http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2016237419-A1
Outgoing Links
Predicate | Object |
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assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_31973d94de6256d5aae4938102b059e2 http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_eab56e4fe8837840887f41af83e328ee |
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/C12Q1-37 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N33-542 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-76 |
filingDate | 2014-09-25-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_1063b06eefbf319047ce8e02d819ea9f http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_426ef29e34224d08d1c3a3d224cbdca6 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_06d04c9bb747fcf2249ce07b36e07946 |
publicationDate | 2016-08-18-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber | US-2016237419-A1 |
titleOfInvention | Human trypsinogen with reduced autoactivation and its use in an immunoassay |
abstract | The present invention relates to a polypeptide consisting 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 comprising an 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: 223.