Predicate |
Object |
assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_3155069b833b184bcd4ad12f7100dd4c |
classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y402-01022 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K38-00 |
classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-88 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P3-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P43-00 |
classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-88 |
filingDate |
2017-03-14-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f828543b04b3b769b00295de8daf68bd |
publicationDate |
2017-09-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber |
US-2017253865-A1 |
titleOfInvention |
Human Cystathionine Beta-Synthase Variants and Methods of Production Thereof |
abstract |
Human cystathionine β-synthase variants are disclosed, as well as a method to produce recombinant human cystathionine β-synthase and variants thereof. More particularly, the role of both the N-terminal and C-terminal regions of human CBS has been studied, and a variety of truncation mutants and modified CBS homologues are described. In addition, a method to express and purify recombinant human cystathionine β-synthase (CBS) and variants thereof which have only one or two additional amino acid residues at the N-terminus are described. |
isCitedBy |
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-11400143-B2 |
priorityDate |
2002-06-17-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type |
http://data.epo.org/linked-data/def/patent/Publication |