產(chǎn)品詳情
  • 產(chǎn)品名稱:ActiveHumanCaspasesSetIII

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  • 產(chǎn)品廠商:Biovision
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ActiveHumanCaspasesSetIII
詳情介紹:
Unit Definition One unit of the recombinant human caspases is the enzyme activity that cleaves 1 nmol of the individual caspase substrate (YVAD-pNA for caspase-1, VDVAD-pNA for caspase-2, DEVD-pNA for caspase-3, VEID-pNA for caspase-6, DEVD-pNA for caspase-7, IETD-pNA for caspase-8, LEHD-pNA for caspase-9, and IETD-pNA for caspase-10) per hour at 37°C in a reaction solution containing 50 mM Hepes, pH 7.2, 50 mM NaCl, 0.1% Chaps, 10 mM EDTA, 5% Glycerol, and 10 mM DTT.
Sub Type Cocktail
Background Highly active recombinant human caspases were expressed in E. coli and purified. Active recombinant caspases are useful in screening caspase inhibitors, studying enzyme kinetics and regulation, determining substrate specificity, and as a positive control in caspase activity assays.
Synonyms: Active Human Caspases Set, active human caspase, active caspases, human caspases, caspase enzyme, caspase protein,
Application Notes Highly active recombinant human caspases were expressed in E. coli and purified. Active recombinant caspases are useful in screening caspase inhibitors, studying enzyme kinetics and regulation, determining substrate specificity, and as a positive control in caspase activity assays. For a complete caspase activity assay protocol, please refer to Fluorometric or Colorimetric Caspase Activity Assay Kits.
Comment

physical form description: Lyophilized powder
Contains active caspase-1/-2/-3/-6/-7/-8/-9/-10.

Restrictions For Research Use only
Format Lyophilized
Reconstitution The active recombinant caspases can be reconstituted to 0.1-1 unit per μl in PBS or the Reaction Buffer described above (available from BioVision, Cat.# 1068-20) for longer stability. We recommend using 1 unit per assay for analyzing caspase activity.
Buffer 50 mM Hepes,?pH 7.2, 50 mM NaCl, 0.1?% Chaps, 10 mM EDTA, 5?% Glycerol, and 10 mM DTT.
Handling Advice Centrifuge the vial prior to opening.
Storage -80 °C
Expiry Date 12 months