|Other Names||Sulfotransferase family cytosolic 1B member 1, ST1B1, Sulfotransferase 1B1, 282-, Sulfotransferase 1B2, ST1B2, Thyroid hormone sulfotransferase, SULT1B1, ST1B2, SULT1B2|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2600b was selected from the C-term region of human SULT1B1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized 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||Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine, reverse triiodothyronine and thyroxine.|
|Tissue Location||Highly expressed in the liver, peripheral blood leukocytes, colon (mucosal lining), small intestine (jejunum) and spleen. A lesser expression was observed in the lung, placenta and thymus.|
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Provided below are standard protocols that you may find useful for product applications.
Sulfotransferases such as SULT1B1 catalyze the biotransformation of a large number of endogenous compounds such as neurotransmitters, steroids, bile acids, and thyroid hormones, as well as drugs and xenobiotics. Fujita et al. (1997) demonstrated that recombinant rat and human SULT1B1, expressed in E. coli, catalyzed sulfation of p-nitrophenol, 3,3-prime,5-triiodothyronine (T3), and dopamine, but not of beta-estradiol and dehydroepiandrosterone. SULT1B1 showed higher affinities for formation of T3 sulfate than did the phenol sulfotransferases ST1A3 (SULT1A1) or ST1A5. Wang et al. (1998) found that bacterially-expressed SULT1B1 sulfated small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3-prime-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine. No activity was detected against several sterols or dopamine.
Fujita, K., et al., J. Biochem. 122: 1052-1061 (1997).Wang, J., et al., Molec. Pharm. 53: 274-282 (1998).
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