Expression of the Pro-Domain--Deleted Active Form of Caspase-6 in Escherichia coli
DC Field | Value | Language |
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dc.contributor.author | Lee, Phil Young | - |
dc.contributor.author | Cho, Jin Hwa | - |
dc.contributor.author | Chi, Seung Wook | - |
dc.contributor.author | Bae, Kwang-Hee | - |
dc.contributor.author | Cho, Sayeon | - |
dc.contributor.author | Park, Byoung Chul | - |
dc.contributor.author | Kim, Jeong-Hoon | - |
dc.contributor.author | Park, Sung Goo | - |
dc.date.available | 2019-03-08T21:59:05Z | - |
dc.date.issued | 2014-05 | - |
dc.identifier.issn | 1017-7825 | - |
dc.identifier.issn | 1738-8872 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/12285 | - |
dc.description.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. | - |
dc.format.extent | 5 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY | - |
dc.title | Expression of the Pro-Domain--Deleted Active Form of Caspase-6 in Escherichia coli | - |
dc.type | Article | - |
dc.identifier.doi | 10.4014/jmb.1312.12034 | - |
dc.identifier.bibliographicCitation | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.24, no.5, pp 719 - 723 | - |
dc.identifier.kciid | ART001878605 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000336511400018 | - |
dc.identifier.scopusid | 2-s2.0-84900990278 | - |
dc.citation.endPage | 723 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 719 | - |
dc.citation.title | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY | - |
dc.citation.volume | 24 | - |
dc.type.docType | Article | - |
dc.publisher.location | 대한민국 | - |
dc.subject.keywordAuthor | Caspase-6 | - |
dc.subject.keywordAuthor | active form | - |
dc.subject.keywordAuthor | E. coli | - |
dc.subject.keywordAuthor | enzyme assay | - |
dc.subject.keywordPlus | APOPTOSIS | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | INHIBITION | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
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