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SULT1A1 Antibody (Center) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession P50225
Other Accession NP_001046
Clone Names 3112607
Additional Information
Gene ID 6817
Other Names Sulfotransferase 1A1, ST1A1, Aryl sulfotransferase 1, HAST1/HAST2, Phenol sulfotransferase 1, Phenol-sulfating phenol sulfotransferase 1, P-PST 1, ST1A3, Thermostable phenol sulfotransferase, Ts-PST, SULT1A1, STP, STP1
Target/Specificity The synthetic peptide sequence used to generate the antibody AP2606b was selected from the Center region of human SULT1A1. 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.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name SULT1A1
Synonyms STP, STP1
Function Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Displays broad substrate specificity for small phenolic compounds. Plays an important role in the sulfonation of endogenous molecules such as steroid hormones and 3,3'-diiodothyronin (PubMed:16221673, PubMed:12471039, PubMed:22069470, PubMed:21723874, PubMed:10199779, PubMed:7834621). Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil (By similarity). Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis (PubMed:7834621). May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4- ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system.
Cellular Location Cytoplasm {ECO:0000250|UniProtKB:P17988}.
Tissue Location Liver, lung, adrenal, brain, platelets and skin.
Research Areas
Citations (0)
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Background

Sulphation is a significant detoxification pathway for diverse xenobiotics, yet this modification also plays an important role in the metabolism and bioactivation of many dietary and environmental mutagens, including heterocyclic amines implicated in the pathogenesis of several cancers. A major human sulfotransferase, SULT1A1, metabolizes and/or bioactivates many endogenous compounds and is implicated in a range of cancers because of its ability to transform xenobiotics to cellular mutagens and carcinogens. Genetic polymorphisms in human sulfotransferase 1A1 SULT1A1 have a major impact on SULT1A1 enzyme activity and affect the risk for cancer development in humans. A G--->A transition at codon 213 (CGC/Arg to CAC/His) of the SULT1A1 gene has been identified (SULT1A1*2), and individuals homozygous for the His allele have a markedly lower activity and stability of this enzyme than those with the high activity SULT1A1*1 allozyme, which has been associated with protection against dietary toxins and reduced susceptibility to colorectal and breast cancers.There is an increasing incidence of SULT1A1*1 homozygosity and decreasing incidence of SULT1A1*2 homozygosity with increasing age, indicating a potential association of SULT1A1*1 allozyme(s) with protection against cell and/or tissue damage during aging. CLN3, the locus for Batten disease, maps to the same region 16p12.1-p11.2 as SULT12A1, making SULT1A1 a candidate gene for this disorder.

References

Carcinogenesis 25 (5), 773-778 (2004)J. Biol. Chem. 279 (18), 18799-18805 (2004)Cancer Lett. 202 (1), 61-69 (2003)J. Biol. Chem. 278 (9), 7655-7662 (2003)Int. J. Cancer 103 (1), 101-104 (2003)Chem. Biol. Interact. 129 (1-2), 141-170 (2000)

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$ 277.78
Cat# BP2606b
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