http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-108504670-B
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-50 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-70 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y208-01007 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-13 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-54 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-10 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-70 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-50 |
| filingDate | 2018-02-27-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2022-01-04-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2022-01-04-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-108504670-B |
| titleOfInvention | A kind of construction method and application of Escherichia coli cold shock aided expression plasmid |
| abstract | The invention relates to a construction scheme of an Escherichia coli soluble type expression plasmid and a method for preparing a water-soluble heterologous polypeptide by using the same. The seamless cloning technology is used to construct a cold-shock-assisted solubilization type expression plasmid which is fused and expressed by a small molecule ubiquitin-related modified protein (SUMO) controlled by the promoter of a cold-shock gene and an exogenous gene. A chimeric cysteine desulfurase is cloned into the plasmid of the present invention. Compared with the well-known pCold I and pET28 series plasmids, the water solubility, stability and enzymatic activity of the recombinant protein are obviously improved. Compared with the well-known pCold TF plasmid, SUMO does not affect the spatial conformation of the target protein. According to the ratio of Ulp1 protease and recombinant protein to 1U:0.5-1mg, at 25℃, the cleavage efficiency of SUMO tag is greater than 95%, and the cleavage efficiency of SUMO tag is more than 95%. It is very suitable for the preparation of natural N terminal protein. |
| priorityDate | 2018-02-27-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 65.