#160831

Temperature sensitive Protease-V25

Cat. #160831

Temperature sensitive Protease-V25

Cat. #: 160831

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This fee is applicable only for non-profit organisations. If you are a for-profit organisation or a researcher working on commercially-sponsored academic research, you will need to contact our licensing team for a commercial use license.

Contributor

Institute: The University of Victoria

Tool Details
Handling
Related Tools
References

Tool Details

*FOR RESEARCH USE ONLY (for other uses, please contact the licensing team)

  • Tool name: Temperature sensitive Protease-V25
  • Alternate name: V25
  • Research fields: Genetics
  • Description: This novel temperature sensitive protease, a variant of subtilisin Carlsberg (SubC) protease, is expressed in Bacillus subtilis . Variant 25 (V25) has been shown to be capable of degrading a broad range of proteins in their native or denatured state. V25 has properties that allow it to digest a substrate at elevated temperatures in the 55°C range and still be deactivated at a moderate temperature in the range of 60-65°C. All activity is destroyed after a 10 minute incubation at 60°C (See Figure above.). Due to the unique properties of V25 this variant has been shown to be useful in denaturing proteins in a complex mixture while retaining the ability to inactivate the enzyme below 65°C. It has also been shown to improve molecular biology research, automated processes like Next-Gen Sequencing and disease diagnostics workflows. No column purification or treatment at extreme temperatures are required to completely deactivate this variant. This protease remains active in the presence of detergent such as SDS and Triton X-100.
  • Additional notes: Canadian Patent Application No. 3028612 US Patent No. 10894954

Handling

  • Storage conditions: Activity remains stable over several months when the protease is stored at 4° C or lower. When stored at -80° C the protease remains stable for up to two years.

Related Tools

  • Related tools: Temperature sensitive Protease-V24

References

  • Thompson et al. 2020. FEMS Microbiol Lett. 367(19):. PMID: 33016320.