Recombinant Human SULT1C4 protein is a Human Full Length protein, in the 1 to 302 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic compounds. Can also sulfonate estrogenic compounds, however, the dietary flavonoids (phytoestrogen) and environmental estrogens, like bisphenol A are better substrates than 17beta-estradiol (E2) (PubMed:17425406, PubMed:26948952, PubMed:28222028, PubMed:9852044). Mediates the sulfation of doxorubicin and its analog epirubicin, two antitumor anthracyclines (PubMed:26948952).
SULT1C2, SULT1C4, Sulfotransferase 1C4, ST1C4, Sulfotransferase 1C2, SULT1C#2
Recombinant Human SULT1C4 protein is a Human Full Length protein, in the 1 to 302 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab156984 is purified using conventional chromatography techniques.
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic compounds. Can also sulfonate estrogenic compounds, however, the dietary flavonoids (phytoestrogen) and environmental estrogens, like bisphenol A are better substrates than 17beta-estradiol (E2) (PubMed:17425406, PubMed:26948952, PubMed:28222028, PubMed:9852044). Mediates the sulfation of doxorubicin and its analog epirubicin, two antitumor anthracyclines (PubMed:26948952).
Belongs to the sulfotransferase 1 family.
The protein SULT1C4 also known as Sulfotransferase Family 1C Member 4 catalyzes the sulfate conjugation of various hormones neurotransmitters drugs and xenobiotic compounds. It acts by transferring a sulfo group from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to these molecules which often results in their increased water solubility. This protein has a molecular mass of approximately 32 kDa. SULT1C4 expression occurs mainly in fetal tissues such as the liver and kidney indicating its potential importance during developmental stages.
Enzymes like SULT1C4 modify small molecules through the addition of sulfate groups altering their biological availability and activity. SULT1C4 does not appear to be part of a larger protein complex but its sulfation activity contributes to the modulation of molecular signaling pathways. This supports roles in detoxification processes and regulation of molecular activity through changes in solubility and molecular recognition.
Enzymes like SULT1C4 participate in the sulfation pathway that involves the phase II metabolism of xenobiotics. Within this pathway SULT1C4 works alongside other sulfotransferases such as SULT1A1 and SULT1E1 which also catalyze the sulfation of different substrates. SULT1C4 and these related proteins help in the detoxification pathway that enhances the clearance of drugs and bile acid metabolism.
Enzymes similar to SULT1C4 influence conditions related to impaired detoxification or hormonal imbalances. One such condition is thyroid disorder where sulfation can affect the availability of thyroid hormones. Another condition is cancer where the sulfation pathway can impact the activation or deactivation of carcinogens. In cancer for instance this enzyme might interact with proteins like cytochromes P450 altering the carcinogenic potential of certain compounds and impacting the disease progression.
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15% SDS-PAGE analysis of ab156984 (3μg).
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