Fast and highly efficient purification of 6×histidine-tagged recombinant proteins by Ni-decorated MnFe2O4@SiO2@NH2@2AB as novel and efficient affinity adsorbent magnetic nanoparticles-Reference-Cited by-同舟云学术

Fast and highly efficient purification of 6×histidine-tagged recombinant proteins by Ni-decorated MnFe2O4@SiO2@NH2@2AB as novel and efficient affinity adsorbent magnetic nanoparticles

Published:2016 Issue:43 Volume:6 Page:36840-36848
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Rashid Zahra¹²³⁴⁵,Naeimi Hossein¹²³⁴⁵,Zarnani Amir-Hassan⁶⁷⁸⁹¹⁰,Nazari Mahboobeh¹¹⁷⁸⁹¹⁰,Nejadmoghaddam Mohammad-Reza¹¹⁷⁸⁹¹⁰,Ghahremanzadeh Ramin¹¹⁷⁸⁹¹⁰

Affiliation:

1. Department of Organic Chemistry

2. Faculty of Chemistry

3. University of Kashan

4. Kashan

5. I. R. Iran

6. Reproductive Immunology Research Center

7. Avicenna Research Institute

8. ACECR

9. Tehran

10. Iran

11. Nanobiotechnology Research Center

Abstract

A fast, convenient, and inexpensive method for the preparation of MnFe₂O₄@SiO₂@NH₂@2AB-Ni magnetic nanoparticles as an efficient and novel affinity adsorbent for the highly specific capture of 6×histidine-tagged recombinant protein-A is reported.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/RA/C5RA25949E

Reference52 articles.

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3. Protein production and purification

4. Nitrilotriacetic Acid-Modified Magnetic Nanoparticles as a General Agent to Bind Histidine-Tagged Proteins

5. Design and characterization of Ni2+ and Co2+ decorated Porous Magnetic Silica spheres synthesized by hydrothermal-assisted modified-Stöber method for His-tagged proteins separation

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