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)
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.
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
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
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.
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.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
