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Data on the specificity of an antibody to Drosophila vesicular acetylcholine transporter

The role of the vesicular acetylcholine transporter (VAChT) in the regulation of cholinergic neurotransmission has not been fully elucidated. Here we sought to develop a tool for studying vesicular acetylcholine transporter function, and we present data on the validation of our new anti-VAChT antibo...

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Detalles Bibliográficos
Autores principales: Boppana, Sridhar, Lawal, Hakeem O.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5635202/
https://www.ncbi.nlm.nih.gov/pubmed/29034290
http://dx.doi.org/10.1016/j.dib.2017.09.008
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author Boppana, Sridhar
Lawal, Hakeem O.
author_facet Boppana, Sridhar
Lawal, Hakeem O.
author_sort Boppana, Sridhar
collection PubMed
description The role of the vesicular acetylcholine transporter (VAChT) in the regulation of cholinergic neurotransmission has not been fully elucidated. Here we sought to develop a tool for studying vesicular acetylcholine transporter function, and we present data on the validation of our new anti-VAChT antibody. We show that the immunoreactivity of the antibody is not due to an artifact of secondary antibody staining, and we present two additional validation data. First, the peptide epitope used to generate the antibody is able to block the binding of the anti-VAChT antibody in vivo. Further, RNA interference (RNAi) -mediated knockdown of VAChT function in cholinergic neurons drastically reduces anti-VAChT staining in those constructs. Additional evidence for the antibody functionality is presented in our research article on the subject (Boppana et al., 2017) [1].
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spelling pubmed-56352022017-10-13 Data on the specificity of an antibody to Drosophila vesicular acetylcholine transporter Boppana, Sridhar Lawal, Hakeem O. Data Brief Neurosciences    The role of the vesicular acetylcholine transporter (VAChT) in the regulation of cholinergic neurotransmission has not been fully elucidated. Here we sought to develop a tool for studying vesicular acetylcholine transporter function, and we present data on the validation of our new anti-VAChT antibody. We show that the immunoreactivity of the antibody is not due to an artifact of secondary antibody staining, and we present two additional validation data. First, the peptide epitope used to generate the antibody is able to block the binding of the anti-VAChT antibody in vivo. Further, RNA interference (RNAi) -mediated knockdown of VAChT function in cholinergic neurons drastically reduces anti-VAChT staining in those constructs. Additional evidence for the antibody functionality is presented in our research article on the subject (Boppana et al., 2017) [1]. Elsevier 2017-09-23 /pmc/articles/PMC5635202/ /pubmed/29034290 http://dx.doi.org/10.1016/j.dib.2017.09.008 Text en © 2017 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Neurosciences   
Boppana, Sridhar
Lawal, Hakeem O.
Data on the specificity of an antibody to Drosophila vesicular acetylcholine transporter
title Data on the specificity of an antibody to Drosophila vesicular acetylcholine transporter
title_full Data on the specificity of an antibody to Drosophila vesicular acetylcholine transporter
title_fullStr Data on the specificity of an antibody to Drosophila vesicular acetylcholine transporter
title_full_unstemmed Data on the specificity of an antibody to Drosophila vesicular acetylcholine transporter
title_short Data on the specificity of an antibody to Drosophila vesicular acetylcholine transporter
title_sort data on the specificity of an antibody to drosophila vesicular acetylcholine transporter
topic Neurosciences   
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5635202/
https://www.ncbi.nlm.nih.gov/pubmed/29034290
http://dx.doi.org/10.1016/j.dib.2017.09.008
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