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  <Article>
    <Journal>
      <PublisherName>Dove Medical Press</PublisherName>
      <JournalTitle>Acta Medica Okayama</JournalTitle>
      <Issn>2230-3170</Issn>
      <Volume>2011</Volume>
      <Issue>1</Issue>
      <PubDate PubStatus="ppublish">
        <Year>2011</Year>
        <Month/>
      </PubDate>
    </Journal>
    <ArticleTitle>Detection of in situ cleaved p115 with the cut specific antibodies in rapid protein inactivation system by tobacco etch viral protease cleavage</ArticleTitle>
    <FirstPage LZero="delete">5</FirstPage>
    <LastPage>11</LastPage>
    <Language>EN</Language>
    <AuthorList>
      <Author>
        <FirstName EmptyYN="N">Mayuko</FirstName>
        <LastName>Koreishi</LastName>
        <Affiliation>The Research Core for Interdisciplinary Sciences (RCIS), Okayama University</Affiliation>
      </Author>
      <Author>
        <FirstName EmptyYN="N">Yasuko</FirstName>
        <LastName>Honjo</LastName>
        <Affiliation>The Research Core for Interdisciplinary Sciences (RCIS), Okayama University</Affiliation>
      </Author>
      <Author>
        <FirstName EmptyYN="N">Ayano</FirstName>
        <LastName>Satoh</LastName>
        <Affiliation>The Research Core for Interdisciplinary Sciences (RCIS), Okayama University</Affiliation>
      </Author>
    </AuthorList>
    <PublicationType/>
    <ArticleIdList>
      <ArticleId IdType="doi"/>
    </ArticleIdList>
    <Abstract>Gene perturbation methods are commonly used in the study of gene and protein function. The authors of this paper recently developed a rapid protein inactivation technique utilizing tobacco etch virus (TEV)-derived protease. TEV protease recognizes the ENLYFQG (Glu-Asn-Leu-Tyr-Phe-Gln-Gly) amino acid sequence and specifically cleaves between Q and G. The authors developed antibodies that recognize the cleaved TEV (ENLYFQ) sequence, both in vitro and in vivo, but do not bind to uncleaved TEV (ENLYFQG). Using these antibodies, in situ protein cleavage was successfully detected. These antibodies used in combination with the TEV protease may be a useful complement to other perturbation methods.</Abstract>
    <CoiStatement>No potential conflict of interest relevant to this article was reported.</CoiStatement>
    <ObjectList>
      <Object Type="keyword">
        <Param Name="value">TEV protease</Param>
      </Object>
      <Object Type="keyword">
        <Param Name="value">Golgi</Param>
      </Object>
      <Object Type="keyword">
        <Param Name="value">golgins</Param>
      </Object>
      <Object Type="keyword">
        <Param Name="value">microinjection</Param>
      </Object>
      <Object Type="keyword">
        <Param Name="value">recombinant proteins</Param>
      </Object>
    </ObjectList>
    <ReferenceList/>
  </Article>
</ArticleSet>
