Nanobody (31 results)

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Taschenbuch. Condition: Neu. Anti-Schistosoma Nanobody Conjugate: A Novel Theranostic Tool | Single-Domain Antibody-Nanoparticles Conjugate: A Novel Tool for Diagnostic and Therapeutic Application | Mohamed Sallam | Taschenbuch | 144 S. | Englisch | 2013 | LAP LAMBERT Academic Publishing | EAN 9783659385681 | Verantwortliche Person für die EU: BoD - Books on Demand, In de Tarpen 42, 22848 Norderstedt, info[at]bod[dot]de | Anbieter: preigu.

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Taschenbuch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware 136 pp. Englisch.

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Taschenbuch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Nanobodies are recombinant single-domain antibodies of camelid origin. We set out to generate nanobodies as tools to study nuclear pore complexes (NPCs) that constitute the major passageways for nucleocytoplasmic exchange. Therefore, we developed an optimized phage display-based workflow for the generation of nanobodies from an immunized animal. The identified nanobodies were functionally expressed in the E. coli cytoplasm in a disulfide bond-free form, thus overcoming the engineering limitations imposed by conventional periplasmic secretion. Using protease-cleavable affinity tags, we developed a generic strategy for native protein complex isolation from eukaryotic sources, e.g. for structural analyses by electron microscopy. We further established a reliable fluorescent labeling strategy of nanobodies that is based on engineered surface cysteines and maleimide chemistry. In contrast to NHS labeling of lysines, maleimide labeling is site-specific, does not interfere with antigen recognition and yields superior imaging reagents, especially for super-resolution microscopy. Using our optimized workflow, we obtained a large toolbox of nanobodies against constituents of Xenopus NPCs that can now be used to study various unresolved aspects of NPC structure, assembly and function. 154 pp. Deutsch.

Taschenbuch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware 144 pp. Englisch.

Kartoniert / Broschiert. Condition: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. KlappentextrnrnNanobodies are recombinant single-domain antibodies of camelid origin. We set out to generate nanobodies as tools to study nuclear pore complexes (NPCs) that constitute the major passageways for nucleocytoplasmic exchange. Therefo.

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Condition: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Sallam MohamedMohamed Sallam is an Egyptian researcher at the DKFZ, Heidelberg, Germany. He has a B.Sc. in Biochemistry and an M.Sc. in Nanotechnology. During his research he applied many state-of-the-art techniques for the utilizati.

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Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Eukaryotic cells are divided into a nuclear and a cytoplasmic compartment. This separates transcription from translation and makes gene expression dependent on nucleocytoplasmic transport. The members of the importin ß superfamily function as shuttling nuclear transport receptors (NTRs) that recognize and actively transport cargoes through nuclear pores. An estimated 5 000 to 10 000 different human proteins are subject to active nuclear transport. Numerous cargo/NTR pairs have been identified, however, we are still far from a complete understanding as it has been very challenging to setup a systematic in vivo analysis that integrates the impact of all transport pathways.In this study, we obtained anti-NTR nanobodies against TRN1, Xpo4, Xpo7, and CAS. Our aim was to identify nanobodies, and prepare nanobody fusions, that impede nuclear pore-passage of the targeted NTR and thus, interrupt a given transport cycle. These nanobody fusions were observed to inhibit the partition of NTR/cargo complexes into a reconstituted FG phase. We also observed that the nanobodies and nanobody fusions inhibit NTR transport in permeabilized cells.Cuvillier Verlag, Nonnenstieg 8, 37075 Göttingen 136 pp. Englisch.

Taschenbuch. Condition: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Eukaryotic cells are divided into a nuclear and a cytoplasmic compartment. This separates transcription from translation and makes gene expression dependent on nucleocytoplasmic transport. The members of the importin ß superfamily function as shuttling nuclear transport receptors (NTRs) that recognize and actively transport cargoes through nuclear pores. An estimated 5 000 to 10 000 different human proteins are subject to active nuclear transport. Numerous cargo/NTR pairs have been identified, however, we are still far from a complete understanding as it has been very challenging to setup a systematic in vivo analysis that integrates the impact of all transport pathways.In this study, we obtained anti-NTR nanobodies against TRN1, Xpo4, Xpo7, and CAS. Our aim was to identify nanobodies, and prepare nanobody fusions, that impede nuclear pore-passage of the targeted NTR and thus, interrupt a given transport cycle. These nanobody fusions were observed to inhibit the partition of NTR/cargo complexes into a reconstituted FG phase. We also observed that the nanobodies and nanobody fusions inhibit NTR transport in permeabilized cells.

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Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Nanobodies are recombinant single-domain antibodies of camelid origin. We set out to generate nanobodies as tools to study nuclear pore complexes (NPCs) that constitute the major passageways for nucleocytoplasmic exchange. Therefore, we developed an optimized phage display-based workflow for the generation of nanobodies from an immunized animal. The identified nanobodies were functionally expressed in the E. coli cytoplasm in a disulfide bond-free form, thus overcoming the engineering limitations imposed by conventional periplasmic secretion. Using protease-cleavable affinity tags, we developed a generic strategy for native protein complex isolation from eukaryotic sources, e.g. for structural analyses by electron microscopy. We further established a reliable fluorescent labeling strategy of nanobodies that is based on engineered surface cysteines and maleimide chemistry. In contrast to NHS labeling of lysines, maleimide labeling is site-specific, does not interfere with antigen recognition and yields superior imaging reagents, especially for super-resolution microscopy. Using our optimized workflow, we obtained a large toolbox of nanobodies against constituents of Xenopus NPCs that can now be used to study various unresolved aspects of NPC structure, assembly and function.Cuvillier Verlag, Nonnenstieg 8, 37075 Göttingen 154 pp. Deutsch.

Taschenbuch. Condition: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Nanobodies are recombinant single-domain antibodies of camelid origin. We set out to generate nanobodies as tools to study nuclear pore complexes (NPCs) that constitute the major passageways for nucleocytoplasmic exchange. Therefore, we developed an optimized phage display-based workflow for the generation of nanobodies from an immunized animal. The identified nanobodies were functionally expressed in the E. coli cytoplasm in a disulfide bond-free form, thus overcoming the engineering limitations imposed by conventional periplasmic secretion. Using protease-cleavable affinity tags, we developed a generic strategy for native protein complex isolation from eukaryotic sources, e.g. for structural analyses by electron microscopy. We further established a reliable fluorescent labeling strategy of nanobodies that is based on engineered surface cysteines and maleimide chemistry. In contrast to NHS labeling of lysines, maleimide labeling is site-specific, does not interfere with antigen recognition and yields superior imaging reagents, especially for super-resolution microscopy. Using our optimized workflow, we obtained a large toolbox of nanobodies against constituents of Xenopus NPCs that can now be used to study various unresolved aspects of NPC structure, assembly and function.

Taschenbuch. Condition: Neu. A toolkit to study nuclear transport pathways: nanobody-mediated inhibition of importin ż-related nuclear transport receptors (NTRs) | Dilantha Perera | Taschenbuch | Englisch | 2023 | Cuvillier | EAN 9783736978478 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu Print on Demand.

Taschenbuch. Condition: Neu. Rapid nanobody discovery and novel nanobody engineering strategies for the study of the nuclear pore complex | Tino Pleiner | Taschenbuch | 154 S. | Deutsch | 2017 | Cuvillier | EAN 9783736995154 | Verantwortliche Person für die EU: BoD - Books on Demand, In de Tarpen 42, 22848 Norderstedt, info[at]bod[dot]de | Anbieter: preigu Print on Demand.

Taschenbuch. Condition: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering.

Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand Titel. Neuware VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 144 pp. Englisch.

Buch. Condition: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Nanobodies have become outstanding tools for biomedical research, diagnostics and therapy. Recent advances in the identification and functionalization of target-specific nanobodies now make nanobody-based approaches broadly available to many researches in the field. This book provides a compilation of original research articles and comprehensive reviews covering important and up to date aspects of research on nanobodies and their applications for immunoassays, proteomics, protein crystallization and in vitro and in vivo imaging.

Condition: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. KlappentextrnrnNanobodies have become outstanding tools for biomedical research, diagnostics and therapy. Recent advances in the identification and functionalization of target-specific nanobodies now make nanobody-based approaches broadly availa.