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Selection of aptamers for a protein target in cell lysate and their application to protein purification
Functional genomics requires structural and functional studies of a large number of proteins. While the production of proteins through over-expression in cultured cells is a relatively routine procedure, the subsequent protein purification from the cell lysate often represents a significant challeng...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2677892/ https://www.ncbi.nlm.nih.gov/pubmed/19304751 http://dx.doi.org/10.1093/nar/gkp176 |
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author | Javaherian, Sahar Musheev, Michael U. Kanoatov, Mirzo Berezovski, Maxim V. Krylov, Sergey N. |
author_facet | Javaherian, Sahar Musheev, Michael U. Kanoatov, Mirzo Berezovski, Maxim V. Krylov, Sergey N. |
author_sort | Javaherian, Sahar |
collection | PubMed |
description | Functional genomics requires structural and functional studies of a large number of proteins. While the production of proteins through over-expression in cultured cells is a relatively routine procedure, the subsequent protein purification from the cell lysate often represents a significant challenge. The most direct way of protein purification from a cell lysate is affinity purification using an affinity probe to the target protein. It is extremely difficult to develop antibodies, classical affinity probes, for a protein in the cell lysate; their development requires a pure protein. Thus, isolating the protein from the cell lysate requires antibodies, while developing antibodies requires a pure protein. Here we resolve this loop problem. We introduce AptaPIC, Aptamer-facilitated Protein Isolation from Cells, a technology that integrates (i) the development of aptamers for a protein in cell lysate and (ii) the utilization of the developed aptamers for protein isolation from the cell lysate. Using MutS protein as a target, we demonstrate that this technology is applicable to the target protein being at an expression level as low as 0.8% of the total protein in the lysate. AptaPIC has the potential to considerably speed up the purification of proteins and, thus, accelerate their structural and functional studies. |
format | Text |
id | pubmed-2677892 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-26778922009-05-15 Selection of aptamers for a protein target in cell lysate and their application to protein purification Javaherian, Sahar Musheev, Michael U. Kanoatov, Mirzo Berezovski, Maxim V. Krylov, Sergey N. Nucleic Acids Res Methods Online Functional genomics requires structural and functional studies of a large number of proteins. While the production of proteins through over-expression in cultured cells is a relatively routine procedure, the subsequent protein purification from the cell lysate often represents a significant challenge. The most direct way of protein purification from a cell lysate is affinity purification using an affinity probe to the target protein. It is extremely difficult to develop antibodies, classical affinity probes, for a protein in the cell lysate; their development requires a pure protein. Thus, isolating the protein from the cell lysate requires antibodies, while developing antibodies requires a pure protein. Here we resolve this loop problem. We introduce AptaPIC, Aptamer-facilitated Protein Isolation from Cells, a technology that integrates (i) the development of aptamers for a protein in cell lysate and (ii) the utilization of the developed aptamers for protein isolation from the cell lysate. Using MutS protein as a target, we demonstrate that this technology is applicable to the target protein being at an expression level as low as 0.8% of the total protein in the lysate. AptaPIC has the potential to considerably speed up the purification of proteins and, thus, accelerate their structural and functional studies. Oxford University Press 2009-05 2009-03-20 /pmc/articles/PMC2677892/ /pubmed/19304751 http://dx.doi.org/10.1093/nar/gkp176 Text en © 2009 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Methods Online Javaherian, Sahar Musheev, Michael U. Kanoatov, Mirzo Berezovski, Maxim V. Krylov, Sergey N. Selection of aptamers for a protein target in cell lysate and their application to protein purification |
title | Selection of aptamers for a protein target in cell lysate and their application to protein purification |
title_full | Selection of aptamers for a protein target in cell lysate and their application to protein purification |
title_fullStr | Selection of aptamers for a protein target in cell lysate and their application to protein purification |
title_full_unstemmed | Selection of aptamers for a protein target in cell lysate and their application to protein purification |
title_short | Selection of aptamers for a protein target in cell lysate and their application to protein purification |
title_sort | selection of aptamers for a protein target in cell lysate and their application to protein purification |
topic | Methods Online |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2677892/ https://www.ncbi.nlm.nih.gov/pubmed/19304751 http://dx.doi.org/10.1093/nar/gkp176 |
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