Mouse MMP2 protein, His tag (active)

GeneTex

Mouse MMP2 protein (active)

9

MMP2 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, 72kDa 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 MMP2 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 MMP2 protein was as a negative control, and blood sample was as a positive control.

Functional Assay

Research Use Only

Unconjugated

Lyophilized

72 kDa type IV collagenase

This gene encodes a member of the matrix metalloproteinase family of extracellular matrix-degrading enzymes that are involved in tissue remodeling, wound repair, progression of atherosclerosis and tumor invasion. The encoded preproprotein undergoes proteolytic processing to generate a mature, zinc-dependent endopeptidase enzyme that hydrolyzes collagens, gelatins, laminin, fibronectin and elastin. Mice lacking the encoded protein exhibit suppressed angiogenesis and attenuated features of human multicentric osteolysis with arthritis including abnormal skeletal and craniofacial development. [provided by RefSeq, Feb 2016]

-20°C or -80°C,2°C to 8°C

12352204