http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-114317576-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_9ecfd47f0f57946be6c39cc502f7a8ea |
| classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-19 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-70 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-61 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-66 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-18 |
| filingDate | 2020-09-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_5b6d8400a6ae4048a0c04a589e568df1 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_e8e19d1ee83d993547a24b897a6ecf2a http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_7b41772d761e8027f702a9b520d0e6de |
| publicationDate | 2022-04-12-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-114317576-A |
| titleOfInvention | Human growth hormone recombinant expression vector, engineering bacterium for expressing human growth hormone, construction method and application thereof |
| abstract | The invention provides a recombinant expression vector of human growth hormone, which is constructed by introducing human growth hormone DNA with a fusion tag and an enterokinase enzyme cutting site, the nucleotide sequence of which is shown as SEQ ID No.2, into an expression plasmid. The invention also provides engineering bacteria for efficiently expressing human growth hormone, a construction method and application thereof. The invention has the following technical effects: 1) the thioredoxin TrxA fusion tag can ensure that the intra-protein disulfide bond of the human growth hormone is correctly formed and the correct structure of the protein. The method has the advantages of promoting the full folding of human growth hormone in escherichia coli cells, improving the solubility of supernatant of human growth hormone protein after the bacteria are broken, and automatically shearing to finally obtain the human growth hormone without a fusion tag, thereby avoiding unnecessary human immunogenicity. 2) Besides the fusion tag of the thioredoxin TrxA, the fusion tag of the thioredoxin TrxA also has a His affinity tag, and the target protein with the purity of more than 95 percent can be obtained simply through affinity chromatography. |
| isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-115947864-A http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-115011568-A |
| priorityDate | 2020-09-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 135.