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.
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
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
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
The mechanisms underlying ribonucleoprotein (RNP) granule assembly, including the basis for establishing and maintaining RNP granules with distinct composition, are unknown. One prominent type of RNP granule is the stress granule (SG), a dynamic and reversible cytoplasmic assembly formed in
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
