http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-110218737-B

Outgoing Links

Predicate Object
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http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2319-04
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http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K16-241
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http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-81
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-66
filingDate 2019-06-17-04:00^^<http://www.w3.org/2001/XMLSchema#date>
grantDate 2022-12-23-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationDate 2022-12-23-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber CN-110218737-B
titleOfInvention A recombinant vector that uses endoplasmic reticulum retention signal peptide to improve the antigen-binding ability of yeast cell surface to display Fab fragments
abstract The invention discloses a recombinant carrier which utilizes yeast endoplasmic reticulum retention signal peptide to improve the ability of yeast cell surface to display Fab fragment antigen binding, and belongs to the technical field of antibody engineering. The present invention uses the GAL1-GAL10 bidirectional promoter vector to simultaneously express the VH-CH1 and VL-CL domains of Adalimumab or Infliximab, and assembles natural Fab fragments in the endoplasmic reticulum through the amino-terminal endoplasmic reticulum positioning signal peptide. Then use the Aga1‑Aga2 yeast cell display system to display on the cell surface. At the same time, by fusing the endoplasmic reticulum retention signal peptide of Saccharomyces cerevisiae to the carboxy terminus of the VL-CL domain of the Fab fragment, the ability of the Fab fragment displayed on the yeast cell surface to bind antigens was significantly improved, and the display of functional Fab fragments was promoted, thereby It is more suitable for the yeast cell surface display of Fab fragments, and provides an optimized strategy for the Fab modification method in antibody engineering.
priorityDate 2019-06-17-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

Incoming Links

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Total number of triples: 26.