Abstract: Disclosed herein is a phage-displayed single-chain variable fragment (scFv) library, that comprised a plurality of phage-displayed scFvs characterized with (1) a specific CS combination; (2) a specific distribution of aromatic residues in each CDR; and (3) a specific sequence in each CDR. The present scFv library could be used to efficiently produce different antibodies with binding affinity to different antigens. Accordingly, the present disclosure provides a potential means to generate different antigen-specific antibodies promptly in accordance with the need in experimental researches and/or clinical applications.

Abstract: Disclosed herein is a phage-displayed single-chain variable fragment (scFv) library, which comprises a plurality of phage-displayed scFvs characterized in having a specific CS combination and a specific sequence in each CDR. The present scFv library is useful in efficiently producing different antibodies with binding affinity to different antigens. Accordingly, the present disclosure provides a potential means to generate different antigen-specific antibodies promptly in accordance with the need in experimental researches and/or clinical applications.

Abstract: Disclosed herein is a phage-displayed single-chain variable fragment (scFv) library, that comprised a plurality of phage-displayed scFvs characterized with (1) a specific CS combination; (2) a specific distribution of aromatic residues in each CDR; and (3) a specific sequence in each CDR. The present scFv library could be used to efficiently produce different antibodies with binding affinity to different antigens. Accordingly, the present disclosure provides a potential means to generate different antigen-specific antibodies promptly in accordance with the need in experimental researches and/or clinical applications.

Abstract: Disclosed herein are phage-displayed single-chain variable fragment (scFv) libraries, which comprised a plurality of scFvs with a specific sequence in each CDR. The present scFv libraries could be used to efficiently produce different antibodies with high binding affinity to H1 hemagglutinin of influenza virus. Accordingly, the present disclosure provides a potential means to generate different antigen-specific antibodies promptly in accordance with the need in experimental researches and/or clinical applications.

Abstract: Disclosed herein is a phage-displayed single-chain variable fragment (scFv) library, that comprised a plurality of phage-displayed scFvs characterized with (1) a specific CS combination; (2) a specific distribution of aromatic residues in each CDR; and (3) a specific sequence in each CDR. The present scFv library could be used to efficiently produce different antibodies with binding affinity to different antigens. Accordingly, the present disclosure provides a potential means to generate different antigen-specific antibodies promptly in accordance with the need in experimental researches and/or clinical applications.

Abstract: Disclosed herein is a phage-displayed single-chain variable fragment (scFv) library, which comprises a plurality of phage-displayed scFvs characterized in having a specific CS combination and a specific sequence in each CDR. The present scFv library is useful in efficiently producing different antibodies with binding affinity to different antigens. Accordingly, the present disclosure provides a potential means to generate different antigen-specific antibodies promptly in accordance with the need in experimental researches and/or clinical applications.

Abstract: Disclosed herein is an immunoconjugate comprising an antibody, a functional motif, and a linker connecting the functional motif to the antibody. According to embodiments of the present disclosure, the antibody may recognize tumor-associated antigens (TAAs), and serves as a targeting module for delivering the functional motif connected therewith to the tumor cells thereby inhibiting tumor growth or detecting the distribution of tumor cells. Also disclosed herein are methods of treating cancers and methods of diagnosing cancers by use of the present immunoconjugate.

Abstract: Disclosed are nucleic acid libraries for identifying a signal peptide that facilitates production of disulfide-stabilized single chain antibody, and for facilitating production of a disulfide-stabilized single chain antibody. Also disclosed are host cell libraries and phage libraries including the nucleic acid libraries. Further disclosed are methods for identifying a signal peptide that facilitates production of disulfide-stabilized single chain antibody, and methods for producing a disulfide-stabilized single chain antibody and non-fusion form thereof.

Abstract: Disclosed herein is a phage-displayed single-chain variable fragment (scFv) library, that comprised a plurality of phage-displayed scFvs characterized with (1) a specific CS combination; (2) a specific distribution of aromatic residues in each CDR; and (3) a specific sequence in each CDR. The present scFv library could be used to efficiently produce different antibodies with binding affinity to different antigens. Accordingly, the present disclosure provides a potential means to generate different antigen-specific antibodies promptly in accordance with the need in experimental researches and/or clinical applications.

Abstract: Disclosed herein are methods for high-throughput screening of a functional antibody fragment for an immunoconjugate that targets a protein antigen. The method combines a phage-displayed synthetic antibody library and high-throughput cytotoxicity screening of non-covalently assembled immunotoxins or cytotoxic drug to identify highly functional synthetic antibody fragments for delivering toxin payloads.

Abstract: Disclosed herein are phage-displayed single-chain variable fragment (scFv) libraries, which comprised a plurality of scFvs with a specific sequence in each CDR. The present scFv libraries could be used to efficiently produce different antibodies with high binding affinity to H1 hemagglutinin of influenza virus. Accordingly, the present disclosure provides a potential means to generate different antigen-specific antibodies promptly in accordance with the need in experimental researches and/or clinical applications.

Abstract: Disclosed are nucleic acid libraries for identifying a signal peptide that facilitates production of disulfide-stabilized single chain antibody, and for facilitating production of a disulfide-stabilized single chain antibody. Also disclosed are host cell libraries and phage libraries including the nucleic acid libraries. Further disclosed are methods for identifying a signal peptide that facilitates production of disulfide-stabilized single chain antibody, and methods for producing a disulfide-stabilized single chain antibody and non-fusion form thereof.

Abstract: Disclosed are nucleic acid libraries for identifying a signal peptide that facilitates production of disulfide-stabilized single chain antibody, and for facilitating production of a disulfide-stabilized single chain antibody. Also disclosed are host cell libraries and phage libraries including the nucleic acid libraries. Further disclosed are methods for identifying a signal peptide that facilitates production of disulfide-stabilized single chain antibody, and methods for producing a disulfide-stabilized single chain antibody and non-fusion form thereof.

Abstract: Disclosed are nucleic acid libraries for identifying a signal peptide that facilitates production of disulfide-stabilized single chain antibody, and for facilitating production of a disulfide-stabilized single chain antibody. Also disclosed are host cell libraries and phage libraries including the nucleic acid libraries. Further disclosed are methods for identifying a signal peptide that facilitates production of disulfide-stabilized single chain antibody, and methods for producing a disulfide-stabilized single chain antibody and non-fusion form thereof.

Abstract: Disclosed are nucleic acid libraries for identifying a signal peptide that facilitates production of disulfide-stabilized single chain antibody, and for facilitating production of a disulfide-stabilized single chain antibody. Also disclosed are host cell libraries and phage libraries including the nucleic acid libraries. Further disclosed are methods for identifying a signal peptide that facilitates production of disulfide-stabilized single chain antibody, and methods for producing a disulfide-stabilized single chain antibody and non-fusion form thereof.