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C6607

Sigma-Aldrich

Caspase 10 human

>90% (SDS-PAGE), recombinant, expressed in E. coli, lyophilized powder, 8,000 units/mg protein (Bradford)

Synonym(e):

Flice2, Mch4

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About This Item

MDL-Nummer:
MFCD03456342
UNSPSC-Code:
12352200
NACRES:
NA.32

Rekombinant

expressed in E. coli

Qualitätsniveau

200

Assay

>90% (SDS-PAGE)

Form

lyophilized powder

Spezifische Aktivität

8,000 units/mg protein (Bradford)

Mol-Gew.

~30 kDa

Löslichkeit

PBS: soluble

UniProt-Hinterlegungsnummer

Q92851

Versandbedingung

dry ice

Lagertemp.

−70°C

Angaben zum Gen

human ... CASP10(843)

Biochem./physiol. Wirkung

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.

Einheitendefinition

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.

Physikalische Form

Lyophilized powder containing 0.052% ammonium sulfate, 0.158% Tris−HCl, and 0.76% sodium chloride.

Lagerklassenschlüssel

10 - Combustible liquids

WGK

nwg

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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Die Dokumentenbibliothek aufrufen

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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