Articles with "fab" as a keyword



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Generation and selection of naïve Fab library for parasitic antigen: Anti‐BmSXP antibodies for lymphatic filariasis

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Published in 2018 at "Biotechnology and Applied Biochemistry"

DOI: 10.1002/bab.1591

Abstract: Phage display has been applied successfully as a tool for the generation of monoclonal antibodies (mAbs). Naive antibody libraries are unique as they are able to overcome several limitations associated with conventional mAb generation methods… read more here.

Keywords: lymphatic filariasis; bmsxp; fab; generation ... See more keywords
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Engineered FcRn Binding Fusion Peptides Significantly Enhance the Half-Life of a Fab Domain in Cynomolgus Monkeys.

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Published in 2019 at "Biotechnology journal"

DOI: 10.1002/biot.201800007

Abstract: There is a rapidly growing reinvigoration of the investigation of small proteins, cyclic peptides, and mAb derived domains as biotherapies. The drugability of these structures are challenged by fast peripheral clearance properties that can reduce… read more here.

Keywords: fcrn binding; cynomolgus monkeys; fab; fusion ... See more keywords
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Corrigendum to “Application of the NZ‐1 Fab as a crystallization chaperone for PA tag‐inserted target proteins”

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Published in 2020 at "Protein Science"

DOI: 10.1002/pro.3810

Abstract: Construct PDZ tandem (181-PA12-184) PDZ tandem (181-PA12-186) PDZ tandem (263-PA12-266) PDZ tandem (263-PA12-267) PDZ tandem (263-PA12-267) Form Fab-bound Fab-bound Fab-bound Fab-bound Fab-free Space group P212121 P212121 I422 P4212 P212121 Cell dimensions a, b, c (Å)… read more here.

Keywords: pdz tandem; pa12; bound fab; fab ... See more keywords
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A general platform for efficient extracellular expression and purification of Fab from Escherichia coli

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Published in 2019 at "Applied Microbiology and Biotechnology"

DOI: 10.1007/s00253-019-09745-8

Abstract: Antigen-binding fragments (Fabs) are an important part of monoclonal antibody (mAb) therapeutics and can be cost-effectively produced using an Escherichia coli (E. coli) expression system. However, Fabs tend to form undesirable aggregates when expressed in… read more here.

Keywords: general platform; escherichia coli; fab fragments; fab ... See more keywords
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NMR mapping of the highly flexible regions of 13C/15N-labeled antibody TTAC-0001-Fab.

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Published in 2020 at "Journal of biomolecular NMR"

DOI: 10.1007/s10858-020-00313-1

Abstract: Monoclonal antibody (mAb) drugs are clinically important for the treatment of various diseases. TTAC-0001 is under development as a new anti-cancer antibody drug targeting VEGFR-2. As the less severe toxicity of TTAC-0001 compared to Bevacizumab,… read more here.

Keywords: 13c 15n; antibody; fab; 15n labeled ... See more keywords
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Effect of DnaK/DnaJ/GrpE and DsbC Chaperons on Periplasmic Expression of Fab Antibody by E. coli SEC Pathway

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Published in 2017 at "International Journal of Peptide Research and Therapeutics"

DOI: 10.1007/s10989-017-9637-x

Abstract: Expression of recombinant protein that possess disulfide bonds especially Fab antibody fragment in periplasm of E. coli is the most favorable platform. But formation of inclusion bodies and inefficient translocation of desired protein to the… read more here.

Keywords: fab antibody; fab; dnak dnaj; effect ... See more keywords
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Optimal expression of a Fab-effector fusion protein in Escherichia coli by removing the cysteine residues responsible for an interchain disulfide bond of a Fab molecule.

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Published in 2017 at "Immunology letters"

DOI: 10.1016/j.imlet.2017.02.008

Abstract: Development of novel bi-functional or even tri-functional Fab-effector fusion proteins would have a great potential in the biomedical sciences. However, the expression of Fab-effector fusion proteins in Escherichia coli is problematic especially when a eukaryotic… read more here.

Keywords: effector fusion; fab; expression; fab effector ... See more keywords
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A universal phage display system for the seamless construction of Fab libraries.

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Published in 2017 at "Journal of immunological methods"

DOI: 10.1016/j.jim.2017.07.011

Abstract: The construction of Fab phage libraries requires the cloning of domains from both the light and the heavy chain of antibodies. Despite the advent of powerful strategies such as splicing-by-overlap extension PCR, obtaining high quality… read more here.

Keywords: construction fab; universal phage; fab libraries; fab ... See more keywords
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Cryo-EM structure of full-length HIV-1 Env bound with the Fab of antibody PG16.

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Published in 2020 at "Journal of molecular biology"

DOI: 10.1016/j.jmb.2019.11.028

Abstract: The HIV-1 envelope protein (Env) is the target of neutralizing antibodies and the template for vaccine immunogen design. The dynamic conformational equilibrium of trimeric Env influences its antigenicity and potential immunogenicity. Antibodies that bind at… read more here.

Keywords: cryo structure; hiv; fab; structure ... See more keywords
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Neutron Reflection Study of Surface Adsorption of Fc, Fab, and the Whole mAb.

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Published in 2017 at "ACS applied materials & interfaces"

DOI: 10.1021/acsami.7b06131

Abstract: Characterizing the influence of fragment crystallization (Fc) and antigen-binding fragment (Fab) on monoclonal antibody (mAb) adsorption at the air/water interface is an important step to understanding liquid mAb drug product stability during manufacture, shipping, and… read more here.

Keywords: neutron reflection; adsorption; surface; amount ... See more keywords
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Interaction of Periplasmic Fab Production and Intracellular Redox Balance in Escherichia coli Affects Product Yield

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Published in 2022 at "ACS Synthetic Biology"

DOI: 10.1021/acssynbio.1c00502

Abstract: Antibody fragments such as Fab’s require the formation of disulfide bonds to achieve a proper folding state. During their recombinant, periplasmic expression in Escherichia coli, oxidative folding is mediated by the DsbA/DsbB system in concert… read more here.

Keywords: fab; escherichia coli; intracellular redox; cell ... See more keywords