SULT1B1 Proteins, Antibodies, cDNA Clones Research Reagents

SULT1B1 (Sulfotransferase Family 1B Member 1) is a protein coding gene located on human chromosome 4q13.3. SULT1B1 is also known as ST1B1, ST1B2 and SULT1B2. The human SULT1B1 gene encodes a 34899 Da protein containing 296 amino acids. The SULT1B1 protein is biasedly expressed in duodenum, small intestine and other tissues. Among its related pathways are Cytochrome P450 - arranged by substrate type and Sulfation Biotransformation Reaction. SULT1B1 is related to sulfotransferase activity and aryl sulfotransferase activity. SULT1E1 is an important paralog of SULT1B1 gene.

SULT1B1 Protein (1)

    SULT1B1 Antibody (2)

      SULT1B1 cDNA Clone (29)

      SULT1B1 qPCR Primer (1)

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      SULT1B1 Background

      Sulfotransferase family cytosolic 1B member 1, also known as Sulfotransferase 1B1, Sulfotransferase 1B2, Thyroid hormone sulfotransferase, SULT1B1 and ST1B2, is a cytoplasm protein that belongs to the sulfotransferase 1 family. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. SULT1B1 is highly expressed in the liver, peripheral blood leukocytes, colon (mucosal lining), small intestine (jejunum) and spleen. A lesser expression of SULT1B1 was observed in the lung, placenta and thymus. SULT1B1 catalyzes 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. SULT1B1 sulfates dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine, reverse triiodothyronine and thyroxine.

      SULT1B1 References

      • Fujita K. et al., 1997, J. Biochem. 122:1052-61.
      • Kester,MH.et al., 2003,Am J Physiol Endocrinol Metab. 285 (3):E592-8.
      • Meinl W, et al., 2001, Biochem Biophys Res Commun. 288 (4): 855-62.
      • Dombrovski L. et al., 2006, Proteins 64: 1091-4.

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