http://rdf.ncbi.nlm.nih.gov/pubchem/patent/DE-102005050732-A1
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_313c2ac1c6159e38a96bd17d83b17a2b |
| classificationCPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2319-02 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-245 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-195 |
| filingDate | 2005-10-22-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_b9a0ab5e2b2d675262dd15a7ee528a14 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f5ebaeb4d512859b95cea28172c7a409 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_e5b0adf100d6b400a33f02525f8b0090 |
| publicationDate | 2007-04-26-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | DE-102005050732-A1 |
| titleOfInvention | Periplasmic production of therapeutically relevant proteins by fusion to Escherichia coli Ecotin |
| abstract | ThenThe present invention relates to a process for producing naturally foldednrecombinant proteins for use in medical diagnosticsnand therapy in a prokaryotic host. The host organismncontainsna recombinant DNA used fornencoded a fusion protein. The N-terminal part of the fusion proteinncoded fornthe Ecotin signal peptide from Escherichia coli and Ecotin. The C-terminalnPart of the fusion protein containsnthe sequence of the desirednrecombinant protein. The N- and C-terminal protein domains can therebynlinked by a short synthetic peptide sequencenbe. Whilenproduction in bacterial host cells becomes the fusion proteinnsecreted into the periplasm and it forms the natural foldednStructure. |
| priorityDate | 2005-10-22-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 169.