Matrix Metalloproteinase 13, Recombinant, Human (Matrix Metalloproteinase-13, MMP13, MMP-13, Collagenase 3)

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 60kD. 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. 48kD which easily autodegrades into a 30kD form. This highly active 30kD form still retains the characteristics of the app. 48kD 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).\n\nThis product contains neither an N- nor C-terminal tag. This product is APMA activated, which had been removed after activation employing SEC and dialysis.\n\nSource:\nRecombinant corresponding to full-length human MMP-13 expressed in Sf9 cells.\n\nMolecular Weight:\n~53.82kD (471aa residues)\n\nActivation:\nIt has been shown that the proform of MMP-13 can be activated by plasmin and by the two matrix metalloproteinases MMP-2 and MMP-14 . Extended plasmin-activation can deactivate active MMP-13. The proenzyme activated by APMA (p-aminophenylmercuric acetate), yields the active enzyme with a relative molecular weight of 48kD which easily autodegrades into a 30kD form. This highly active 30kD form still retains the characteristics of the 48kD form. Indeed, it cleaves the type II collagen, displays the gelatinolytic activity and is inhibited by the tissue inhibitor of matrix metalloproteinases (TIMP-1, 2, and 3) and by EDTA.\n\nInhibitors:\nN,N'-bisaryl-pyrimidine-4,6-dicarboxamide derivatives are indicated to be selective for MMP- 13 inhibition (Engel et al., 2005). N-Hydroxy-3-hydroxy-4-arylsulfonyltetrahydropyranyl-3- carboxamides were designed as novel inhibitors of MMP-13 and aggrecanase based on known endocyclic hydroxamate inhibitors of matrix metalloproteinases (Noe et al., 2004). The activated MMP-13 is inhibited by tissue inhibitors of matrix metalloproteinase-1, -2, and -3 and by chelators of divalent cations like EDTA or o-phenanthroline.\n\nStorage and Stability:\nAliquot to avoid repeated freezing and thawing and store at -70 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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