Titlebook: Site-Specific Protein Labeling; Methods and Protocol Arnaud Gautier,Marlon J. Hinner Book 2015 Springer Science+Business Media New York 201

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Book 2015ormation on the design and generation of the organic molecules used for the labeling step. Chapters provide protocols for labeling techniques and applications, with an additional focus on general background information on the design and generation of the organic molecules used for the labeling step.

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2-Cyanobenzothiazole (CBT) Condensation for Site-Specific Labeling of Proteins at the Terminal Cystduction of N-terminal cysteine-containing proteins has been well developed for native chemical ligation. This protocol describes the preparation of . luciferase (rLuc) with 1,2-aminothiol at either its N- or C-terminus, and site-specific labeling of rLuc with fluorescein or .F via CBT condensation.

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Ligand-Directed Tosyl Chemistry for Selective Native Protein Labeling In Vitro, In Cells, and In Viion. Here we describe the principle of the LDT chemistry and the protocol for selective chemical labeling of native carbonic anhydrase in vitro, in blood cells (ex vivo), and in living mice (in vivo).

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Site-Specific Protein Labeling in the Pharmaceutical Industry: Experiences from Novartis Drug Discoe way down to biopharmaceuticals with improved properties such as antibody–drug conjugates. In the first part of the present chapter the significance and use of labeled proteins in biophysical methods, biochemical and cellular assays, in vivo imaging, and biopharmaceuticals is reviewed in general. I

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Getting Across the Cell Membrane: An Overview for Small Molecules, Peptides, and Proteins, often challenging, because to reach the cytosol, exogenous molecules must first traverse the cell membrane. This review provides a broad overview of how certain molecules are thought to cross this barrier, and what kinds of approaches are being made to enhance the intracellular delivery of those th

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Considerations and Protocols for the Synthesis of Custom Protein Labeling Probes,f specifically attaching chemical probes to individual proteins with spatial and temporal resolution has greatly improved our ability to visualize and characterize proteins in their native environment. The continued development of novel molecular probes for protein labeling is, therefore, of fundame

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Fluorescent Labeling of SNAP-Tagged Proteins in Cells,ltransferase (hAGT) that reacts specifically with benzylguanine (BG) and benzylchloropyrimidine (CP) derivatives, leading to covalent labeling of SNAP-tag with a synthetic probe (Gronemeyer et al., Protein Eng Des Sel 19:309–316, 2006; Curr Opin Biotechnol 16:453–458, 2005; Keppler et al., Nat Biote