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publicationDate 2018-12-11-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber US-10150807-B2
titleOfInvention Method for isolation of soluble polypeptides
abstract Polypeptides with desirable biophysical properties such as solubility, stability, high expression, monomericity, binding specificity or non-aggregation, including monomeric human V H s and V L s, are identified using a high throughput method for screening polypeptides, comprising the steps of obtaining a phage display library, allowing infection of a bacterial lawn by the library phage, and identifying phage which form larger than average plaques on the bacterial lawn. Sequences of monomeric human V H s and V L s are identified, which may be useful for immunotherapy or as diagnostic agents. Multimer complexes of human V H s and V L s are also identified. The V H s and V L s identified may be used to create further libraries for identifying additional polypeptides. Further, the V H s and V L s may be subjected to DNA shuffling to select for improved biophysical properties.
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http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP13190
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9TQY7
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ91CD5
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP34006
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCO12980
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP35050
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ993M1
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9GKA1
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP34005
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP13391
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP35049
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP34747
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ3KSM3

Total number of triples: 321.