|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|
email@example.com, and receive a free "I Love Antibodies" mug.
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).
If you have any additional inquiries please email technical services at firstname.lastname@example.org.