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Title 

Expression of the pro-domain-deleted active form of caspase-6 in Escherichia coli

Authors 

Phil Young LeeJin Hwa ChoSeung-Wook ChiKwang-Hee BaeS ChoByoung Chul ParkJeong Hoon KimSung Goo Park

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2014

Citation 

Journal of Microbiology and Biotechnology, vol. 24, no. 5, pp. 719-723

Keywords 

Active formCaspase-6E. coliEnzyme assay

Abstract 

Caspases are a family of cysteine proteases that play an important role in the apoptotic pathway. Caspase-6 is an apoptosis effector that cleaves a variety of cellular substrates. The active form of the enzyme is required for use in research. However, it has been difficult to obtain sufficient quantities of active caspase-6 from Escherichia coli. In the present study, we constructed a caspase-6 with a 23-amino-acid deletion in the pro-domain. This engineered enzyme was expressed as a soluble protein in E. coli and was purified using affinity resin. In vitro enzyme assay and cleavage analysis revealed that the engineered active caspase-6 protein had characteristics similar to those of wild-type caspase-6. This novel method can be a valuable tool for obtaining active caspase-6 that can be used for screening caspase-6-specific substrates, which in turn can be used to elucidate the function of caspase-6 in apoptosis.

ISSN 

1017-7825

Link 

http://dx.doi.org/10.4014/jmb.1312.12034

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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