SULT1A1 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- 产品详情
- 实验流程
- 背景知识
Application ![]()
| WB, E |
---|---|
Primary Accession | P50225 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 34165 Da |
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 | This SULT1A1 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 246-279 amino acids of human SULT1A1. |
Dilution | WB~~1:1000 E~~Use at an assay dependent concentration. |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
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 | SULT1A1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
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 group. 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 (PubMed:12471039, PubMed:16221673, PubMed:21723874, PubMed:22069470, 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 (PubMed:35165440). Catalyzes the sulfate conjugation of dopamine (PubMed:8093002). Catalyzes the sulfation of T4 (L-thyroxine/3,5,3',5'- tetraiodothyronine), T3 (3,5,3'-triiodothyronine), rT3 (3,3',5'- triiodothyronine) and 3,3'-T2 (3,3'-diiodothyronine), with a substrate preference of 3,3'-T2 > rT3 > T3 > T4 (PubMed:10199779). |
Cellular Location | Cytoplasm. |
Tissue Location | Liver, lung, adrenal, brain, platelets and skin. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N- hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.
REFERENCES
Zhu X.,et al.Biochem. Biophys. Res. Commun. 195:120-127(1993).
Zhu X.,et al.Biochem. Biophys. Res. Commun. 192:671-676(1993).
Wilborn T.W.,et al.Mol. Pharmacol. 43:70-77(1993).
Yamazoe Y.,et al.Chem. Biol. Interact. 92:107-117(1994).
Hwang S.-R.,et al.Biochem. Biophys. Res. Commun. 207:701-707(1995).

终于等到您。ABCEPTA(百远生物)抗体产品。
点击下方“我要评价 ”按钮提交您的反馈信息,您的反馈和评价是我们最宝贵的财富之一,
我们将在1-3个工作日内处理您的反馈信息。
如有疑问,联系:0512-88856768 tech-china@abcepta.com.