CASPASE 3 HUMAN >=90% (SDS-PAGE) RECOMBINANT EXPRESSED IN E. COLI (C-TERMINAL HISTIDINE-TAGGED) BUFFERED AQUEOUS GLYCEROL SOLUTI

General description

Human recombinant C-terminal histidine tagged caspase 3 is a fully active protein consisting of 17 kDa and 13.5 kDa subunits; the 13.5 kDa subunit contains the histidine tag.

Application

Caspase 3 human has been used to digest human r-vimentin. It has also been used in caspase-3 inhibition assay and protease inhibition assay.

Biochem/physiol Actions

Caspase 3 is a member of the CED-3 subfamily of caspases and is responsible for the cleavage of many key proteins such as the nuclear enzyme poly(ADP-ribose) polymerase (PARP), the inhibitor of caspase-activated deoxyribonuclease (ICAD), and gelsolin, a protein involved in apoptosis regulation. Caspase 3 is considered to be an effector caspase, activating pro-caspase 6 and pro-caspase 9 in vitro. Caspase 3 can be activated by caspase 8, caspase 6, and granzyme B.

Unit Definition

One unit will cleave 1.0 μmole of N-acetyl-Asp-Glu-Val-Asp-pNA per min at pH 7.4 at 25 °C.

Physical form

Solution in 10% (w/v) glycerol containing 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM DTT, 1 mM EDTA, 0.1% CHAPS

Preparation Note

Caspase 3 is synthesized as a 32 kDa proenzyme. The active enzyme is a heterodimer of two large (17 kDa) subunits and two small (12 kDa) subunits.

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