http://rdf.ncbi.nlm.nih.gov/pubchem/patent/AU-2013202566-C1
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_f21c1009c60308a64b8e7dc0bb989632 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K19-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-62 |
| filingDate | 2013-04-05-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2018-07-12-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_41b2a917644e7647d953222d7c8c6b57 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_d5f3186aabda571cc88e21228823e8d1 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_e53bd74d8d74d721c11a8ba5a27949c9 |
| publicationDate | 2018-07-12-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | AU-2013202566-C1 |
| titleOfInvention | Proteolytically cleavable fusion protein comprising a blood coagulation factor |
| abstract | The invention relates to therapeutic fusion proteins in which a coagulation factor is fused to a half-life enhancing polypeptide, and both are connected by a linker peptide that is proteolytically cleavable. The cleavage of such linkers liberates the coagulation factor from any activity-compromising steric hindrance caused by the half-life enhancing polypeptide and, thereby, allows the generation of fusion proteins with high molar specific activity when tested in coagulation-related assays. Furthermore, the fact that the linker is cleavable can enhance the rates of inactivation and/or elimination after proteolytic cleavage of the peptide linker compared to the corresponding therapeutic fusion protein linked by the non-cleavable linker having the amino acid sequence GGGGGGV. |
| priorityDate | 2006-06-14-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 704.