C8726
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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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
Activation of caspase-9 (CASP9) through apoptotic stimuli initiates the caspase cascade. Caspases have been implicated in many disorders including cancer, inflammatory disease, neurodegenerative diseases, stroke and myocardial infarction.
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
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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
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
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.
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
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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