Human MMP9 protein, His tag (Active)

GeneTex

Human MMP9 protein, His tag (Active)

9

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 human MMP9 (1000ng, 500ng, 100ng, 10ng) 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 this experiment we use heat-denatured MMP9 protein as negative control, and blood sample as positive control.

Research Use Only

Unconjugated

Lyophilized

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [provided by RefSeq, Jul 2008]

-20°C or -80°C,2°C to 8°C

12352204