TrxA and SUMO double-solubilized expression tag sequence and application thereof

A technology for expressing tag sequences and solubilizing tags, applied in recombinant DNA technology, biochemical equipment and methods, using vectors to introduce foreign genetic material, etc. The effect is not very satisfactory and other problems, to save time and cost of research, promote correct folding, and accurate enzyme digestion
CN108300728AInactive Publication Date: 2018-07-20SHENYANG INST OF APPLIED ECOLOGY - CHINESE ACAD OF SCI
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Patent Information

Authority / Receiving Office
CN · China
Current Assignee / Owner
SHENYANG INST OF APPLIED ECOLOGY - CHINESE ACAD OF SCI
Publication Date
2018-07-20
Estimated Expiration
Not applicable · inactive patent

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Abstract

The invention relates to the fields of gene recombination and prokaryotic expression of proteins, and concretely relates to a double-solubilized expression tag sequence formed through fusing Escherichia coli thioredoxin TrxA and a small ubiquitin-like modifier SUMO, and an application thereof in a prokaryotic expression vector. An SUMO and TrxA double-solubilized expression tag has a base sequencerepresented by SEQ ID NO:1 in a sequence table. The sequence is applied to the upstream of the foreign protein encoding gene of the prokaryotic expression vector, and participates in fusion expression as a solubilizing tag together with a foreign gene in order to significantly promote the solubility of the expressed foreign protein and improve the recovery efficiency of a soluble foreign protein.
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Description

technical field

[0001] The present invention relates to the field of gene recombination and protein prokaryotic expression, specifically a dual prokaryotic expression tag, which is composed of Escherichia coli thioredoxin TrxA and small ubiquitin-like modification protein SUMO in series, which is used for prokaryotic expression vectors Upstream of foreign protein coding genes to promote correct folding of the expressed foreign protein and enhance solubility. Background technique

[0002] Since the prokaryotic expression system lacks an appropriate post-translational processing mechanism, in the process of expressing foreign proteins in Escherichia coli as the host bacteria, insoluble inclusion bodies will be formed due to incorrect protein folding, which requires complex denaturation and renaturation treatment again. It is difficult to express large amounts of soluble foreign protein.

[0003] Escherichia coli thioredoxin TrxA has the function of catalyzing the reduction of...

Claims

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