Expression and purification of Litopenaeus vannamei allergen protein Lit v1.2 / 中国免疫学杂志
Chinese Journal of Immunology
;
(12): 1659-1662, 2015.
Article
in Chinese
| WPRIM
| ID: wpr-484782
ABSTRACT
Objective:
To obtain purified recombinant Litopenaeus vannamei allergen protein Lit v 1.2.Methods:
The target gene of Lit v 1.2 was inserted into clone vector pGEM-T and then ligated to the expression vector pET 44a.The pET44a-Liv 1.2 was transformed into Rosetta and screened by ampicillin resistance .The recombinant protein was expressed by IPTG induction .The protein was purified by 6-His tag affinity chromatography and the purification was analyzed by SDS-PAGE gel electrophoresis .Results:
The ex-pression plasmid pET44a-Lit v 1.2 was constructed.SDS-PAGE showed that expressed Lit v 1.2 was efficient and soluble in E.coli Rosetta.The protein molecular weight was consistent with the theoretical value .The highly purified target protein was obtained.Conclusion:
In this study ,we successfully gained highly purified recombinant allergen protein Lit v 1.2 which was expressed in prokaryotic system and purified by affinity chromatography column .The purified Lit v 1.2 protein will facilitate us to further study its role in immunological responses .
Full text:
Available
Index:
WPRIM (Western Pacific)
Language:
Chinese
Journal:
Chinese Journal of Immunology
Year:
2015
Type:
Article
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