For the accurate and sensitive assessment of DUB activity
Features
  • Screen potential inhibitors and activators for activity against specific DUBs
  • Optimize reaction conditions for specific DUBs to facilitate their use in high-throughput screening
  • Continuous kinetic or end-point assays can be performed in a 96-well plate format
  • Plate-based fluorescence measurement (ex: 360 nm, em: 460 nm)
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DUB Activity Assay Kit

Item No. 701490

Technical Information
Synonyms
  • Deubiquitinating Enzyme
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    Deubiquitinating enzymes (DUBs) remove ubiquitin from modified proteins in order to recycle ubiquitin attached to inappropriate targets, to remove and disassemble polyubiquitin chains, and to process proteins prior to their degradation by the proteasome.1 They have been implicated in a number of human diseases and thus, are attractive targets for potential therapeutic intervention via the development of suitable inhibitors and modulators.2,1 Cayman's DUB Activity Assay Kit facilitates the rapid, robust measurement of deubiquitinating enzyme activity in vitro. The kit utilizes a high purity, fluorogenic substrate (ubiquitin-AMC) together with suitable calibration standards and controls for the accurate and sensitive assessment of DUB activity. Continuous kinetic or end-point assays can be performed in a 96-well plate format for multi-sample analysis.

    Needed but not supplied: Please download the kit booklet to verify if UltraPure Water (Milli-Q or equivalent) or any other components are needed for this assay.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Ciechanover, A. Intracellular protein degradation: From a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Bioorg. Med. Chem. 21(12), 3400-3410 (2013).

    2. Fraile, J.M., Quesada, V., Rodríguez, D., et alDeubiquitinases in cancer: New functions and therapeutic options. Oncogene 31(19), 2373-2388 (2012).