||Recombinant Human CASP4 was produced inE. coli.
||Caspase-4 is a member of the caspase family of cysteine proteases. It exists in cells as an inactive pro-enzyme. The pro-enzyme is matured by proteolysis to yield large and small subunits. The active enzyme is a heterotetramer consisting of two large and two small subunits. The expressed caspase-4 spontaneously undergoes auto-processing to yield subunits characteristic of the native enzyme. The active caspase-4 is routinely tested for its ability to enzymatically cleave the substrate WEHD-AFC or WEHD-pNA.
||Reconstitute with PBS containing 15% glycerol to 1U/µl.
||~5"000U/mg protein. One unit is defined as the amount of enzyme that cleaves 1nmol of the caspase substrate WEHD-pNA per hour at 37°C in reaction solution containing 50mM HEPES, pH 7.2, 50mM NaCl, 0.1% CHAPS, 10mM EDTA, 5% glycerol and 10mM DTT.
||Useful in screening caspase inhibitors, studying enzyme regulation and kinetics, determining target substrate or as a positive control in caspase activity assays. We recommend using 1 unit per assay for analyzing caspase activity.
||Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and store at -80℃.