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C8726

Sigma-Aldrich

Caspase 9 human

≥90% (SDS-PAGE), recombinant, expressed in E. coli (C-terminal histidine-tagged), buffered aqueous solution, >2,000 units/mg protein

Synonym(s):

ICE-Lap6, Mch6

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About This Item

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204

recombinant

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

Quality Level

Assay

≥90% (SDS-PAGE)

form

buffered aqueous solution

specific activity

>2,000 units/mg protein

mol wt

N-terminal prodomain plus the large subunit. 36 kDa (caspase 9 expressed as a C-terminal histidine-tagged protein appears as a two-subunit protein)
small subunit 13 kDa (subunit containing the histidine tag)

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... CASP9(842)

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Biochem/physiol Actions

When cells receive apoptotic stimuli, such as activation of the TNFα/Fas cell surface receptor, caspase 8 activation, Bid processing and its translocation to the mitochondria ensue. As a result mitochondria release cytochrome c which then binds to Apaf-1, the mammalian Ced-4 homologue, together with dATP. The resultant complex recruits caspase 9 leading to its activation. It then cleaves downstream caspases such as caspase 3, 6, and 7, initiating the caspase cascade. Caspase 9 exhibits basal activity. It can be further activated via interaction of its N-terminal prodomain with the activator protein Apaf-1 in the presence of cytochrome c and dATP. Caspases have been implicated in many disorders including cancer, inflammatory disease, neurodegenerative diseases, stroke and myocardial infarction.

Unit Definition

One unit will cleave 1.0 nmol of Ac-Leu-Glu-His-Asp-AFC per hr at 25 °C at pH 6.5.

Physical form

Solution in 10% sucrose containing 50 mM HEPES, pH 7.5, 5 mM DTT, 0.1% CHAPS, 1 mM EDTA, 50 mM NaCl.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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K Kuida
The international journal of biochemistry & cell biology, 32(2), 121-124 (2000-02-25)
Caspase-9 is a member of caspase family of cysteine proteases that have been implicated in apoptosis and cytokine processing. When cells receive apoptotic stimuli, mitochondria releases cytochrome c which then binds to Apaf-1, the mammalian Ced-4 homologue, together with dATP.
H Duan et al.
The Journal of biological chemistry, 271(28), 16720-16724 (1996-07-12)
Members of the ICE/Ced-3 gene family are likely effector components of the cell death machinery. Here, we characterize a novel member of this family designated ICE-LAP6. By phylogenetic analysis, ICE-LAP6 is classified into the Ced-3 subfamily which includes Ced-3, Yama/CPP32/apopain
S M Srinivasula et al.
The Journal of biological chemistry, 271(43), 27099-27106 (1996-10-25)
Recent evidence suggests that CPP32 is an essential component of an aspartate-specific cysteine protease (ASCP) cascade responsible for apoptosis execution in mammalian cells. Activation of CPP32 could lead to activation of other downstream ASCPs, resulting in late morphological changes such
H R Stennicke et al.
The Journal of biological chemistry, 274(13), 8359-8362 (1999-03-20)
The recombinant form of the proapoptotic caspase-9 purified following expression in Escherichia coli is processed at Asp315, but largely inactive; however, when added to cytosolic extracts of human 293 cells it is activated 2000-fold in the presence of cytochrome c
BCL-2 family members and the mitochondria in apoptosis.
A Gross et al.
Genes & development, 13(15), 1899-1911 (1999-08-13)

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