|Cat. No. :
|Product Overview :
||Recombinant Human CASP3 produced inE.Coliis a double, non-glycosylated, polypeptide chain cotaning 258 amino acids and having a molecular mass of 29.7 kDa. The Caspase-3 is fused to His-Tag at C-terminus and purified by proprietary chromatographic techniques.
||CASP3 is part of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspase-3 enzyme results in the execution-phase of cell apoptosis/programmed cell death. Caspase 3 has been called the "henchman that goes around and executes the cell." Caspase3 exists as an inactive proenzyme which undergoes proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. CSN-mediated deneddylation is regulated by active CASP3. CASP-3 cleavage of RAD51 results in a functional decrease in RAD51 strand exchange activity and inhibition of caspase 3 activity increases RAD51 protein levels.
|Amino Acid Sequence :
||SGISLDNSYK MDYPEMGLCI IINNKNFHKS TGMTSRSGTD VDAANLRETF RNLKYEVRNK NDLTREEIVE LMRDVSKEDH SKRSSFVCVL LSHGEEGIIF GTNGPVDLKK ITNFFRGDRC RSLTGKPKLF IIQACRGTEL DCGIETDSGV DDDMACHKIP VEADFLYAYS TAPGYYSWRN SKDGSWFIQS LCAMLKQYAD KLEFMHILTR VNRKVATEFE SFSFDATFHA KKQIPCIVSM LTKELYFYHH HHHHHHHH.
|Physical Appearance :
||Sterile Filtered clear solution.
||Greater than 90.0% as determined by both: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
||The Caspase3 solution (0.5 mg/ml) contains 50mM Hepes, pH-7.4 + 100 mM NaCl, 0.1% Chaps, 10 mM DTT & 10% glycerol.
|Protein Uses :
||Caspase-3 should be preincubated with 10 mM DTT at room temperature for one hour to fully reduce the enzyme, before cleavage begins. If product tolerates reduced conditions, assay can be carried out in 20 mM Hepes, pH-7.4 + 150 mM NaCl & 10 mM DTT.
||CASP3 Recombinant Human although stable at 4°C for 30 days, should be stored desiccated below -20°C for periods greater than 30 days. Please avoid freeze-thaw cycles.