|Other Names||Sulfotransferase 1C4, ST1C4, 282-, Sulfotransferase 1C2, SULT1C#2, SULT1C4, SULT1C2|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2608a was selected from the N-term region of human SULT1C2 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.|
|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 drugs, xenobiotic compounds, hormones, and neurotransmitters. May be involved in the activation of carcinogenic hydroxylamines. Shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF).|
|Tissue Location||Expressed at high levels in fetal lung and kidney and at low levels in fetal heart, adult kidney, ovary and spinal chord|
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Provided below are standard protocols that you may find useful for product applications.
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. The gene structure (number and length of exons) is similar among family members. SULT1C2 belongs to the SULT1 subfamily, responsible for transferring a sulfo moiety from PAPS to phenol-containing compounds. SULT1C2 belongs to a SULT subfamily that shows specificity for hydroxyarylamines. SULT1C2 catalyzes the sulfonation of p-nitrophenol and N-hydroxy-2-acetylaminofluorene, but not dopamine.
Mutat. Res. 482 (1-2), 27-40 (2001)Chem. Biol. Interact. 129 (1-2), 141-170 (2000)Genomics 65 (2), 157-165 (2000)J. Biol. Chem. 273 (51), 33929-33935 (1998).FASEB J. 11 (1), 3-14 (1997.
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