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Caspase-6 (human), (recombinant) (active)

 
ALX-201-060-U025 25 U 254.00 USD
 
ALX-201-060-U100 100 U 461.00 USD
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Product Specification

Alternative Name:Mch2
 
Source:Produced in E. coli. Contains an N-terminal His-tag.
 
EC:3.4.22.59
 
UniProt ID:P55212
 
Formulation:Lyophilized.
 
Purity:≥95% (SDS-PAGE)
 
Biological Activity:Cleaves substrates exhibiting consensus sequence VEID, e.g. Ac-VEID-AFC (Prod. No. ALX-260-111), Ac-VEID-AMC (Prod. No. ALX-260-064) and Ac-VEID-pNA (Prod. No. ALX-260-063).
 
Specific Activity:~13'000U/mg protein. One unit is defined as the amount of enzyme that cleaves 1nmol of the caspase substrate VEID-pNA per hour at 37°C in a reaction solution containing 50mM HEPES, pH 7.2, 50mM NaCl, 0.1% CHAPS, 10mM EDTA, 5% glycerol and 10mM DTT.
 
Application Notes:Useful in screening caspase inhibitors, studying enzyme regulation, determining specificity of caspase substrates or as positive control in caspase activity assays. We recommend using 1U per assay for analyzing caspase activity.
 
Reconstitution:Reconstitute to 1U/µl with PBS containing 15% glycerol.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Handling:Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and store at -80°C.
 
Scientific Background:Caspase-6 (also known as Mch2) is a member of the interleukin-1β converting enzyme (ICE) family of cysteine proteases. Same as other caspases, caspase-6 also exists in cells as an inactive proenzyme. During apoptosis procaspase-6 is processed at aspartate residues by self-proteolysis and/or cleavage by another caspase. The processed form of caspase-6 consists of large (18kDa) and small (11kDa) subunits which associate to form the active enzyme. The active caspase-6 has been shown involving in the proteolysis of poly(ADP-ribose) polymerase (PARP), an enzyme that is involved in DNA repair and genomic maintenance.
 
201-060
Figure: Active human caspase was expressed in E. coli  and purified. The activity of recombinant caspase-6 was determined by cleaving AFC conjugates of VEID. The cleavage activity was effectively inhibited by the corresponding peptide inhibitor as indicated.
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201-060

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