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Sulfate metabolites R-6-S and R-4'-S were generated from raloxifene in SULT293 expression HEK293 cells. Cellular excretion of the raloxifene sulfates was mainly mediated by BCRP and MRP4.
A systematic analysis showed that three of the twelve human SULTs, SULT1A1 (show SULT1A1 Proteins), SULT1A3 and SULT1C4 (show SULT1C4 Proteins), displayed the strongest sulphating activity towards acetaminophen.
This study aimed to establish SULT1A3 stably transfected HEK293 cells, and to determine the contributions of BCRP and MRP transporters to excretion of chrysin and apigenin sulfates.
Data indicate that protein-ligand interaction energy by using docking Quantitative Structure-Activity Relationships(QSAR) models showed accuracy of 67.28%, 78.00% and 75.46%, for the isoforms SULT1A1, SULT1A3 and SULT1E1, respectively.
The expression of ALDOA (show ALDOA Proteins) and/or SULT1A3 is significantly higher.
M-PST (show SULT1A4 Proteins) is involved in protective and detoxification mechanisms that may operate in neurodegenerative processes in the brain
structure-function relationships in the stereospecific and manganese-dependent 3,4-dihydroxyphenylalanine/tyrosine-sulfating activity of human monoamine-form phenol sulfotransferase (show SULT1A1 Proteins), SULT1A3
the differential substrate specificity of the two enzymes M-PST (show SULT1A4 Proteins) and P-PST (show SULT1A2 Proteins) for the thirteen drug compounds tested
For SULT1A3, substrate inhibition is found for dopamine but not with pNP (show NP Proteins). Based on modeling and kinetic studies, it is proposed that substrate inhibition by dopamine in SULT1A3 is caused by binding of two dopamine molecules in the active site.
Of the 11 human cytosol sulfotransferase enzymes tested, only SULT1A3 displayed sulfating activity toward nitrotyrosine. The pH-dependence and kinetic constants of SULT1A3 with nitrotyrosine or dopamine as substrate were determined.
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. This gene encodes a phenol sulfotransferase with thermolabile enzyme activity. Four sulfotransferase genes are located on the p arm of chromosome 16\; this gene and SULT1A4 arose from a segmental duplication. This gene is the most centromeric of the four sulfotransferase genes. Read-through transcription exists between this gene and the upstream SLX1A (SLX1 structure-specific endonuclease subunit homolog A) gene that encodes a protein containing GIY-YIG domains.
sulfotransferase family, cytosolic, 1A, phenol-preferring, member 3
, aryl sulfotransferase 1A3/1A4
, catecholamine-sulfating phenol sulfotransferase
, dopamine-specific sulfotransferase
, monoamine-sulfating phenosulfotransferase
, phenol sulfotransferase 1A5
, placental estrogen sulfotransferase
, sulfotransferase 1A3/1A4
, thermolabile (monoamine, M form) phenol sulfotransferase