C6607
Caspase 10 human
>90% (SDS-PAGE), recombinant, expressed in E. coli, lyophilized powder, 8,000 units/mg protein (Bradford)
Synonym(s):
Flice2, Mch4
Product Name
Caspase 10 human, >90% (SDS-PAGE), recombinant, expressed in E. coli, lyophilized powder, 8,000 units/mg protein (Bradford)
recombinant
expressed in E. coli
assay
>90% (SDS-PAGE)
form
lyophilized powder
specific activity
8,000 units/mg protein (Bradford)
mol wt
~30 kDa
solubility
PBS: soluble
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Quality Level
Gene Information
human ... CASP10(843)
Biochem/physiol Actions
Caspase 10 has two death effector domains (DEDs) that bind to the DED in the adapter molecule FADD and recruits both TNFR1 and CD95 to form complexes with these receptors. Caspase 10 cleaves and activates caspases 3, 4, 6, 7, 8 and 9 which causes the proteolytic cleavage of many key proteins such as PARP. Based on gene expression studies, caspase 10 may be crucial in embryonic development. In view of its structural homology to caspase 8, the initiator caspase in death receptor-mediated apoptosis, caspase 10 may function in a similar and redundant manner.
Other Notes
One unit will hydrolyze 1 nmol of the caspase substrate IETD-pNA to IETD and p-nitroaniline per hour at pH 7.2 at 37 °C.
Physical form
Lyophilized powder containing 0.052% ammonium sulfate, 0.158% Tris−HCl, and 0.76% sodium chloride.
Storage Class
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Caspases: the executioners of apoptosis.
Cohen, G.M.
Biochemistry, 326 (part 1), 1-1 (1997)
Marcin Poreba et al.
Nature protocols, 12(10), 2189-2214 (2017-09-22)
Many biologically and chemically based approaches have been developed to design highly active and selective protease substrates and probes. It is, however, difficult to find substrate sequences that are truly selective for any given protease, as different proteases can demonstrate
Marcin Poreba et al.
Nature protocols, 12(10), 2189-2214 (2017-09-22)
Many biologically and chemically based approaches have been developed to design highly active and selective protease substrates and probes. It is, however, difficult to find substrate sequences that are truly selective for any given protease, as different proteases can demonstrate
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