|Synonyms||Biotin-Phenol; BP; N-(4-Hydroxyphenethyl)-5-((3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamide|
|Purity Chemicals||≥97% (HPLC)|
|Appearance||White to light pink solid.|
|Solubility||Soluble in DMSO or acetonitrile.|
|Identity||Determined by NMR.|
|Declaration||Manufactured by Chemodex.|
|Other Product Data||
Click here for Original Manufacturer Product Datasheet
|Shipping and Handling|
|Short Term Storage||+4°C|
|Long Term Storage||-20°C|
Keep cool and dry.
Protect from light and moisture.
|Use/Stability||Stable for at least 2 years after receipt when stored at -20°C.|
|Product Specification Sheet|
Biotin derivative. Substrate of the horseradish peroxidase enzyme and used as a reagent to amplify immunohistochemical signals. It is based on the HRP-catalyzed deposition of tyramide conjugates (such as biotinyl-tyramide) on a solid phase. Subsequent reaction with streptavidin fluorophore results in the localization of the fluorophore at the site of tyramide deposition. This fluorescence-based tyramide signal amplification (TSA) has been widely used in immunohistochemistry, immunoelectron microscopy, fluorescent in situ hybridization (FISH) and fluorescence ELISA. The TSA method has been reported to increase the detection sensitivity up to 100-fold as compared with conventional avidin–biotinylated enzyme complex procedures. It can be used together with both chromogenic and fluorescence visualization methods. It can be added to any other standard IHC protocol and reduces the use of other reagents; improves signal to noise by reducing the titer of other reagents in the assay protocol and enables multi-target detection in both IHC and (F)ISH applications.
(1) B. Hunyady, et al.; J. Histochem. Cytochem. 44, 1353 (1996) | (2) G. Mayer, et al.; J. Histochem. Cytochem. 45, 1449 (1997) | (3) J.A. McKay, et al.; Mol. Path. 50, 322 (1997) | (4) M.F. Evans, et al.; Mod. Pathol. 15, 1339 (2002) | (5) Q. Chenac, et al.; Anal. Lett. 45, 219 (2012) | (6) H. Gong, et al.; Anal. Bioch. 426, 27 (2012) | (7) E. Draberova, et al.; J. Immunol. Methods 395, 63 (2013)
RANKL deletion in periodontal ligament and bone lining cells blocks orthodontic tooth movement: C.Y. Yang, et al.; Int. J. Oral Sci. 10, 3 (2018)
Mapping the mammalian ribosome quality control complex interactome using proximity labeling approaches: N. Zuzow, et al.; MBoC, ahead of print (2018)
Identification of novel dense-granule proteins in Toxoplasma gondii by two proximity-based biotinylation approaches: M. Pan, et al.; J. Proteom. Res., in press (2018)
Proximity Labeling To Map Host-Pathogen Interactions at the Membrane of a Bacterium-Containing Vacuole in Chlamydia trachomatis-Infected Human Cells: M.G. Olson, et al.; Infect. Immun. 87, e00537 (2019)
Coupling APEX labeling to imaging mass spectrometry of single organelles reveals heterogeneity in lysosomal protein turnover: D.P. Narendra, et al.; J. Cell Biol. ahead of print, (2019)
Spatially resolved cell polarity proteomics of a human epiblast model: S. Wang, et al.; Sci. Adv. 7, (2021)