Production of antisera to synthetic decapeptide of the Cooh-Terminus of rat glut2
Autor(a) principal: | |
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Data de Publicação: | 1998 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Archives of Biology and Technology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89131998000200004 |
Resumo: | In the present study, the production of an anti-GLUT 2 antibody is reported. The antibody (S-5096) was raised in New Zealand rabbits immunized with an immunogen prepared by cross-linking the synthetic peptide and a carrier protein. A COOH-terminal decapeptide of rat GLUT 2 predicted sequence was synthesized and coupled to keyhole limpet hemocyanin, using the glutaraldehyde method. Subcellular membrane fractions were prepared from renal cortex (C) and medulla (M), and subjected to Western blotting analysis using the antiserum in a 1:200 dilution and, subsequently, [125I]protein A. As the results showed, the S-5096 anti-serum showed clear blots in kidney samples, stronger in cortex than in medulla as expected, whereas white adipose tissue and heart samples did not show any immunoreactivity. In addition, immunoblots were detected in samples prepared from duodenum and jejunum, as well as from isolated pancreatic B cells. In conclusion, the results clearly show that an anti-Glut 2 antibody, efficient enough to detect the rat protein by Western blotting analysis, was obtained. |
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Brazilian Archives of Biology and Technology |
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Production of antisera to synthetic decapeptide of the Cooh-Terminus of rat glut2glucose transporterGLUT 2antibodycoupling peptideIn the present study, the production of an anti-GLUT 2 antibody is reported. The antibody (S-5096) was raised in New Zealand rabbits immunized with an immunogen prepared by cross-linking the synthetic peptide and a carrier protein. A COOH-terminal decapeptide of rat GLUT 2 predicted sequence was synthesized and coupled to keyhole limpet hemocyanin, using the glutaraldehyde method. Subcellular membrane fractions were prepared from renal cortex (C) and medulla (M), and subjected to Western blotting analysis using the antiserum in a 1:200 dilution and, subsequently, [125I]protein A. As the results showed, the S-5096 anti-serum showed clear blots in kidney samples, stronger in cortex than in medulla as expected, whereas white adipose tissue and heart samples did not show any immunoreactivity. In addition, immunoblots were detected in samples prepared from duodenum and jejunum, as well as from isolated pancreatic B cells. In conclusion, the results clearly show that an anti-Glut 2 antibody, efficient enough to detect the rat protein by Western blotting analysis, was obtained.Instituto de Tecnologia do Paraná - Tecpar1998-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89131998000200004Brazilian Archives of Biology and Technology v.41 n.2 1998reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89131998000200004info:eu-repo/semantics/openAccessVestri,SandroNikami,HidekiSaito,MasayukiMachado,Ubiratan F.eng2011-07-27T00:00:00Zoai:scielo:S1516-89131998000200004Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2011-07-27T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
Production of antisera to synthetic decapeptide of the Cooh-Terminus of rat glut2 |
title |
Production of antisera to synthetic decapeptide of the Cooh-Terminus of rat glut2 |
spellingShingle |
Production of antisera to synthetic decapeptide of the Cooh-Terminus of rat glut2 Vestri,Sandro glucose transporter GLUT 2 antibody coupling peptide |
title_short |
Production of antisera to synthetic decapeptide of the Cooh-Terminus of rat glut2 |
title_full |
Production of antisera to synthetic decapeptide of the Cooh-Terminus of rat glut2 |
title_fullStr |
Production of antisera to synthetic decapeptide of the Cooh-Terminus of rat glut2 |
title_full_unstemmed |
Production of antisera to synthetic decapeptide of the Cooh-Terminus of rat glut2 |
title_sort |
Production of antisera to synthetic decapeptide of the Cooh-Terminus of rat glut2 |
author |
Vestri,Sandro |
author_facet |
Vestri,Sandro Nikami,Hideki Saito,Masayuki Machado,Ubiratan F. |
author_role |
author |
author2 |
Nikami,Hideki Saito,Masayuki Machado,Ubiratan F. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Vestri,Sandro Nikami,Hideki Saito,Masayuki Machado,Ubiratan F. |
dc.subject.por.fl_str_mv |
glucose transporter GLUT 2 antibody coupling peptide |
topic |
glucose transporter GLUT 2 antibody coupling peptide |
description |
In the present study, the production of an anti-GLUT 2 antibody is reported. The antibody (S-5096) was raised in New Zealand rabbits immunized with an immunogen prepared by cross-linking the synthetic peptide and a carrier protein. A COOH-terminal decapeptide of rat GLUT 2 predicted sequence was synthesized and coupled to keyhole limpet hemocyanin, using the glutaraldehyde method. Subcellular membrane fractions were prepared from renal cortex (C) and medulla (M), and subjected to Western blotting analysis using the antiserum in a 1:200 dilution and, subsequently, [125I]protein A. As the results showed, the S-5096 anti-serum showed clear blots in kidney samples, stronger in cortex than in medulla as expected, whereas white adipose tissue and heart samples did not show any immunoreactivity. In addition, immunoblots were detected in samples prepared from duodenum and jejunum, as well as from isolated pancreatic B cells. In conclusion, the results clearly show that an anti-Glut 2 antibody, efficient enough to detect the rat protein by Western blotting analysis, was obtained. |
publishDate |
1998 |
dc.date.none.fl_str_mv |
1998-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89131998000200004 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89131998000200004 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1516-89131998000200004 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
dc.source.none.fl_str_mv |
Brazilian Archives of Biology and Technology v.41 n.2 1998 reponame:Brazilian Archives of Biology and Technology instname:Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR |
instname_str |
Instituto de Tecnologia do Paraná (Tecpar) |
instacron_str |
TECPAR |
institution |
TECPAR |
reponame_str |
Brazilian Archives of Biology and Technology |
collection |
Brazilian Archives of Biology and Technology |
repository.name.fl_str_mv |
Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar) |
repository.mail.fl_str_mv |
babt@tecpar.br||babt@tecpar.br |
_version_ |
1750318267820408832 |