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
Gespeichert in:
| 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] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2015 |
|---|
| Schlagwörter: |
Radio-Immunoprecipitation Assay buffer (RIPA buffer) |
|---|
| 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 |
|---|---|
| Übergeordnetes Werk: |
volume:7 ; year:2015 ; number:3 ; month:09 ; pages:184-189 |
| Links: |
|---|
| DOI / URN: |
10.1007/s13530-015-0236-y |
|---|
| Katalog-ID: |
SPR031728421 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | SPR031728421 | ||
| 003 | DE-627 | ||
| 005 | 20201125152602.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 201007s2015 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1007/s13530-015-0236-y |2 doi | |
| 035 | |a (DE-627)SPR031728421 | ||
| 035 | |a (SPR)s13530-015-0236-y-e | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Sekhon, Simranjeet Singh |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers |
| 264 | 1 | |c 2015 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 520 | |a 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. | ||
| 650 | 4 | |a Radio-Immunoprecipitation Assay buffer (RIPA buffer) |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Urea lysis buffer |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Two-dimensional gel electrophoresis |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Proteome profiling |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Ahn, Ji-Young |e verfasserin |4 aut | |
| 700 | 1 | |a Shin, Woori |e verfasserin |4 aut | |
| 700 | 1 | |a Kim, Gonhyung |e verfasserin |4 aut | |
| 700 | 1 | |a Yoon, Hobaek |e verfasserin |4 aut | |
| 700 | 1 | |a Min, Jiho |e verfasserin |4 aut | |
| 700 | 1 | |a Kim, Yang-Hoon |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Toxicology and Environmental Health Sciences |d Korean Society of Environmental Risk Assessment and Health Science, 2011 |g 7(2015), 3 vom: Sept., Seite 184-189 |w (DE-627)SPR031726593 |7 nnns |
| 773 | 1 | 8 | |g volume:7 |g year:2015 |g number:3 |g month:09 |g pages:184-189 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.1007/s13530-015-0236-y |z lizenzpflichtig |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a SYSFLAG_A | ||
| 912 | |a GBV_SPRINGER | ||
| 951 | |a AR | ||
| 952 | |d 7 |j 2015 |e 3 |c 09 |h 184-189 | ||
| author_variant |
s s s ss sss j y a jya w s ws g k gk h y hy j m jm y h k yhk |
|---|---|
| matchkey_str |
sekhonsimranjeetsinghahnjiyoungshinwoori:2015----:aperprtofrpiapoemcrflnorbimsladednsnrdomuorcpt |
| hierarchy_sort_str |
2015 |
| publishDate |
2015 |
| allfields |
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 |
| spelling |
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 |
| allfields_unstemmed |
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 |
| allfieldsGer |
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 |
| allfieldsSound |
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 |
| language |
English |
| source |
Enthalten in Toxicology and Environmental Health Sciences 7(2015), 3 vom: Sept., Seite 184-189 volume:7 year:2015 number:3 month:09 pages:184-189 |
| sourceStr |
Enthalten in Toxicology and Environmental Health Sciences 7(2015), 3 vom: Sept., Seite 184-189 volume:7 year:2015 number:3 month:09 pages:184-189 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| topic_facet |
Radio-Immunoprecipitation Assay buffer (RIPA buffer) Urea lysis buffer Two-dimensional gel electrophoresis Proteome profiling |
| isfreeaccess_bool |
false |
| container_title |
Toxicology and Environmental Health Sciences |
| authorswithroles_txt_mv |
Sekhon, Simranjeet Singh @@aut@@ Ahn, Ji-Young @@aut@@ Shin, Woori @@aut@@ Kim, Gonhyung @@aut@@ Yoon, Hobaek @@aut@@ Min, Jiho @@aut@@ Kim, Yang-Hoon @@aut@@ |
| publishDateDaySort_date |
2015-09-01T00:00:00Z |
| hierarchy_top_id |
SPR031726593 |
| id |
SPR031728421 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR031728421</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20201125152602.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201007s2015 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s13530-015-0236-y</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR031728421</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s13530-015-0236-y-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Sekhon, Simranjeet Singh</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2015</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">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.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Radio-Immunoprecipitation Assay buffer (RIPA buffer)</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Urea lysis buffer</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Two-dimensional gel electrophoresis</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Proteome profiling</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ahn, Ji-Young</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Shin, Woori</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kim, Gonhyung</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yoon, Hobaek</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Min, Jiho</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kim, Yang-Hoon</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Toxicology and Environmental Health Sciences</subfield><subfield code="d">Korean Society of Environmental Risk Assessment and Health Science, 2011</subfield><subfield code="g">7(2015), 3 vom: Sept., Seite 184-189</subfield><subfield code="w">(DE-627)SPR031726593</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:7</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:3</subfield><subfield code="g">month:09</subfield><subfield code="g">pages:184-189</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://dx.doi.org/10.1007/s13530-015-0236-y</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_SPRINGER</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">7</subfield><subfield code="j">2015</subfield><subfield code="e">3</subfield><subfield code="c">09</subfield><subfield code="h">184-189</subfield></datafield></record></collection>
|
| author |
Sekhon, Simranjeet Singh |
| spellingShingle |
Sekhon, Simranjeet Singh misc Radio-Immunoprecipitation Assay buffer (RIPA buffer) misc Urea lysis buffer misc Two-dimensional gel electrophoresis misc Proteome profiling Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers |
| authorStr |
Sekhon, Simranjeet Singh |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)SPR031726593 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| author_role |
aut aut aut aut aut aut aut |
| collection |
springer |
| remote_str |
true |
| illustrated |
Not Illustrated |
| topic_title |
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 |
| topic |
misc Radio-Immunoprecipitation Assay buffer (RIPA buffer) misc Urea lysis buffer misc Two-dimensional gel electrophoresis misc Proteome profiling |
| topic_unstemmed |
misc Radio-Immunoprecipitation Assay buffer (RIPA buffer) misc Urea lysis buffer misc Two-dimensional gel electrophoresis misc Proteome profiling |
| topic_browse |
misc Radio-Immunoprecipitation Assay buffer (RIPA buffer) misc Urea lysis buffer misc Two-dimensional gel electrophoresis misc Proteome profiling |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
cr |
| hierarchy_parent_title |
Toxicology and Environmental Health Sciences |
| hierarchy_parent_id |
SPR031726593 |
| hierarchy_top_title |
Toxicology and Environmental Health Sciences |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)SPR031726593 |
| title |
Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers |
| ctrlnum |
(DE-627)SPR031728421 (SPR)s13530-015-0236-y-e |
| title_full |
Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers |
| author_sort |
Sekhon, Simranjeet Singh |
| journal |
Toxicology and Environmental Health Sciences |
| journalStr |
Toxicology and Environmental Health Sciences |
| lang_code |
eng |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
2015 |
| contenttype_str_mv |
txt |
| container_start_page |
184 |
| author_browse |
Sekhon, Simranjeet Singh Ahn, Ji-Young Shin, Woori Kim, Gonhyung Yoon, Hobaek Min, Jiho Kim, Yang-Hoon |
| container_volume |
7 |
| format_se |
Elektronische Aufsätze |
| author-letter |
Sekhon, Simranjeet Singh |
| doi_str_mv |
10.1007/s13530-015-0236-y |
| author2-role |
verfasserin |
| title_sort |
sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (ripa) and urea lysis buffers |
| title_auth |
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. |
| collection_details |
GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER |
| container_issue |
3 |
| title_short |
Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers |
| url |
https://dx.doi.org/10.1007/s13530-015-0236-y |
| remote_bool |
true |
| author2 |
Ahn, Ji-Young Shin, Woori Kim, Gonhyung Yoon, Hobaek Min, Jiho Kim, Yang-Hoon |
| author2Str |
Ahn, Ji-Young Shin, Woori Kim, Gonhyung Yoon, Hobaek Min, Jiho Kim, Yang-Hoon |
| ppnlink |
SPR031726593 |
| mediatype_str_mv |
c |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| doi_str |
10.1007/s13530-015-0236-y |
| up_date |
2024-07-04T01:00:59.562Z |
| _version_ |
1803608244421132288 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR031728421</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20201125152602.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201007s2015 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s13530-015-0236-y</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR031728421</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s13530-015-0236-y-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Sekhon, Simranjeet Singh</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Sample preparation for optimal proteomic profiling of rabbit muscle and tendon using radio-immunoprecipitation assay (RIPA) and urea lysis buffers</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2015</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">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.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Radio-Immunoprecipitation Assay buffer (RIPA buffer)</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Urea lysis buffer</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Two-dimensional gel electrophoresis</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Proteome profiling</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ahn, Ji-Young</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Shin, Woori</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kim, Gonhyung</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yoon, Hobaek</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Min, Jiho</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kim, Yang-Hoon</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Toxicology and Environmental Health Sciences</subfield><subfield code="d">Korean Society of Environmental Risk Assessment and Health Science, 2011</subfield><subfield code="g">7(2015), 3 vom: Sept., Seite 184-189</subfield><subfield code="w">(DE-627)SPR031726593</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:7</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:3</subfield><subfield code="g">month:09</subfield><subfield code="g">pages:184-189</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://dx.doi.org/10.1007/s13530-015-0236-y</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_SPRINGER</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">7</subfield><subfield code="j">2015</subfield><subfield code="e">3</subfield><subfield code="c">09</subfield><subfield code="h">184-189</subfield></datafield></record></collection>
|
| score |
7.4012823 |