Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers
Abstract Proteome profiling is most commonly based on a two-dimensional gel electrophoresis to separate and visualize proteins for identification. The success of a proteomic experiment is critically dependent on the sample preparation. The two most effective and widely used lysis buffers for extract...
Ausführliche Beschreibung
Autor*in: |
Sekhon, Simranjeet Singh [verfasserIn] Ahn, Ji-Young [verfasserIn] Shin, Woori [verfasserIn] Kim, Gonhyung [verfasserIn] Yoon, Hobaek [verfasserIn] Min, Jiho [verfasserIn] Kim, Yang-Hoon [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
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2015 |
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Schlagwörter: |
Radio-Immunoprecipitation Assay buffer (RIPA buffer) |
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Übergeordnetes Werk: |
Enthalten in: Toxicology and Environmental Health Sciences - Korean Society of Environmental Risk Assessment and Health Science, 2011, 7(2015), 3 vom: Sept., Seite 184-189 |
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Übergeordnetes Werk: |
volume:7 ; year:2015 ; number:3 ; month:09 ; pages:184-189 |
Links: |
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DOI / URN: |
10.1007/s13530-015-0236-y |
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SPR031728421 |
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10.1007/s13530-015-0236-y doi (DE-627)SPR031728421 (SPR)s13530-015-0236-y-e DE-627 ger DE-627 rakwb eng Sekhon, Simranjeet Singh verfasserin aut Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Proteome profiling is most commonly based on a two-dimensional gel electrophoresis to separate and visualize proteins for identification. The success of a proteomic experiment is critically dependent on the sample preparation. The two most effective and widely used lysis buffers for extracting proteins from cells and tissues are Radio-Immunoprecipitation Assay buffer (RIPA buffer) and Urea lysis buffer. These buffers are rapid and highly efficient for cell lysis and good solublization of a wide range of proteins. In this study, the proteome profile of Rabbit muscle and tendon was analysed by 2-D gel electrophoresis using RIPA buffer and Urea lysis buffers. The variations in lysis buffers for extracting proteins clearly improve the resolution of protein identification spots as compared to conventional methods. Radio-Immunoprecipitation Assay buffer (RIPA buffer) (dpeaa)DE-He213 Urea lysis buffer (dpeaa)DE-He213 Two-dimensional gel electrophoresis (dpeaa)DE-He213 Proteome profiling (dpeaa)DE-He213 Ahn, Ji-Young verfasserin aut Shin, Woori verfasserin aut Kim, Gonhyung verfasserin aut Yoon, Hobaek verfasserin aut Min, Jiho verfasserin aut Kim, Yang-Hoon verfasserin aut Enthalten in Toxicology and Environmental Health Sciences Korean Society of Environmental Risk Assessment and Health Science, 2011 7(2015), 3 vom: Sept., Seite 184-189 (DE-627)SPR031726593 nnns volume:7 year:2015 number:3 month:09 pages:184-189 https://dx.doi.org/10.1007/s13530-015-0236-y lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 7 2015 3 09 184-189 |
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10.1007/s13530-015-0236-y doi (DE-627)SPR031728421 (SPR)s13530-015-0236-y-e DE-627 ger DE-627 rakwb eng Sekhon, Simranjeet Singh verfasserin aut Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Proteome profiling is most commonly based on a two-dimensional gel electrophoresis to separate and visualize proteins for identification. The success of a proteomic experiment is critically dependent on the sample preparation. The two most effective and widely used lysis buffers for extracting proteins from cells and tissues are Radio-Immunoprecipitation Assay buffer (RIPA buffer) and Urea lysis buffer. These buffers are rapid and highly efficient for cell lysis and good solublization of a wide range of proteins. In this study, the proteome profile of Rabbit muscle and tendon was analysed by 2-D gel electrophoresis using RIPA buffer and Urea lysis buffers. The variations in lysis buffers for extracting proteins clearly improve the resolution of protein identification spots as compared to conventional methods. Radio-Immunoprecipitation Assay buffer (RIPA buffer) (dpeaa)DE-He213 Urea lysis buffer (dpeaa)DE-He213 Two-dimensional gel electrophoresis (dpeaa)DE-He213 Proteome profiling (dpeaa)DE-He213 Ahn, Ji-Young verfasserin aut Shin, Woori verfasserin aut Kim, Gonhyung verfasserin aut Yoon, Hobaek verfasserin aut Min, Jiho verfasserin aut Kim, Yang-Hoon verfasserin aut Enthalten in Toxicology and Environmental Health Sciences Korean Society of Environmental Risk Assessment and Health Science, 2011 7(2015), 3 vom: Sept., Seite 184-189 (DE-627)SPR031726593 nnns volume:7 year:2015 number:3 month:09 pages:184-189 https://dx.doi.org/10.1007/s13530-015-0236-y lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 7 2015 3 09 184-189 |
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10.1007/s13530-015-0236-y doi (DE-627)SPR031728421 (SPR)s13530-015-0236-y-e DE-627 ger DE-627 rakwb eng Sekhon, Simranjeet Singh verfasserin aut Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Proteome profiling is most commonly based on a two-dimensional gel electrophoresis to separate and visualize proteins for identification. The success of a proteomic experiment is critically dependent on the sample preparation. The two most effective and widely used lysis buffers for extracting proteins from cells and tissues are Radio-Immunoprecipitation Assay buffer (RIPA buffer) and Urea lysis buffer. These buffers are rapid and highly efficient for cell lysis and good solublization of a wide range of proteins. In this study, the proteome profile of Rabbit muscle and tendon was analysed by 2-D gel electrophoresis using RIPA buffer and Urea lysis buffers. The variations in lysis buffers for extracting proteins clearly improve the resolution of protein identification spots as compared to conventional methods. Radio-Immunoprecipitation Assay buffer (RIPA buffer) (dpeaa)DE-He213 Urea lysis buffer (dpeaa)DE-He213 Two-dimensional gel electrophoresis (dpeaa)DE-He213 Proteome profiling (dpeaa)DE-He213 Ahn, Ji-Young verfasserin aut Shin, Woori verfasserin aut Kim, Gonhyung verfasserin aut Yoon, Hobaek verfasserin aut Min, Jiho verfasserin aut Kim, Yang-Hoon verfasserin aut Enthalten in Toxicology and Environmental Health Sciences Korean Society of Environmental Risk Assessment and Health Science, 2011 7(2015), 3 vom: Sept., Seite 184-189 (DE-627)SPR031726593 nnns volume:7 year:2015 number:3 month:09 pages:184-189 https://dx.doi.org/10.1007/s13530-015-0236-y lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 7 2015 3 09 184-189 |
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10.1007/s13530-015-0236-y doi (DE-627)SPR031728421 (SPR)s13530-015-0236-y-e DE-627 ger DE-627 rakwb eng Sekhon, Simranjeet Singh verfasserin aut Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Proteome profiling is most commonly based on a two-dimensional gel electrophoresis to separate and visualize proteins for identification. The success of a proteomic experiment is critically dependent on the sample preparation. The two most effective and widely used lysis buffers for extracting proteins from cells and tissues are Radio-Immunoprecipitation Assay buffer (RIPA buffer) and Urea lysis buffer. These buffers are rapid and highly efficient for cell lysis and good solublization of a wide range of proteins. In this study, the proteome profile of Rabbit muscle and tendon was analysed by 2-D gel electrophoresis using RIPA buffer and Urea lysis buffers. The variations in lysis buffers for extracting proteins clearly improve the resolution of protein identification spots as compared to conventional methods. Radio-Immunoprecipitation Assay buffer (RIPA buffer) (dpeaa)DE-He213 Urea lysis buffer (dpeaa)DE-He213 Two-dimensional gel electrophoresis (dpeaa)DE-He213 Proteome profiling (dpeaa)DE-He213 Ahn, Ji-Young verfasserin aut Shin, Woori verfasserin aut Kim, Gonhyung verfasserin aut Yoon, Hobaek verfasserin aut Min, Jiho verfasserin aut Kim, Yang-Hoon verfasserin aut Enthalten in Toxicology and Environmental Health Sciences Korean Society of Environmental Risk Assessment and Health Science, 2011 7(2015), 3 vom: Sept., Seite 184-189 (DE-627)SPR031726593 nnns volume:7 year:2015 number:3 month:09 pages:184-189 https://dx.doi.org/10.1007/s13530-015-0236-y lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 7 2015 3 09 184-189 |
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10.1007/s13530-015-0236-y doi (DE-627)SPR031728421 (SPR)s13530-015-0236-y-e DE-627 ger DE-627 rakwb eng Sekhon, Simranjeet Singh verfasserin aut Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Proteome profiling is most commonly based on a two-dimensional gel electrophoresis to separate and visualize proteins for identification. The success of a proteomic experiment is critically dependent on the sample preparation. The two most effective and widely used lysis buffers for extracting proteins from cells and tissues are Radio-Immunoprecipitation Assay buffer (RIPA buffer) and Urea lysis buffer. These buffers are rapid and highly efficient for cell lysis and good solublization of a wide range of proteins. In this study, the proteome profile of Rabbit muscle and tendon was analysed by 2-D gel electrophoresis using RIPA buffer and Urea lysis buffers. The variations in lysis buffers for extracting proteins clearly improve the resolution of protein identification spots as compared to conventional methods. Radio-Immunoprecipitation Assay buffer (RIPA buffer) (dpeaa)DE-He213 Urea lysis buffer (dpeaa)DE-He213 Two-dimensional gel electrophoresis (dpeaa)DE-He213 Proteome profiling (dpeaa)DE-He213 Ahn, Ji-Young verfasserin aut Shin, Woori verfasserin aut Kim, Gonhyung verfasserin aut Yoon, Hobaek verfasserin aut Min, Jiho verfasserin aut Kim, Yang-Hoon verfasserin aut Enthalten in Toxicology and Environmental Health Sciences Korean Society of Environmental Risk Assessment and Health Science, 2011 7(2015), 3 vom: Sept., Seite 184-189 (DE-627)SPR031726593 nnns volume:7 year:2015 number:3 month:09 pages:184-189 https://dx.doi.org/10.1007/s13530-015-0236-y lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 7 2015 3 09 184-189 |
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Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers Radio-Immunoprecipitation Assay buffer (RIPA buffer) (dpeaa)DE-He213 Urea lysis buffer (dpeaa)DE-He213 Two-dimensional gel electrophoresis (dpeaa)DE-He213 Proteome profiling (dpeaa)DE-He213 |
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Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers |
abstract |
Abstract Proteome profiling is most commonly based on a two-dimensional gel electrophoresis to separate and visualize proteins for identification. The success of a proteomic experiment is critically dependent on the sample preparation. The two most effective and widely used lysis buffers for extracting proteins from cells and tissues are Radio-Immunoprecipitation Assay buffer (RIPA buffer) and Urea lysis buffer. These buffers are rapid and highly efficient for cell lysis and good solublization of a wide range of proteins. In this study, the proteome profile of Rabbit muscle and tendon was analysed by 2-D gel electrophoresis using RIPA buffer and Urea lysis buffers. The variations in lysis buffers for extracting proteins clearly improve the resolution of protein identification spots as compared to conventional methods. |
abstractGer |
Abstract Proteome profiling is most commonly based on a two-dimensional gel electrophoresis to separate and visualize proteins for identification. The success of a proteomic experiment is critically dependent on the sample preparation. The two most effective and widely used lysis buffers for extracting proteins from cells and tissues are Radio-Immunoprecipitation Assay buffer (RIPA buffer) and Urea lysis buffer. These buffers are rapid and highly efficient for cell lysis and good solublization of a wide range of proteins. In this study, the proteome profile of Rabbit muscle and tendon was analysed by 2-D gel electrophoresis using RIPA buffer and Urea lysis buffers. The variations in lysis buffers for extracting proteins clearly improve the resolution of protein identification spots as compared to conventional methods. |
abstract_unstemmed |
Abstract Proteome profiling is most commonly based on a two-dimensional gel electrophoresis to separate and visualize proteins for identification. The success of a proteomic experiment is critically dependent on the sample preparation. The two most effective and widely used lysis buffers for extracting proteins from cells and tissues are Radio-Immunoprecipitation Assay buffer (RIPA buffer) and Urea lysis buffer. These buffers are rapid and highly efficient for cell lysis and good solublization of a wide range of proteins. In this study, the proteome profile of Rabbit muscle and tendon was analysed by 2-D gel electrophoresis using RIPA buffer and Urea lysis buffers. The variations in lysis buffers for extracting proteins clearly improve the resolution of protein identification spots as compared to conventional methods. |
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Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers |
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10.1007/s13530-015-0236-y |
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