http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-112661849-B
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/Y02A50-30 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K16-40 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-85 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-535 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-573 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-569 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-13 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K16-12 |
| filingDate | 2020-12-17-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2022-05-20-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2022-05-20-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-112661849-B |
| titleOfInvention | Preparation method and application of clostridium difficile recombinant protein monoclonal antibody |
| abstract | The invention belongs to the field of biotechnology. The invention relates to a recombinant protein, which is formed by repeated tandem connection of two dominant antigen epitopes of Clostridium difficile membrane protein-Glutamate Dehydrogenase (GDH), and in order to improve the expression quantity of the recombinant protein in Escherichia coli, an amino acid sequence of the recombinant protein is converted into a corresponding nucleotide sequence by adopting an Escherichia coli preferred codon, the nucleotide sequence is chemically synthesized, and a recombinant expression vector is constructed. The invention also relates to a phage library established by the recombinant protein immunized mouse, a single-chain antibody scfv sequence corresponding to GDH is obtained through panning and screening, the obtained scfv sequence is constructed into a complete mouse IgG1 antibody sequence expression vector, a monoclonal antibody is expressed through transient HEK293F cells, the monoclonal antibody is purified and respectively marked with horseradish peroxidase (HRP), and the optimal monoclonal antibody pairing combination is determined through ELISA orthogonal experiments. |
| priorityDate | 2020-12-17-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 281.