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, Ile169~Glu387
Application Notes:
MMP9 is a zinc-dependent enzymes capable of cleaving components of the extracellular matrix, which belongs to the matrix metalloproteinase (MMP) family. It is a gelatinase A, 92kDa type IV collagenase which can hydrolyze gelatin under certain conditions. Gelatin zymography is mainly used for the detection of the gelatinases, MMP-2 and MMP-9 and It is extremely sensitive because levels of 10pg of MMP-2 can already be detected. Briefly, various concentrations of recombinant pig MMP9 (1000 ng, 500 ng, 100 ng, 10 ng, 1ng, 0.1 ng) were denatured by SDS loading buffer, electrophoresed through sodium dodecylsulphate- polyacrylamide gel (SDS-PAGE, 10% gels) containing gelatin (1 mg/ml) with nonreducing conditions. After renaturation, incubation and CCB-stained, active MMP2 would hydrolyze gelatin nearby, which was indicated by the white binds on the gel. In the experiment, using a heat-denatured MMP9 protein was as a negative control, and blood sample was as a positive control.
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