Tris-acetate polyacrylamide gradient gel electrophoresis for the analysis of protein oligomerization
Here we report a new approach for studying protein oligomerization in cells using a single electrophoresis gel. We combined the use of a crosslinking reagent for sample preparation, such as glutaraldehyde, with the analysis of oligomers by Tris-acetate polyacrylamide gel electrophoresis. The use of...
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| Veröffentlicht in: | Analytical and bioanalytical chemistry 2016-02, Vol.408 (6), p.1715-1719 |
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| container_title | Analytical and bioanalytical chemistry |
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| creator | Cubillos-Rojas, Monica Schneider, Taiane Sánchez-Tena, Susana Bartrons, Ramon Ventura, Francesc Rosa, Jose Luis |
| description | Here we report a new approach for studying protein oligomerization in cells using a single electrophoresis gel. We combined the use of a crosslinking reagent for sample preparation, such as glutaraldehyde, with the analysis of oligomers by Tris-acetate polyacrylamide gel electrophoresis. The use of a 3–15 % Tris-acetate polyacrylamide gradient gel allows for the simultaneous analysis of proteins of masses ranging from 10 to 500 kDa. We showed the usefulness of this method for analyzing endogenous p53 oligomerization with high resolution and sensitivity in human cells. Oligomerization analysis was dependent on the crosslinker concentration used. We also showed that this method could be used to study the regulation of oligomerization. In all experiments, Tris-acetate polyacrylamide gel electrophoresis proved to be a robust, manageable, and cost- and time-efficient method that provided excellent results using a single gel. This approach can be easily extrapolated to the study of other oligomers. All of these features make this method a highly useful tool for the analysis of protein oligomerization. |
| doi_str_mv | 10.1007/s00216-015-9283-0 |
| format | Article |
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We combined the use of a crosslinking reagent for sample preparation, such as glutaraldehyde, with the analysis of oligomers by Tris-acetate polyacrylamide gel electrophoresis. The use of a 3–15 % Tris-acetate polyacrylamide gradient gel allows for the simultaneous analysis of proteins of masses ranging from 10 to 500 kDa. We showed the usefulness of this method for analyzing endogenous p53 oligomerization with high resolution and sensitivity in human cells. Oligomerization analysis was dependent on the crosslinker concentration used. We also showed that this method could be used to study the regulation of oligomerization. In all experiments, Tris-acetate polyacrylamide gel electrophoresis proved to be a robust, manageable, and cost- and time-efficient method that provided excellent results using a single gel. This approach can be easily extrapolated to the study of other oligomers. All of these features make this method a highly useful tool for the analysis of protein oligomerization.</description><identifier>ISSN: 1618-2642</identifier><identifier>EISSN: 1618-2650</identifier><identifier>DOI: 10.1007/s00216-015-9283-0</identifier><identifier>PMID: 26753978</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Acetates - chemistry ; Analysis ; Analytical Chemistry ; Antibodies ; Biochemistry ; Bleomycin - pharmacology ; Cell Line ; Characterization and Evaluation of Materials ; Chemical properties ; Chemistry ; Chemistry and Materials Science ; Cross-Linking Reagents - chemistry ; Crosslinking ; Doxorubicin - pharmacology ; Electrophoresis ; Electrophoresis, Polyacrylamide Gel - methods ; Extrapolation ; Food Science ; Gel electrophoresis ; gels ; Glutaral - chemistry ; glutaraldehyde ; Humans ; Kinases ; Laboratory Medicine ; Molecular Weight ; Monitoring/Environmental Analysis ; Oligomerization ; Oligomers ; polyacrylamide ; polyacrylamide gel electrophoresis ; Polyacrylamides ; Polymer crosslinking ; Protein Multimerization - drug effects ; Proteins ; Proteins - analysis ; Proteins - metabolism ; Reagents ; Sample preparation ; Tumor proteins ; Tumor Suppressor Protein p53 - analysis ; Tumor Suppressor Protein p53 - metabolism</subject><ispartof>Analytical and bioanalytical chemistry, 2016-02, Vol.408 (6), p.1715-1719</ispartof><rights>Springer-Verlag Berlin Heidelberg 2016</rights><rights>COPYRIGHT 2016 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c564t-5e137ef2eb4345590628f57afec73afb9086aa08491b67a2cf16248bffa36e713</citedby><cites>FETCH-LOGICAL-c564t-5e137ef2eb4345590628f57afec73afb9086aa08491b67a2cf16248bffa36e713</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00216-015-9283-0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00216-015-9283-0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26753978$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cubillos-Rojas, Monica</creatorcontrib><creatorcontrib>Schneider, Taiane</creatorcontrib><creatorcontrib>Sánchez-Tena, Susana</creatorcontrib><creatorcontrib>Bartrons, Ramon</creatorcontrib><creatorcontrib>Ventura, Francesc</creatorcontrib><creatorcontrib>Rosa, Jose Luis</creatorcontrib><title>Tris-acetate polyacrylamide gradient gel electrophoresis for the analysis of protein oligomerization</title><title>Analytical and bioanalytical chemistry</title><addtitle>Anal Bioanal Chem</addtitle><addtitle>Anal Bioanal Chem</addtitle><description>Here we report a new approach for studying protein oligomerization in cells using a single electrophoresis gel. We combined the use of a crosslinking reagent for sample preparation, such as glutaraldehyde, with the analysis of oligomers by Tris-acetate polyacrylamide gel electrophoresis. The use of a 3–15 % Tris-acetate polyacrylamide gradient gel allows for the simultaneous analysis of proteins of masses ranging from 10 to 500 kDa. We showed the usefulness of this method for analyzing endogenous p53 oligomerization with high resolution and sensitivity in human cells. Oligomerization analysis was dependent on the crosslinker concentration used. We also showed that this method could be used to study the regulation of oligomerization. In all experiments, Tris-acetate polyacrylamide gel electrophoresis proved to be a robust, manageable, and cost- and time-efficient method that provided excellent results using a single gel. This approach can be easily extrapolated to the study of other oligomers. 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drug effects</subject><subject>Proteins</subject><subject>Proteins - analysis</subject><subject>Proteins - metabolism</subject><subject>Reagents</subject><subject>Sample preparation</subject><subject>Tumor proteins</subject><subject>Tumor Suppressor Protein p53 - analysis</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><issn>1618-2642</issn><issn>1618-2650</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNksFuFSEUhidGY2v1AdzoJG66GT0wDDDLptFq0sSF7ZqcmXuY0jDDFbiL69PLZGo1LowrCHz_4cBHVb1m8J4BqA8JgDPZAOuanuu2gSfVKZNMN1x28PRxLvhJ9SKleyigZvJ5dcKl6tpe6dNqdxNdanCkjJnqffBHHOPR4-x2VE8Rd46WXE_ka_I05hj2dyFScqm2Idb5jmpc0B_XhWDrfQyZ3FIH76YwU3Q_MLuwvKyeWfSJXj2MZ9Xtp483l5-b669XXy4vrpuxkyI3HbFWkeU0iFZ0XQ-Sa9sptDSqFu3Qg5aIoEXPBqmQj5ZJLvRgLbaSFGvPqvOtbunj-4FSNrNLI3mPC4VDMkz1Lee6l91_oLI8kuQgCvruL_Q-HGK59UppVgxIoX9TE3oybrEhRxzXouZCCK4ZyH6l2EaNMaQUyZp9dDPGo2FgVqdmc2qKKrM6NVAybx7OPwwz7R4TvyQWgG9AKlvLRPGPBv9R9e0WshgMTuUXmNtvHJgEgE4opdqfeHe0wQ</recordid><startdate>20160201</startdate><enddate>20160201</enddate><creator>Cubillos-Rojas, Monica</creator><creator>Schneider, Taiane</creator><creator>Sánchez-Tena, Susana</creator><creator>Bartrons, Ramon</creator><creator>Ventura, Francesc</creator><creator>Rosa, Jose Luis</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</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>3V.</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H8D</scope><scope>H8G</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PDBOC</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope></search><sort><creationdate>20160201</creationdate><title>Tris-acetate polyacrylamide gradient gel electrophoresis for the analysis of protein oligomerization</title><author>Cubillos-Rojas, Monica ; Schneider, Taiane ; Sánchez-Tena, Susana ; Bartrons, Ramon ; Ventura, Francesc ; Rosa, Jose Luis</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c564t-5e137ef2eb4345590628f57afec73afb9086aa08491b67a2cf16248bffa36e713</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Acetates - 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Academic</collection><jtitle>Analytical and bioanalytical chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cubillos-Rojas, Monica</au><au>Schneider, Taiane</au><au>Sánchez-Tena, Susana</au><au>Bartrons, Ramon</au><au>Ventura, Francesc</au><au>Rosa, Jose Luis</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tris-acetate polyacrylamide gradient gel electrophoresis for the analysis of protein oligomerization</atitle><jtitle>Analytical and bioanalytical chemistry</jtitle><stitle>Anal Bioanal Chem</stitle><addtitle>Anal Bioanal Chem</addtitle><date>2016-02-01</date><risdate>2016</risdate><volume>408</volume><issue>6</issue><spage>1715</spage><epage>1719</epage><pages>1715-1719</pages><issn>1618-2642</issn><eissn>1618-2650</eissn><abstract>Here we report a new approach for studying protein oligomerization in cells using a single electrophoresis gel. We combined the use of a crosslinking reagent for sample preparation, such as glutaraldehyde, with the analysis of oligomers by Tris-acetate polyacrylamide gel electrophoresis. The use of a 3–15 % Tris-acetate polyacrylamide gradient gel allows for the simultaneous analysis of proteins of masses ranging from 10 to 500 kDa. We showed the usefulness of this method for analyzing endogenous p53 oligomerization with high resolution and sensitivity in human cells. Oligomerization analysis was dependent on the crosslinker concentration used. We also showed that this method could be used to study the regulation of oligomerization. In all experiments, Tris-acetate polyacrylamide gel electrophoresis proved to be a robust, manageable, and cost- and time-efficient method that provided excellent results using a single gel. This approach can be easily extrapolated to the study of other oligomers. All of these features make this method a highly useful tool for the analysis of protein oligomerization.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>26753978</pmid><doi>10.1007/s00216-015-9283-0</doi><tpages>5</tpages></addata></record> |
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| subjects | Acetates - chemistry Analysis Analytical Chemistry Antibodies Biochemistry Bleomycin - pharmacology Cell Line Characterization and Evaluation of Materials Chemical properties Chemistry Chemistry and Materials Science Cross-Linking Reagents - chemistry Crosslinking Doxorubicin - pharmacology Electrophoresis Electrophoresis, Polyacrylamide Gel - methods Extrapolation Food Science Gel electrophoresis gels Glutaral - chemistry glutaraldehyde Humans Kinases Laboratory Medicine Molecular Weight Monitoring/Environmental Analysis Oligomerization Oligomers polyacrylamide polyacrylamide gel electrophoresis Polyacrylamides Polymer crosslinking Protein Multimerization - drug effects Proteins Proteins - analysis Proteins - metabolism Reagents Sample preparation Tumor proteins Tumor Suppressor Protein p53 - analysis Tumor Suppressor Protein p53 - metabolism |
| title | Tris-acetate polyacrylamide gradient gel electrophoresis for the analysis of protein oligomerization |
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