Predicate |
Object |
assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_3ff8f50a324cedb30bdebcb00bdfd27b |
classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-6869 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2319-30 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2319-00 |
classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-70503 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-705 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-70539 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-435 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-62 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-46 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-47 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-6869 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K19-00 |
classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-435 |
filingDate |
2011-02-18-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f23ddea5bbf14abdcb6b17e19d5e07ed http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_1451ee80a2e2748dfe9a2b21eb0636f8 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_7e2402ef7580b903314f962ef7263228 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_93e7402be7c991071842c1098e6e2657 |
publicationDate |
2012-12-26-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber |
EP-2536746-A2 |
titleOfInvention |
Disulphide bond-stabilized functional soluble mhc class ii heterodimers |
abstract |
The present invention relates to disulphide bond stabilized recombinant MHC class II molecules. In particular, the present invention provides a recombinant MHC class II molecule, which comprises: (i) all or part of the extracellular portion of an MHC class II α chain; (ii) all or part of the extracellular portion of an MHC class II β chain; wherein (i) and (ii) provide a functional peptide binding domain and wherein (i) and (ii) are linked by a disulphide bond between cysteine residues located in the α2 domain of said α chain and the β2 domain of said β chain, wherein said cysteine residues are not present in native MHC class II α2 and β2 domains. Methods of producing these molecules in prokaryotic systems and various uses of these molecules form further aspects. |
priorityDate |
2010-02-18-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type |
http://data.epo.org/linked-data/def/patent/Publication |