Matches in DBpedia 2016-04 for { ?s ?p "Affilin® artificial proteins have the ability to selectively bind antigens. Affilin® is a registered trademark of Scil Proteins GmbH. Affilin proteins are structurally derived from human ubiquitin (historically also from gamma-B crystallin). Affilin proteins are constructed by modification of surface-exposed amino acids of these proteins and isolated by display techniques such as phage display and screening. They resemble antibodies in their affinity and specificity to antigens but not in structure, which makes them a type of antibody mimetic. Affilin proteins are being developed as potential new biopharmaceutical drugs, diagnostics and affinity ligands."@en }
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- Affilin abstract "Affilin® artificial proteins have the ability to selectively bind antigens. Affilin® is a registered trademark of Scil Proteins GmbH. Affilin proteins are structurally derived from human ubiquitin (historically also from gamma-B crystallin). Affilin proteins are constructed by modification of surface-exposed amino acids of these proteins and isolated by display techniques such as phage display and screening. They resemble antibodies in their affinity and specificity to antigens but not in structure, which makes them a type of antibody mimetic. Affilin proteins are being developed as potential new biopharmaceutical drugs, diagnostics and affinity ligands.".
- Q382468 abstract "Affilin® artificial proteins have the ability to selectively bind antigens. Affilin® is a registered trademark of Scil Proteins GmbH. Affilin proteins are structurally derived from human ubiquitin (historically also from gamma-B crystallin). Affilin proteins are constructed by modification of surface-exposed amino acids of these proteins and isolated by display techniques such as phage display and screening. They resemble antibodies in their affinity and specificity to antigens but not in structure, which makes them a type of antibody mimetic. Affilin proteins are being developed as potential new biopharmaceutical drugs, diagnostics and affinity ligands.".