Preparation and characterization of polyclonal antibodies against human chaperonin 10
Early pregnancy factor (EPF) has been identified as an extracellular homologue of chaperonin 10 (Cpn10), a heat shock protein that functions within the cell as a molecular chaperone. Here, we report the production of polyclonal antibodies directed against several different regions of the human Cpn10...
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| Veröffentlicht in: | Cell stress & chaperones 2000-01, Vol.5 (1), p.14-20 |
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| container_title | Cell stress & chaperones |
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| creator | Somodevilla-Torres, Maria J. Hillyard, Narelle C. Morton, Halle Alewood, Dianne Halliday, Judy A. Alewood, Paul F. Vesey, David A. Walsh, Michael D. Cavanagh, Alice C. |
| description | Early pregnancy factor (EPF) has been identified as an extracellular homologue of chaperonin 10 (Cpn10), a heat shock protein that functions within the cell as a molecular chaperone. Here, we report the production of polyclonal antibodies directed against several different regions of the human Cpn10 molecule and their application to specific protein quantitation and localization techniques. These antibodies will be valuable tools in further studies to elucidate the mechanisms underlying the differential spatial and temporal localization of EPF and Cpn10 and in studies to elucidate structure and function. |
| doi_str_mv | 10.1379/1466-1268(2000)005<0014:PACOPA>2.0.CO;2 |
| format | Article |
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Here, we report the production of polyclonal antibodies directed against several different regions of the human Cpn10 molecule and their application to specific protein quantitation and localization techniques. 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Here, we report the production of polyclonal antibodies directed against several different regions of the human Cpn10 molecule and their application to specific protein quantitation and localization techniques. These antibodies will be valuable tools in further studies to elucidate the mechanisms underlying the differential spatial and temporal localization of EPF and Cpn10 and in studies to elucidate structure and function.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies - immunology</subject><subject>Antibody formation</subject><subject>Antibody Specificity</subject><subject>Antigens</subject><subject>Bioassay</subject><subject>Blotting, Western</subject><subject>Carcinoma - chemistry</subject><subject>Cell growth</subject><subject>Chaperonin 10 - analysis</subject><subject>Chaperonin 10 - immunology</subject><subject>Chaperonins</subject><subject>Colorectal Neoplasms - chemistry</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Gels</subject><subject>Humans</subject><subject>Immune Sera</subject><subject>Immunization</subject><subject>Molecular Sequence Data</subject><subject>Molecules</subject><subject>Neoplasm Proteins - analysis</subject><subject>Peptide Fragments - immunology</subject><subject>Precipitin Tests</subject><subject>Pregnancy</subject><subject>Rabbits</subject><subject>Recombinant Fusion Proteins - immunology</subject><subject>Short Communications</subject><subject>Sodium</subject><issn>1355-8145</issn><issn>1466-1268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqdkM1q3DAURkVJaCZp36AUr0Ky8ORe2bKsJgQGkyaFwMwiXQvZljsaPJIreRbp00fGQ9p1V_r5zv0kDiE3CEvMuLjBvChSpEV5RQHgGoDdAWD-bbOq1pvVPV3Cslrf0g9k8U6exH3GWFpizs7IeQi7OMk5x4_kDIEDlhlbkJ8brwfl1WicTZRtk2YbT82ovfkzX7ouGVz_2vTOqj4io6lda3RI1C9lbBiT7WGv7DQ3aO-ssQnCJ3LaqT7oz8f1grx8f3ipntLn9eOPavWc1jmKMW1LTpWohcgKnWWiyzmnutBCACoFnGVtAawURdMitDm0TclY13SIGqlCzC7I5Vw7ePf7oMMo9yY0uu-V1e4QJAeRl0hZBB9nsPEuBK87OXizV_5VIshJsJy0yUmbnATLKFhOguUsWFIJslpLGpu-Hp881Hvd_tMzG43AlxnYhdH5v3kByAWP8cMc18Y5q__7H2-3FJd8</recordid><startdate>200001</startdate><enddate>200001</enddate><creator>Somodevilla-Torres, Maria J.</creator><creator>Hillyard, Narelle C.</creator><creator>Morton, Halle</creator><creator>Alewood, Dianne</creator><creator>Halliday, Judy A.</creator><creator>Alewood, Paul F.</creator><creator>Vesey, David A.</creator><creator>Walsh, Michael D.</creator><creator>Cavanagh, Alice C.</creator><general>Cell Stress Society International</general><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>200001</creationdate><title>Preparation and characterization of polyclonal antibodies against human chaperonin 10</title><author>Somodevilla-Torres, Maria J. ; Hillyard, Narelle C. ; Morton, Halle ; Alewood, Dianne ; Halliday, Judy A. ; Alewood, Paul F. ; Vesey, David A. ; Walsh, Michael D. ; Cavanagh, Alice C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b419t-d872a9b9936e339f4772e6e9901aa0753d605896cd10d40dc855fcf11e12a113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies - immunology</topic><topic>Antibody formation</topic><topic>Antibody Specificity</topic><topic>Antigens</topic><topic>Bioassay</topic><topic>Blotting, Western</topic><topic>Carcinoma - chemistry</topic><topic>Cell growth</topic><topic>Chaperonin 10 - analysis</topic><topic>Chaperonin 10 - immunology</topic><topic>Chaperonins</topic><topic>Colorectal Neoplasms - chemistry</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Gels</topic><topic>Humans</topic><topic>Immune Sera</topic><topic>Immunization</topic><topic>Molecular Sequence Data</topic><topic>Molecules</topic><topic>Neoplasm Proteins - analysis</topic><topic>Peptide Fragments - immunology</topic><topic>Precipitin Tests</topic><topic>Pregnancy</topic><topic>Rabbits</topic><topic>Recombinant Fusion Proteins - immunology</topic><topic>Short Communications</topic><topic>Sodium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Somodevilla-Torres, Maria J.</creatorcontrib><creatorcontrib>Hillyard, Narelle C.</creatorcontrib><creatorcontrib>Morton, Halle</creatorcontrib><creatorcontrib>Alewood, Dianne</creatorcontrib><creatorcontrib>Halliday, Judy A.</creatorcontrib><creatorcontrib>Alewood, Paul F.</creatorcontrib><creatorcontrib>Vesey, David A.</creatorcontrib><creatorcontrib>Walsh, Michael D.</creatorcontrib><creatorcontrib>Cavanagh, Alice C.</creatorcontrib><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>Cell stress & chaperones</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Somodevilla-Torres, Maria J.</au><au>Hillyard, Narelle C.</au><au>Morton, Halle</au><au>Alewood, Dianne</au><au>Halliday, Judy A.</au><au>Alewood, Paul F.</au><au>Vesey, David A.</au><au>Walsh, Michael D.</au><au>Cavanagh, Alice C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation and characterization of polyclonal antibodies against human chaperonin 10</atitle><jtitle>Cell stress & chaperones</jtitle><addtitle>Cell Stress Chaperones</addtitle><date>2000-01</date><risdate>2000</risdate><volume>5</volume><issue>1</issue><spage>14</spage><epage>20</epage><pages>14-20</pages><issn>1355-8145</issn><eissn>1466-1268</eissn><abstract>Early pregnancy factor (EPF) has been identified as an extracellular homologue of chaperonin 10 (Cpn10), a heat shock protein that functions within the cell as a molecular chaperone. Here, we report the production of polyclonal antibodies directed against several different regions of the human Cpn10 molecule and their application to specific protein quantitation and localization techniques. These antibodies will be valuable tools in further studies to elucidate the mechanisms underlying the differential spatial and temporal localization of EPF and Cpn10 and in studies to elucidate structure and function.</abstract><cop>Netherlands</cop><pub>Cell Stress Society International</pub><pmid>10701835</pmid><doi>10.1379/1466-1268(2000)005<0014:PACOPA>2.0.CO;2</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Antibodies Antibodies - immunology Antibody formation Antibody Specificity Antigens Bioassay Blotting, Western Carcinoma - chemistry Cell growth Chaperonin 10 - analysis Chaperonin 10 - immunology Chaperonins Colorectal Neoplasms - chemistry Enzyme-Linked Immunosorbent Assay Gels Humans Immune Sera Immunization Molecular Sequence Data Molecules Neoplasm Proteins - analysis Peptide Fragments - immunology Precipitin Tests Pregnancy Rabbits Recombinant Fusion Proteins - immunology Short Communications Sodium |
| title | Preparation and characterization of polyclonal antibodies against human chaperonin 10 |
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