A novel epitope tag for the detection of rabGTPases
Rab GTPases are localized on the cytoplasmic surface of most intracellular organelles where they play a role in the regulation of vesicular transport. As it has been difficult to detect endogenous rab proteins by morphological methods, their localizations were often inferred from transfection experi...
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| Veröffentlicht in: | Electrophoresis 1997, Vol.18 (14), p.2694-2698 |
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| container_title | Electrophoresis |
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| creator | Nagelkerken, Bas Mohrmann, Karin Gerez, Lisya van Raak, Marcel Leijendekker, Richtje van der Sluijs, Peter |
| description | Rab GTPases are localized on the cytoplasmic surface of most intracellular organelles where they play a role in the regulation of vesicular transport. As it has been difficult to detect endogenous rab proteins by morphological methods, their localizations were often inferred from transfection experiments using epitope‐tagged constructs. Because most of the available epitope tags are only recognitzed by mouse monoclonal antibodies they are often not suitable for double or triple label immunocytochemistry. To overcome this problem, we generated antibodies against a novel 10 amino acid X31 influenza hemagglutin epitope (NH). We here characterized these antibodies and document their utility for detecting early endosomal rab proteins N‐terminally tagged with the NH decapeptide in morphological and biochemical assays. |
| doi_str_mv | 10.1002/elps.1150181427 |
| format | Article |
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As it has been difficult to detect endogenous rab proteins by morphological methods, their localizations were often inferred from transfection experiments using epitope‐tagged constructs. Because most of the available epitope tags are only recognitzed by mouse monoclonal antibodies they are often not suitable for double or triple label immunocytochemistry. To overcome this problem, we generated antibodies against a novel 10 amino acid X31 influenza hemagglutin epitope (NH). 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As it has been difficult to detect endogenous rab proteins by morphological methods, their localizations were often inferred from transfection experiments using epitope‐tagged constructs. Because most of the available epitope tags are only recognitzed by mouse monoclonal antibodies they are often not suitable for double or triple label immunocytochemistry. To overcome this problem, we generated antibodies against a novel 10 amino acid X31 influenza hemagglutin epitope (NH). We here characterized these antibodies and document their utility for detecting early endosomal rab proteins N‐terminally tagged with the NH decapeptide in morphological and biochemical assays.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>DNA Primers</subject><subject>Epitopes, B-Lymphocyte - immunology</subject><subject>GTP-Binding Proteins - analysis</subject><subject>GTP-Binding Proteins - genetics</subject><subject>GTP-Binding Proteins - immunology</subject><subject>Guanine Nucleotides</subject><subject>Guinea Pigs</subject><subject>HeLa Cells</subject><subject>Hemagglutin epitope tag</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - immunology</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>rab4</subject><subject>rab4 GTP-Binding Proteins</subject><subject>rab5</subject><subject>rab5 GTP-Binding Proteins</subject><subject>Rabbits</subject><issn>0173-0835</issn><issn>1522-2683</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1PwkAQhjdGg4iePZn05K2wH93dbjwhATRplCCG42bbTrVaaN0tKv_ekhKMJ0-Tybzvk8mD0CXBfYIxHUBRuT4hHJOQBFQeoS7hlPpUhOwYdTGRzMch46fozLk3jHGggqCDOopTyTHuIjb01uUnFB5UeV1W4NXmxctK69Wv4KVQQ1Ln5dorM8-aeLqYGQfuHJ1kpnBwsZ899DwZL0Z3fvQ4vR8NIz9hIZU-MdIkkgSiWbM0NBAyRWJMU4jjhCRAJSiQAuMYQqwCQcM4EUamQfO84BljPXTdcitbfmzA1XqVuwSKwqyh3DgtFedKCNUEB20wsaVzFjJd2Xxl7FYTrHea9E6T_tXUNK726E28gvSQ33tp7jft_SsvYPsfTo-j2dMfut-2c1fD96Ft7LsWkkmulw9TPZvczqP57UIv2Q-gqYLG</recordid><startdate>1997</startdate><enddate>1997</enddate><creator>Nagelkerken, Bas</creator><creator>Mohrmann, Karin</creator><creator>Gerez, Lisya</creator><creator>van Raak, Marcel</creator><creator>Leijendekker, Richtje</creator><creator>van der Sluijs, Peter</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>1997</creationdate><title>A novel epitope tag for the detection of rabGTPases</title><author>Nagelkerken, Bas ; Mohrmann, Karin ; Gerez, Lisya ; van Raak, Marcel ; Leijendekker, Richtje ; van der Sluijs, Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3827-1a7ac7146c38fd8ae8391b02debbc1ce27e9e7600be8094628bc6a7d426865f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>DNA Primers</topic><topic>Epitopes, B-Lymphocyte - immunology</topic><topic>GTP-Binding Proteins - analysis</topic><topic>GTP-Binding Proteins - genetics</topic><topic>GTP-Binding Proteins - immunology</topic><topic>Guanine Nucleotides</topic><topic>Guinea Pigs</topic><topic>HeLa Cells</topic><topic>Hemagglutin epitope tag</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - immunology</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>rab4</topic><topic>rab4 GTP-Binding Proteins</topic><topic>rab5</topic><topic>rab5 GTP-Binding Proteins</topic><topic>Rabbits</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nagelkerken, Bas</creatorcontrib><creatorcontrib>Mohrmann, Karin</creatorcontrib><creatorcontrib>Gerez, Lisya</creatorcontrib><creatorcontrib>van Raak, Marcel</creatorcontrib><creatorcontrib>Leijendekker, Richtje</creatorcontrib><creatorcontrib>van der Sluijs, Peter</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Electrophoresis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nagelkerken, Bas</au><au>Mohrmann, Karin</au><au>Gerez, Lisya</au><au>van Raak, Marcel</au><au>Leijendekker, Richtje</au><au>van der Sluijs, Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel epitope tag for the detection of rabGTPases</atitle><jtitle>Electrophoresis</jtitle><addtitle>ELECTROPHORESIS</addtitle><date>1997</date><risdate>1997</risdate><volume>18</volume><issue>14</issue><spage>2694</spage><epage>2698</epage><pages>2694-2698</pages><issn>0173-0835</issn><eissn>1522-2683</eissn><abstract>Rab GTPases are localized on the cytoplasmic surface of most intracellular organelles where they play a role in the regulation of vesicular transport. As it has been difficult to detect endogenous rab proteins by morphological methods, their localizations were often inferred from transfection experiments using epitope‐tagged constructs. Because most of the available epitope tags are only recognitzed by mouse monoclonal antibodies they are often not suitable for double or triple label immunocytochemistry. To overcome this problem, we generated antibodies against a novel 10 amino acid X31 influenza hemagglutin epitope (NH). We here characterized these antibodies and document their utility for detecting early endosomal rab proteins N‐terminally tagged with the NH decapeptide in morphological and biochemical assays.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>9527500</pmid><doi>10.1002/elps.1150181427</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0173-0835 |
| ispartof | Electrophoresis, 1997, Vol.18 (14), p.2694-2698 |
| issn | 0173-0835 1522-2683 |
| language | eng |
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| source | MEDLINE; Wiley Online Library All Journals |
| subjects | Animals Base Sequence CHO Cells Cricetinae DNA Primers Epitopes, B-Lymphocyte - immunology GTP-Binding Proteins - analysis GTP-Binding Proteins - genetics GTP-Binding Proteins - immunology Guanine Nucleotides Guinea Pigs HeLa Cells Hemagglutin epitope tag Hemagglutinin Glycoproteins, Influenza Virus - immunology Humans Mice Molecular Sequence Data Mutation rab4 rab4 GTP-Binding Proteins rab5 rab5 GTP-Binding Proteins Rabbits |
| title | A novel epitope tag for the detection of rabGTPases |
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