Reconstitute with 20mM Tris and 150mM NaCl to 0.1-1.0mg/ml. Do not vortex. Lyophilized from 20mM Tris, 150mM NaCl, 1mM EDTA, 1mM DTT, 0.01% SKL, 5% Trehalose, ProClin 300.
Expression System:
E. coli
Form:
Lyophilized powder
Sequence:
N-terminal His-Tag, Glu103~Leu290 (NP_002418.1)
Application Notes:
Matrix Metalloproteinase 13 (MMP13) is a member of the matrix metalloproteinase (MMP) family. MMP13 has been proposed to participate in aggrecan degradation associated with osteoarthritis and cleavage of type II collagen in osteoarthritic cartilage explants and in tumor progression and metastasis. MMP13 is likely to play a crucial role in the modulation of extracellular matrix degradation and cell-matrix interactions. In addition, it can cleave type I, III, IV, IX, X and XIV collagens and fibronectin. Thus we have chosed casein-zymography to measure the activity of MMP13. Briefly, various concentrations of MMP13 (10 µg, 5 µg, 1 µg, 0.1 µg, 0.01 µg) were denatured by SDS loading buffer, electrophoresed through sodium dodecylsulphat-polyacrylamide gel (SDS-PAGE, 15% gels) containing casein (1 mg/mL) with nonreducing conditions. After renaturation, incubation and CCB-stained, active MMP13 would hydrolyze casein nearby, which was indicated by the white bands on the gel. In the experiment, using a heat-denatured MMP13 protein was as a negative control, and trypsase (1µg/ml) was as a positive control.
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