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Human CASP10 / Caspase 10 Recombinant Protein - LS-G4177


Wt. Vol. Conc. Price
25 U - - Unavailable
100 U - - Unavailable

Most Popular CASP10 / Caspase 10 Proteins

Human CASP10 / Caspase 10 Recombinant Protein - LS-G4176
E. coli Expression System
Purified / Lyophilized / Biologically Active
Human CASP10 / Caspase 10 Recombinant Protein - LS-G4177
E. coli Expression System
Purified / Lyophilized / Biologically Active
Human CASP10 / Caspase 10 Recombinant (His + T7) Protein - LS-G24223
E. coli Expression System
His + T7
Human CASP10 / Caspase 10 Recombinant (GST) Protein - LS-G27749
Wheat Wheat Germ Extract
479 AA
Sodium Dodecyl Sulfate - Polyacrylamide Gel Electrophoresis Image
Human CASP10 / Caspase 10 Recombinant (6His,C-terminus) Protein (Val220-Ile480) - LS-G39695
E. coli Expression System
269 AA
Purified / Endotoxin Level: Less than 0.1 EU/µg protein (determined by LAL method).

100% Guaranteed 100% Guaranteed
Recombinant Protein
CASP10 / Caspase 10
two large (18 kDa) and two small (11 kDa) subunits in a heterotetramer form
E. coli
E. coli
Greater than 90% by SDS-PAGE
> 15000 units/mg
Reconstitute in PBS containing 15% glycerol to 1 U/µl.
Store at -70°C. Aliquot to avoid freeze/thaw cycles.
For research use only.

About CASP10 / Caspase 10

Q92851 NM_001230 NP_001221.2

CASP10 Protein, ALPS2 Protein, Caspase-10 Protein, Caspase 10 Protein, CASP-10 Protein, FADD-like ICE2 Protein, FLICE2 Protein, MCH4 Protein, ICE-like apoptotic protease 4 Protein, Apoptotic protease Mch-4 Protein

CASP10 / Caspase 10 is a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 3 and 7, and the protein itself is processed by caspase 8.

Requested From: 
Date Requested: 4/25/2017

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