|Concentration||0.115, >200 munits/mg (international unit 1 mole/min/mg)|
|Calculated MW||53.820 kDa|
|Other Names||Collagenase 3 Collagenase 3 (EC 3.4.24.-) (Matrix metalloproteinase-13) (MMP-13)|
|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.
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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