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Pro-MMP-13, human recombinant protein
Matrix metalloproteinase-9
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P45452 |
|---|---|
| Concentration | 0.115, >200 munits/mg (international unit 1 mole/min/mg) |
| Calculated MW | 53.820 kDa |
| Gene ID | 4322 |
|---|---|
| Gene Symbol | MMP13 |
| Other Names | Collagenase 3 Collagenase 3 (EC 3.4.24.-) (Matrix metalloproteinase-13) (MMP-13) |
| Gene Source | Human |
| Source | Sf9 cells |
| Assay&Purity | SDS-PAGE; ≥95% |
| Assay2&Purity2 | HPLC; |
| Recombinant | Yes |
| Format | Liquid |
| Storage | -80°C; In 50 mM Tris pH 6.5, 250 mM NaCl, 5 mM CaCl2, 1 mM ZnCl2 |
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Provided below are standard protocols that you may find useful for product applications.
Background
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).
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