Expression, purification and identification of the recombinant allergen Der p2 from Dermatophagoides pteronyssinus and investigation on its immunological activities.

Chinese Journal of Zoonoses(2009)

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摘要
The recombinant plasmid p-ET24a-Der-p2 was firstly transformed to E.coli JM109 and purified. Then it was induced to express in large amount with IPTG. After centrifugation of the bacterial cultures,the bacterial pellet was re-suspended and lysed by freezing-thawing treatment and ultrasonication. The inclusion bodies were purified by gel-filtration and chromatography. This highly purified allergen was shown to possess good IgE-binding activity as demonstrated by Western blotting. It suggests that this recombinant allergen can be used as a candidate in vaccine development for mite allergy.
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关键词
affinity chromatography,western blotting,recombinant allergen der p 2,protein expression,dermatophagoides pteronyssinus,gene expression,vaccination
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