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C1224

Sigma-Aldrich

Caspase 3 human

≥90% (SDS-PAGE), recombinant, expressed in E. coli (C-terminal histidine-tagged), buffered aqueous glycerol solution, ≥1.0 units/mg protein

Synonym(s):

Apopain, CPP32, Yama

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About This Item

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli (C-terminal histidine-tagged)

Quality Level

Assay

≥90% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

≥1.0 units/mg protein

mol wt

~30 kDa

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... CASP3(836)

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General description

Research area: Apoptosis

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.

This product may also be used in cell-based apoptosis 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.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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