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

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dc.contributor.authorPhil Young Lee-
dc.contributor.authorJin Hwa Cho-
dc.contributor.authorSeung-Wook Chi-
dc.contributor.authorKwang-Hee Bae-
dc.contributor.authorS Cho-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorJeong Hoon Kim-
dc.contributor.authorSung Goo Park-
dc.date.accessioned2017-04-19T09:54:11Z-
dc.date.available2017-04-19T09:54:11Z-
dc.date.issued2014-
dc.identifier.issn1017-7825-
dc.identifier.uri10.4014/jmb.1312.12034ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/12033-
dc.description.abstractCaspases 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.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleExpression of the pro-domain-deleted active form of caspase-6 in Escherichia coli-
dc.title.alternativeExpression of the pro-domain-deleted active form of caspase-6 in Escherichia coli-
dc.typeArticle-
dc.citation.titleJournal of Microbiology and Biotechnology-
dc.citation.number5-
dc.citation.endPage723-
dc.citation.startPage719-
dc.citation.volume24-
dc.contributor.affiliatedAuthorPhil Young Lee-
dc.contributor.affiliatedAuthorJin Hwa Cho-
dc.contributor.affiliatedAuthorSeung-Wook Chi-
dc.contributor.affiliatedAuthorKwang-Hee Bae-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorJeong Hoon Kim-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.alternativeName이필영-
dc.contributor.alternativeName조진화-
dc.contributor.alternativeName지승욱-
dc.contributor.alternativeName배광희-
dc.contributor.alternativeName조사연-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName김정훈-
dc.contributor.alternativeName박성구-
dc.identifier.bibliographicCitationJournal of Microbiology and Biotechnology, vol. 24, no. 5, pp. 719-723-
dc.identifier.doi10.4014/jmb.1312.12034-
dc.subject.keywordActive form-
dc.subject.keywordCaspase-6-
dc.subject.keywordE. coli-
dc.subject.keywordEnzyme assay-
dc.subject.localactive form-
dc.subject.localActive form-
dc.subject.localCaspase-6-
dc.subject.localEscherichia coli.-
dc.subject.localescherichia coli-
dc.subject.localEscherichia Coli-
dc.subject.localEscherichia coli-
dc.subject.localE.coli-
dc.subject.localescherichia coil-
dc.subject.localE. coli-
dc.subject.localE. Coli-
dc.subject.localEnzyme Assay-
dc.subject.localEnzyme assay-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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