Modified Nanoantibodies Increase Sensitivity in Avidin-Biotin Immunohistochemistry
نویسندگان
چکیده
منابع مشابه
Unbinding biotin from avidin
Atomic force microscopy of single molecules, steered molecular dynamics and the theory of stochastic processes have established a new field that investigates mechanical functions of proteins, such as ligand–receptor binding/unbinding and elasticity of muscle proteins during stretching. The combination of these methods yields information on the energy landscape that controls mechanical function ...
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The crystal structures of a deglycosylated form of the egg-white glycoprotein avidin and of its complex with biotin have been determined to 2.6 and 3.0 A, respectively. The structures reveal the amino acid residues critical for stabilization of the tetrameric assembly and for the exceptionally tight binding of biotin. Each monomer is an eight-stranded antiparallel beta-barrel, remarkably simila...
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BACKGROUND Immunohistochemical methods based on the high affinity of avidin and biotin (e.g. ABC, LSAB) are characterized by high sensitivity and are widely used for detection of immunologic reaction. However, a non-specific reaction, observed in frozen tissues and in paraffin-embedded material, increasing after heat induced epitope retrieval (HIER), and caused either by endogenous biotin or an...
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ژورنال
عنوان ژورنال: Applied Immunohistochemistry & Molecular Morphology
سال: 2018
ISSN: 1541-2016
DOI: 10.1097/pai.0000000000000488