Lyophilized from sterile PBS, pH 7.4, 5 % trehalose and 5 % mannitol.
Bio-activity
Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2, (AnaSpec, Cat#27076). The specific activity is>800 pmoles/min/μg. (Activation description: The proenzyme needs to be activated by APMA for an activated form)
Molecular Mass
Recombinant Human MMP9 consisting of 699 amino acids has a predicted molecular mass of 77.7 kDa. The apparent molecular mass of rhMMP9 is approximately 80-95 kDa in SDS-PAGE due to glycosylation.
Endotoxin
< 1.0 EU per 1 microgram of protein (determined by LAL method).
Purity
> 98 % by SDS-PAGE.
BACKGROUND
Background
Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (PubMed:17650508).
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