Biotinyl tyramide or Biotin-Phenol has been used in proximity-dependent labeling for protein identification.[1][2]
Biochem/physiol Actions
Biotinyl tyramide is a reagent used for tyramide signal amplification for both immunohistochemistry (IHC) and in situ hybridization protocols and with either chromogenic or fluorescence detection. Preliminary binding of a probe is followed by secondary detection of the probe with an HRP-labeled antibody or streptavidin conjugate. Catalysis by the HRP results in the deposition of multiple biotinyl tyramide molecules in the immediate vicinity of the probe that can then be detected with a labeled streptavidin conjugate. Detection sensitivity can be 100-fold or more sensitive compared to conventional detection procedures.
Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc, 27(3), 326-331 (2015-04-10)
This study evaluated the sensitivity of biotinyl-tyramide-based in situ hybridization (TISH) method by comparison with chromogenic in situ hybridization (CISH) and immunohistochemical staining (IHC) methods. This study also determined the effect of fixative and fixation time on the detection of
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 48(12), 1593-1599 (2000-12-02)
To increase the sensitivity of fluorescence in situ hybridization (FISH) for detection of low-abundance mRNAs, we performed FISH on cryostat sections of rat hypothalamus with biotin-labeled riboprobes to leptin receptor (ObRb) and amplified the signal by combining tyramide signal amplification
Interphase chromatin is hierarchically organized into higher-order architectures that are essential for gene functions, yet the biomolecules that regulate these 3D architectures remain poorly understood. Here, we show that scaffold attachment factor B (SAFB), a nuclear matrix (NM)-associated protein with
Stress granules (SGs) are cytoplasmic assemblies of proteins and non-translating mRNAs. Whereas much has been learned about SG formation, a major gap remains in understanding the compositional changes SGs undergo during normal disassembly and under disease conditions. Here, we address
Proximity-dependent biotin labelling revealed undescribed participants of the ecdysone response in Drosophila. Two labelling enzymes (BioID2 and APEX2) were fused to EcR or Usp to biotin label the surrounding proteins. The EcR/Usp heterodimer was found to collaborate with nuclear pore
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