Recombinant Human SULT1B1 protein is a Human Full Length protein, in the 1 to 296 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 - |
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Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3) and reverse triiodothyronine (rT3) (PubMed:28084139, PubMed:9443824, PubMed:9463486). 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 (PubMed:35165440).
ST1B2, SULT1B2, SULT1B1, Sulfotransferase 1B1, ST1B1, Sulfotransferase 1B2, Sulfotransferase family cytosolic 1B member 1, Thyroid hormone sulfotransferase
Recombinant Human SULT1B1 protein is a Human Full Length protein, in the 1 to 296 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl
purified by using conventional chromatography techniques.
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3) and reverse triiodothyronine (rT3) (PubMed:28084139, PubMed:9443824, PubMed:9463486). 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 (PubMed:35165440).
Belongs to the sulfotransferase 1 family.
SULT1B1 also known as Sulfotransferase Family 1B Member 1 is an enzyme that belongs to the sulfotransferase family. It has a molecular weight of approximately 34 kDa. This enzyme is mainly expressed in the liver and small intestine with some presence in the colon and brain. SULT1B1 participates in the sulfation process where it transfers a sulfo group to phenolic compounds aiding in their metabolism and detoxification.
Sulfotransferases like SULT1B1 are essential for the modulation and detoxification of hormones drugs and xenobiotics. This process plays an important role in maintaining balance within the body. While not known to form part of large complexes SULT1B1 works individually on its substrates altering their biological activity and solubility. This metabolic function ensures regulated activity and excretion of various compounds from the body.
SULT1B1 participates in both xenobiotic metabolism and hormone regulation pathways. In the context of xenobiotic metabolism SULT1B1 alongside enzymes like Cytochrome P450s carries out phase II reactions facilitating the elimination of foreign compounds from the body. In hormone regulation SULT1B1's function is to inactivate hormones such as thyroid hormones rendering them less active and promoting their clearance from circulation.
Aberrant activity or expression of SULT1B1 might relate to colorectal cancer and thyroid hormone imbalances. Altered sulfotransferase activity affects hormone regulation contributing to disorders like hypothyroidism. Additionally disruptions may link to other pathways involving proteins such as deiodinases in thyroid regulation emphasizing the importance of balanced sulfation activity in maintaining hormone homeostasis and preventing disease development.
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15% SDS-PAGE using 3µg of ab126691.
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