Pro-MMP-13, human recombinant

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).