|Other Names||UDP-glucuronosyltransferase 2A1, UDPGT 2A1, UGT2A1, UGT2A2|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Active on odorants and seems to be involved in olfaction; it could help clear lipophilic odorant molecules from the sensory epithelium.|
|Cellular Location||Membrane; Single-pass type I membrane protein|
|Tissue Location||Olfactory epithelium and brain. Isoform 2 is mainly expressed in the nasal mucosa|
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Provided below are standard protocols that you may find useful for product applications.
The olfactory neuroepithelium, which lines the posteriornasal cavity, is exposed to a wide range of odorants and airbornetoxic compounds. Odorants, which are mostly small lipophilicmolecules, enter the mucus flow and reach the odorant receptors onsensory neurons. Odorant sensing is generally a transient process,requiring an effective signal termination, which could be providedby biotransformation of the odorant in the epithelial supportingcells. Xenobiotic-metabolizing enzymes in the olfactory epitheliumhave been suggested to catalyze inactivation and facilitateelimination of odorants.
Ross, C.J., et al. Nat. Genet. 41(12):1345-1349(2009)Saito, A., et al. J. Hum. Genet. 54(6):317-323(2009)Mackenzie, P.I., et al. Pharmacogenet. Genomics 15(10):677-685(2005)Iida, A., et al. J. Hum. Genet. 47(10):505-510(2002)
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