DHEA_S
- Known as:
- DHEA_S
- Catalog number:
- BQ 079S
- Product Quantity:
- 96/kit
- Category:
- -
- Supplier:
- Bioquant
- Gene target:
- DHEA_S
Related products to: DHEA_S
5-Androsten-3beta-OL-7, 17-Dione (DHEA) Antibody7a_Hydroxy DHEA 7a_Hydroxy DHEA7_Keto dehydroepi androsterone Keto DHEAAcP_ DHEAAnti- Dehydroepiandrosterone (DHEA) Sulfate-3 AntibodyAnti- Dehydroepiandrosterone (DHEA) Sulfate-7 AntibodyAntibody to Dehydroepiandrosterone (DHEA) Organism: Homo sapiens (Human) Type: Polyclonal Source: RabbitAntibody to Dehydroepiandrosterone (DHEA) Organism: Homo sapiens (Human) Type: Polyclonal Source: RabbitAntimicrobial Drugs: Natural Steroids: DEHYDROEPIANDROSTERONE SULPHATE (DHEA-S), Host animal: Sheep, Format: Purified monoclonal antibodyAntimicrobial Drugs: Natural Steroids: DEHYDROEPIANDROSTERONE SULPHATE (DHEA-S), Host animal: Sheep, Format: Purified monoclonal antibodyBile salt sulfotransferase,Dehydroepiandrosterone sulfotransferase,DHEA-ST,Homo sapiens,HST,HST,Human,Hydroxysteroid Sulfotransferase,ST2,ST2A1,ST2A3,STD,Sulfotransferase 2A1,SULT2A1Biotin-linked Antibody to Dehydroepiandrosterone (DHEA); Reactivity: Homo sapiens (Human) Clonality: Polyclonal Source: RabbitBovine Dehydroepiandrosterone ELISA , DHEABovine Dehydroepiandrosterone ELISA , DHEABovine Dehydroepiandrosterone(DHEA)ELISA Kit Related articles to: DHEA_S
- Digestive system disorders (DSDs) are prevalent and burdensome conditions worldwide. The human proteome serves as a primary source for designing disease treatment targets and holds great potential for drug repurposing. We applied Mendelian randomization analyses to examine the genetic associations between 2321 plasma proteins and 47 DSDs using data from the FinnGen project, identifying 12 causal proteins and validating four (Tripartite Motif Containing 40, Sulfotransferase Family 2A Member 1, Peptidase Inhibitor 16, MHC Class I Polypeptide-Related Sequence B) of them in the UK Biobank. Mediation analysis showed that SULT2A1 may increase the risk of cholelithiasis by reducing 25-hydroxyvitamin D levels. Molecular interaction simulations indicated that the interaction between SULT2A1 and 25-hydroxyvitamin D is comparable to that with the defined substrate 24-OHChol-24-sulfate. We found that elevated levels of SULT2A1 may increase metabolism of approved drugs for cholelithiasis (i.e., ursodeoxycholic acid and chenodeoxycholic acid) by binding deoxycholic acid, thus reducing drug efficacy. We applied the AlphaFold3 strategy to simulate interactions between SULT2A1 and 10,052 small molecules, identifying 5 molecules that may competitively bind to SULT2A1, potentially enhancing the treatment efficacy of deoxycholic acid for cholelithiasis. Overall, our study reveals several causal associations between plasma proteins and DSDs and identifies SULT2A1 as a promising drug repurposing target for cholelithiasis. - Source: PubMed
Publication date: 2026/04/17
Zhang ShixuanLiu ZhenqiuSun DayanWu FeiWei YangJin LiYang ShenHuang JinshiWang Jiucun - Given the existing uncertainties regarding the link between Di(2-ethylhexyl) phthalate (DEHP) exposure and gastric cancer (GC) progression, this study aimed to clarify their association, identify the toxic targets of DEHP, and elucidate the underlying molecular mechanisms. - Source: PubMed
Publication date: 2026/07/16
Li ShenghaoPeng QingHao LiyuanMao JingyuHuo Bingjie - Disruption of bile acid (BA) homeostasis and circadian rhythm are interconnected in chronic liver diseases, yet how circadian dysfunction exacerbates cholestasis remains unclear. This study demonstrates that hepatocyte-specific knockout of the core clock gene Bmal1 in female mice markedly aggravates liver injury, inflammation, and fibrosis in an α-naphthylisothiocyanate (ANIT)-induced intrahepatic cholestasis model. The pathological exacerbation is attributed to a profound loss of circadian oscillation and reduced expression of the detoxification enzyme sulfotransferase family 2A member 1 (SULT2A1), resulting in deficient sulfation and hepatic accumulation of cytotoxic bile acids. This hypersusceptibility was further validated in primary hepatocytes under BA overload. Notably, specific in vivo restoration of hepatic SULT2A1 significantly reversed these pathological progressions. Mechanistically, BMAL1 transcriptionally activates Sult2a1 by directly binding to the E-box element within its promoter region. Taken together, our work elucidates the BMAL1-SULT2A1 axis as an essential circadian defense mechanism that maintains hepatic bile acid detoxification homeostasis in female mice, providing a novel theoretical basis for chronotherapeutic strategies in cholestatic liver diseases. - Source: PubMed
Publication date: 2026/07/15
Xiao YifeiHe JiatianZheng YiZhang XinyuLi JintaoJin MengChen MinWu YushanLiu XiaowenXu HaimanLin LuominWu BaojianGuo LianxiaDong Dong - 24S-hydroxycholesterol (24SOH-Chol) is a bioactive cholesterol metabolite formed in the brain. This endogenous activator of the cholesterol sensor, liver X receptor (LXR) is abundantly found as a sulfate-glucuronide diconjugate in the human plasma. The present study characterizes the human sulfonating (SULT) and glucuronidating (UGT) enzymes; and evaluates how these enzymes impact its ability to bind to and activate LXR. In vitro enzymatic assays identified the human SULT2A1 and UGT1A4 as the major isoforms for hepatic 24SOH-Chol sulfonation and glucuronidation, respectively. Additional assays demonstrated that 24SOH-Chol-3Sulfate,24Glucuronide formation requires the successive involvement of UGT1A4 and SULT2A1. TR-FRET and transient transfection experiments revealed that glucuronidation, but not sulfonation, inactivates 24SOH-Chol. Exposure of human liver cells and humanized UGT1 mice to LXR ligands identified UGT1A4, but not SULT2A1, as a positively regulated LXR target gene, while chromatin immunoprecipitation assays, luciferase reporter and siRNA knock down assays demonstrated the ability of LXR to bind to and activate the human UGT1A4 gene promoter. The present study establishes the complementary roles played by SULT2A1 and UGT1A4 in 24SOH-Chol conjugation. We also identify glucuronidation as a mechanism allowing this cholesterol derivative to self-stimulate its own inactivation. - Source: PubMed
Publication date: 2026/07/13
Brousseau ValérieRettenmeier EvaVerreault MélanieTrottier JocelynChen ShujuanTukey Robert HBarbier Olivier - Liver fibrosis is a reversible phase of arsenic-induced chronic liver injury, with bile acid metabolic alterations closely associated with this pathological process. SIRT1 is a key metabolic regulator and promising therapeutic candidate, while its role in bile acid metabolism during arsenic-induced liver fibrosis remains poorly defined. This study established time-dependent rat models of arsenic-induced liver fibrosis with resveratrol intervention to investigate the potential association between SIRT1, bile acid metabolic disturbance, and liver fibrosis, as well as resveratrol's hepatoprotective effects. Arsenic exposure induces progressive accumulation of hydrophobic bile acids in the liver, inflammation, hepatic stellate cell activation, and fibrosis, accompanied by suppressed expression of bile acid phase II detoxification genes (, , ) and the bile acid efflux transporter gene (BSEP). Arsenic exposure reduces SIRT1 expression and increases C/EBPα acetylation, which may relate to impaired transcription of the aforementioned bile acid metabolic genes. Resveratrol may restore SIRT1 expression, normalize C/EBPα acetylation and bile acid homeostasis, and reduce hepatic arsenic accumulation, thereby alleviating liver fibrosis. Collectively, the SIRT1/C/EBPα axis and bile acid metabolism may be linked to the progression of arsenic-induced liver fibrosis. Resveratrol may exert protective effects via multiple mechanisms, including regulating these molecular targets and reducing hepatic arsenic accumulation. - Source: PubMed
Publication date: 2026/06/05
Wang QiChen HualinRan QimingHu FangFu QiwenMa Lu