Monoclonal antibodies against human Tudor-SN
Tudor-SN is a multifunctional regulator of gene expression that has been shown to function as a transcriptional co-activator, regulator of miRNA processing, mRNA splicing, and stability. Tudor-SN has also been identified as a component in RNA-induced silencing complex. Here we have produced and char...
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| Veröffentlicht in: | Hybridoma (2005) 2010-06, Vol.29 (3), p.231-236 |
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| container_title | Hybridoma (2005) |
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| creator | Saarikettu, Juha Ovod, Vladimir Vuoksio, Milka Grönholm, Juha Yang, Jie Silvennoinen, Olli |
| description | Tudor-SN is a multifunctional regulator of gene expression that has been shown to function as a transcriptional co-activator, regulator of miRNA processing, mRNA splicing, and stability. Tudor-SN has also been identified as a component in RNA-induced silencing complex. Here we have produced and characterized seven monoclonal antibody (MAb) clones against human Tudor-SN. Antibodies were generated against the fourth staphylococcal nuclease-like domain (SN4) and the Tudor domain of human Tudor-SN. The MAbs recognize the Tudor-SN protein in Western blot analysis and immunoprecipitation, and detect the specific antigen in immunohistochemistry assays. One of the antibody clones also recognizes the Drosophila melanogaster and Danio rerio Tudor-SN. Immunocytochemistry of HeLa cells revealed Tudor-SN localization in nucleolus, suggesting a possible new function for the protein in the compartment. An extensive expression analysis in human tissue arrays shows moderate to high expression of Tudor-SN in a wide range of organs and tissues, especially in epithelial cell types. |
| doi_str_mv | 10.1089/hyb.2009.0114 |
| format | Article |
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Tudor-SN has also been identified as a component in RNA-induced silencing complex. Here we have produced and characterized seven monoclonal antibody (MAb) clones against human Tudor-SN. Antibodies were generated against the fourth staphylococcal nuclease-like domain (SN4) and the Tudor domain of human Tudor-SN. The MAbs recognize the Tudor-SN protein in Western blot analysis and immunoprecipitation, and detect the specific antigen in immunohistochemistry assays. One of the antibody clones also recognizes the Drosophila melanogaster and Danio rerio Tudor-SN. Immunocytochemistry of HeLa cells revealed Tudor-SN localization in nucleolus, suggesting a possible new function for the protein in the compartment. An extensive expression analysis in human tissue arrays shows moderate to high expression of Tudor-SN in a wide range of organs and tissues, especially in epithelial cell types.</description><identifier>ISSN: 1554-0014</identifier><identifier>EISSN: 1557-8348</identifier><identifier>DOI: 10.1089/hyb.2009.0114</identifier><identifier>PMID: 20568998</identifier><language>eng</language><publisher>United States: Mary Ann Liebert, Inc</publisher><subject>Analysis ; Animals ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal - isolation & purification ; Bacterial infections ; Blotting, Western ; Cell Nucleus - immunology ; Danio rerio ; Drosophila melanogaster ; Enzyme-Linked Immunosorbent Assay ; Epithelial cells ; Epithelial Cells - immunology ; Gene expression ; Genetic aspects ; HeLa Cells ; Humans ; Hybridomas ; Immunoblotting ; Immunocytochemistry ; Immunohistochemistry ; Immunoprecipitation ; Messenger RNA ; Mice ; miRNA ; Monoclonal antibodies ; mRNA stability ; Nuclear Proteins - genetics ; Nuclear Proteins - immunology ; Nucleoli ; RNA-induced silencing complex ; Splicing ; Tissue Array Analysis ; Transcription ; Western blotting ; Zebrafish</subject><ispartof>Hybridoma (2005), 2010-06, Vol.29 (3), p.231-236</ispartof><rights>COPYRIGHT 2010 Mary Ann Liebert, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-f5c17b3fccd37d0682e4c2b2a70fba324e2d940654dd18df2d3eb7e8c858e2623</citedby><cites>FETCH-LOGICAL-c392t-f5c17b3fccd37d0682e4c2b2a70fba324e2d940654dd18df2d3eb7e8c858e2623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20568998$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Saarikettu, Juha</creatorcontrib><creatorcontrib>Ovod, Vladimir</creatorcontrib><creatorcontrib>Vuoksio, Milka</creatorcontrib><creatorcontrib>Grönholm, Juha</creatorcontrib><creatorcontrib>Yang, Jie</creatorcontrib><creatorcontrib>Silvennoinen, Olli</creatorcontrib><title>Monoclonal antibodies against human Tudor-SN</title><title>Hybridoma (2005)</title><addtitle>Hybridoma (Larchmt)</addtitle><description>Tudor-SN is a multifunctional regulator of gene expression that has been shown to function as a transcriptional co-activator, regulator of miRNA processing, mRNA splicing, and stability. Tudor-SN has also been identified as a component in RNA-induced silencing complex. Here we have produced and characterized seven monoclonal antibody (MAb) clones against human Tudor-SN. Antibodies were generated against the fourth staphylococcal nuclease-like domain (SN4) and the Tudor domain of human Tudor-SN. The MAbs recognize the Tudor-SN protein in Western blot analysis and immunoprecipitation, and detect the specific antigen in immunohistochemistry assays. One of the antibody clones also recognizes the Drosophila melanogaster and Danio rerio Tudor-SN. Immunocytochemistry of HeLa cells revealed Tudor-SN localization in nucleolus, suggesting a possible new function for the protein in the compartment. An extensive expression analysis in human tissue arrays shows moderate to high expression of Tudor-SN in a wide range of organs and tissues, especially in epithelial cell types.</description><subject>Analysis</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Monoclonal - isolation & purification</subject><subject>Bacterial infections</subject><subject>Blotting, Western</subject><subject>Cell Nucleus - immunology</subject><subject>Danio rerio</subject><subject>Drosophila melanogaster</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Epithelial cells</subject><subject>Epithelial Cells - immunology</subject><subject>Gene expression</subject><subject>Genetic aspects</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Hybridomas</subject><subject>Immunoblotting</subject><subject>Immunocytochemistry</subject><subject>Immunohistochemistry</subject><subject>Immunoprecipitation</subject><subject>Messenger RNA</subject><subject>Mice</subject><subject>miRNA</subject><subject>Monoclonal antibodies</subject><subject>mRNA stability</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - immunology</subject><subject>Nucleoli</subject><subject>RNA-induced silencing complex</subject><subject>Splicing</subject><subject>Tissue Array Analysis</subject><subject>Transcription</subject><subject>Western blotting</subject><subject>Zebrafish</subject><issn>1554-0014</issn><issn>1557-8348</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kTtPwzAQgC0EolAYWVElBhhIONt52GNV8ZIKDJTZcvxog5K4xMnQf49DCxISQjfc6fTd2acPoTMMMQbGb1abIiYAPAaMkz10hNM0jxhN2P5XnUQAOBmhY-_fAWjGSH6IRgTSjHHOjtD1k2ucqlwjq4lsurJwujR-IpeybHw3WfW1bCaLXrs2en0-QQdWVt6c7vIYvd3dLmYP0fzl_nE2nUeKctJFNlU4L6hVStNcQ3jTJIoUROZgC0lJYojmCWRpojVm2hJNTZEbpljKDMkIHaPL7d516z564ztRl16ZqpKNcb0XOaWUc2BpIK_-JTEllIVrIQvoxRZdysqIsrGua6UacDElhHNOgPJAxX9QIbSpS-UaY8vQ_zUQbQdU67xvjRXrtqxluxEYxGBIBENiMCQGQ4E_3_24L2qjf-hvJfQTt-yJKA</recordid><startdate>201006</startdate><enddate>201006</enddate><creator>Saarikettu, Juha</creator><creator>Ovod, Vladimir</creator><creator>Vuoksio, Milka</creator><creator>Grönholm, Juha</creator><creator>Yang, Jie</creator><creator>Silvennoinen, Olli</creator><general>Mary Ann Liebert, Inc</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>201006</creationdate><title>Monoclonal antibodies against human Tudor-SN</title><author>Saarikettu, Juha ; Ovod, Vladimir ; Vuoksio, Milka ; Grönholm, Juha ; Yang, Jie ; Silvennoinen, Olli</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-f5c17b3fccd37d0682e4c2b2a70fba324e2d940654dd18df2d3eb7e8c858e2623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Analysis</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Monoclonal - isolation & purification</topic><topic>Bacterial infections</topic><topic>Blotting, Western</topic><topic>Cell Nucleus - immunology</topic><topic>Danio rerio</topic><topic>Drosophila melanogaster</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Epithelial cells</topic><topic>Epithelial Cells - immunology</topic><topic>Gene expression</topic><topic>Genetic aspects</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Hybridomas</topic><topic>Immunoblotting</topic><topic>Immunocytochemistry</topic><topic>Immunohistochemistry</topic><topic>Immunoprecipitation</topic><topic>Messenger RNA</topic><topic>Mice</topic><topic>miRNA</topic><topic>Monoclonal antibodies</topic><topic>mRNA stability</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - immunology</topic><topic>Nucleoli</topic><topic>RNA-induced silencing complex</topic><topic>Splicing</topic><topic>Tissue Array Analysis</topic><topic>Transcription</topic><topic>Western blotting</topic><topic>Zebrafish</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Saarikettu, Juha</creatorcontrib><creatorcontrib>Ovod, Vladimir</creatorcontrib><creatorcontrib>Vuoksio, Milka</creatorcontrib><creatorcontrib>Grönholm, Juha</creatorcontrib><creatorcontrib>Yang, Jie</creatorcontrib><creatorcontrib>Silvennoinen, Olli</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Hybridoma (2005)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Saarikettu, Juha</au><au>Ovod, Vladimir</au><au>Vuoksio, Milka</au><au>Grönholm, Juha</au><au>Yang, Jie</au><au>Silvennoinen, Olli</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monoclonal antibodies against human Tudor-SN</atitle><jtitle>Hybridoma (2005)</jtitle><addtitle>Hybridoma (Larchmt)</addtitle><date>2010-06</date><risdate>2010</risdate><volume>29</volume><issue>3</issue><spage>231</spage><epage>236</epage><pages>231-236</pages><issn>1554-0014</issn><eissn>1557-8348</eissn><abstract>Tudor-SN is a multifunctional regulator of gene expression that has been shown to function as a transcriptional co-activator, regulator of miRNA processing, mRNA splicing, and stability. Tudor-SN has also been identified as a component in RNA-induced silencing complex. Here we have produced and characterized seven monoclonal antibody (MAb) clones against human Tudor-SN. Antibodies were generated against the fourth staphylococcal nuclease-like domain (SN4) and the Tudor domain of human Tudor-SN. The MAbs recognize the Tudor-SN protein in Western blot analysis and immunoprecipitation, and detect the specific antigen in immunohistochemistry assays. One of the antibody clones also recognizes the Drosophila melanogaster and Danio rerio Tudor-SN. Immunocytochemistry of HeLa cells revealed Tudor-SN localization in nucleolus, suggesting a possible new function for the protein in the compartment. An extensive expression analysis in human tissue arrays shows moderate to high expression of Tudor-SN in a wide range of organs and tissues, especially in epithelial cell types.</abstract><cop>United States</cop><pub>Mary Ann Liebert, Inc</pub><pmid>20568998</pmid><doi>10.1089/hyb.2009.0114</doi><tpages>6</tpages></addata></record> |
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| subjects | Analysis Animals Antibodies, Monoclonal - immunology Antibodies, Monoclonal - isolation & purification Bacterial infections Blotting, Western Cell Nucleus - immunology Danio rerio Drosophila melanogaster Enzyme-Linked Immunosorbent Assay Epithelial cells Epithelial Cells - immunology Gene expression Genetic aspects HeLa Cells Humans Hybridomas Immunoblotting Immunocytochemistry Immunohistochemistry Immunoprecipitation Messenger RNA Mice miRNA Monoclonal antibodies mRNA stability Nuclear Proteins - genetics Nuclear Proteins - immunology Nucleoli RNA-induced silencing complex Splicing Tissue Array Analysis Transcription Western blotting Zebrafish |
| title | Monoclonal antibodies against human Tudor-SN |
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