in human mammacarcinoma (Freije et al., 1994, Willmroth et al. 1998) - probably induced by IL1- alpha and IL-1 beta - and shown to be glycosylated and the inactive zymogen displaying a relative molecular weight of 60 kDa. Cleavage of the 84 residue propeptide can be catalysed by other MMPs such as MMP-2, MMP-3 and MMP-14, or by factors like plasmin. The proenzyme activated by APMA (paminohenylmercuric acteate) or leads to the active enzyme with a relative molecular weight of app. 48 kDa which easily autodegrades into a 30 kDa form. This highly active 30 kDa form still retains the characteristics of the app. 48 kDa form. MMP-13 also plays a central role in the MMP activation cascade, both activating and being activated by several MMPs (Leeman et al., 2002).
Biovision | 7785 | Pro-MMP-13 human recombinant DataSheet
Biomolecule/Target: N/A
Synonyms: Matrix metalloproteinase-9
Alternates names: Collagenase 3 Collagenase 3 (EC 3.4.24.-) (Matrix metalloproteinase-13) (MMP-13)
Taglines: A Protein involved in breakdown of extracellular matrix
NCBI Gene ID #: 8600
NCBI Gene Symbol: OPGL
Gene Source: Human
Accession #: O14788
Recombinant: Yes
Source: Sf9 cells
Purity by SDS-PAGEs: 98%
Assay: SDS-PAGE
Purity: N/A
Assay #2: HPLC
Endotoxin Level: N/A
Activity (Specifications/test method): N/A
Biological activity: The ED as determined by the dose-dependent stimulation of IL-8 production by human PBMC is <10 ng/ml.
Results: N/A
Binding Capacity: N/A
Unit Definition: N/A
Molecular Weight: 53.820 kDa
Concentration: 115 µg/ml, >200 munits/mg (international unit 1 mole/min/mg)
Appearance: Liquid
Physical form description: In 50 mM Tris pH 6.5, 250 mM NaCl, 5 mM CaCl2, 1 mM ZnCl2
Reconstitution Instructions: Reconstitute in HO to a concentration of 0.1-1.0 mg /ml. The solution can then be diluted into other aqueous buffers and stored at 4°C for 1 week or 20°C for future use.
Amino acid sequence: N/A
