Abstract
Affinity chromatography on Ni-nitrilotriacetic acid agarose was used to purify human mu-opioid receptors overexpressed in Sf9 cells. We introduced a tag of 6 consecutive histidines at its carboxyl terminus for easy purification of recombinant proteins. The binding activity and identification of the purified receptor were determined by receptor binding assay, SDS-PAGE and Western blotting analysis. This procedure used in the paper offer an easy and fast route to the purification of recombinant human mu-opioid receptors.
Keywords: BACULOVIRUS, opioid receptor (MOR), Spodoptera frugiperda, Trichoplusia ni, Receptor binding assay
Protein & Peptide Letters
Title: One-Step Affinity Purification of Human Mu-Opioid Receptor Overexpressed in Baculovirus System
Volume: 8 Issue: 4
Author(s): Chen Li. Wei, Feng Ya. Ping, Zhou De He, Xu xue-Jun, Chen Jie, Wei Qiang and Chi Zhi-Qiang
Affiliation:
Keywords: BACULOVIRUS, opioid receptor (MOR), Spodoptera frugiperda, Trichoplusia ni, Receptor binding assay
Abstract: Affinity chromatography on Ni-nitrilotriacetic acid agarose was used to purify human mu-opioid receptors overexpressed in Sf9 cells. We introduced a tag of 6 consecutive histidines at its carboxyl terminus for easy purification of recombinant proteins. The binding activity and identification of the purified receptor were determined by receptor binding assay, SDS-PAGE and Western blotting analysis. This procedure used in the paper offer an easy and fast route to the purification of recombinant human mu-opioid receptors.
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Cite this article as:
Wei Li. Chen, Ping Ya. Feng, He De Zhou, xue-Jun Xu, Jie Chen, Qiang Wei and Zhi-Qiang Chi, One-Step Affinity Purification of Human Mu-Opioid Receptor Overexpressed in Baculovirus System, Protein & Peptide Letters 2001; 8 (4) . https://dx.doi.org/10.2174/0929866013409373
DOI https://dx.doi.org/10.2174/0929866013409373 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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