|Application ||WB, E|
|Calculated MW||35520 Da|
|Antigen Region||1-30 aa|
|Other Names||Sulfotransferase 1C4, ST1C4, 282-, Sulfotransferase 1C2, SULT1C#2, SULT1C4, SULT1C2|
|Target/Specificity||This SULT1C2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human SULT1C2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SULT1C2 Antibody (N-term) is for research use only and 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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