Expression of the Pro-Domain--Deleted Active Form of Caspase-6 in Escherichia coli
- Authors
- Lee, Phil Young; Cho, Jin Hwa; Chi, Seung Wook; Bae, Kwang-Hee; Cho, Sayeon; Park, Byoung Chul; Kim, Jeong-Hoon; Park, Sung Goo
- Issue Date
- May-2014
- Publisher
- KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
- Keywords
- Caspase-6; active form; E. coli; enzyme assay
- Citation
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.24, no.5, pp 719 - 723
- Pages
- 5
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 24
- Number
- 5
- Start Page
- 719
- End Page
- 723
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/12285
- DOI
- 10.4014/jmb.1312.12034
- ISSN
- 1017-7825
1738-8872
- 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.
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