http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-2015049166-A1
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_31973d94de6256d5aae4938102b059e2 |
| classificationCPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y304-21004 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-37 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-6427 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-542 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-58 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-37 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-76 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-542 |
| filingDate | 2014-09-25-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_19cfdfe795506c2bfdb924ebae3c3fe9 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_790c5f08256bb115d3a833ed53fd32d1 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f0c97f8b2520acb5333b5357489892a7 |
| publicationDate | 2015-04-09-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | WO-2015049166-A1 |
| titleOfInvention | Human trypsinogen with reduced autoactivation and its use in an immunoassay |
| abstract | The present invention relatesto a polypeptideconsisting of or comprising a variant of human trypsinogen-1, comprising the substitutions: amino acid residue E64 is replaced with an amino acid residue comprising a positively charged side chain, amino acid residue K123 is replaced with an amino acid residue comprisingan aliphatic side chain and amino acid residues Y139 and D147 are replaced with a glutamine or asparagine residue, and wherein said variant is further characterized in that: an amino acid residue selected from E16, E17 and E142 is replaced with an amino acid residue comprising an aliphatic side chain, and/or amino acid residue N18 is replaced with a histidine residue, and/or amino acid residue R107 is replaced with a lysine residue, and/or amino acid residue D138 is replaced with an amino acid residue comprising a positively charged side chain, and wherein said variant is cleavable into a polypeptide having a native-like enzymatic activity when compared to human trypsin-1. |
| priorityDate | 2013-10-02-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 51.