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Bioconjugation technical handbook

Bioconjugation technical handbook Reagents for crosslinking, immobilization, modification, biotinylation, and fluorescent labeling of proteins and peptidesBioconjugation is the process of chemically joining two or more molecules or biomolecules by a covalent bond. This technique utilizes a variety of reagents for the crosslinking, immobilization, modification, and labeling of proteins and peptides. Bioconjugation reagents contain reactive ends to specific functional groups ( , primary amines, sulfhydryls) on proteins or other molecules. The availability of several chemical groups in proteins and peptides make them targets for a wide range of applications, including biotinylation, immobilization to solid supports, protein structural studies, and metabolic labeling. Chemical agents may be used to modify amino acid side chains on proteins and peptides in order to alter charges, block or expose reactive binding sites, inactivate functions, or change functional groups to create targets for crosslinking and labeling.

biomolecules such as proteins and nucleic acids. Protein modification ... free of primary amines can be measured at 260–280 nm, because the NHS byproduct absorbs in that range. ... interpretation of results when thiol-cleavable diimidoesters are used. Imidoester reagent

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