SULT1A1 (Human) IP-WB Antibody Pair
- Known as:
- SULT1A1 (Human) IP-Western Blot Antibody Pair
- Catalog number:
- H00006817-PW2
- Product Quantity:
- 1 Set
- Category:
- -
- Supplier:
- Abno
- Gene target:
- SULT1A1 (Human) IP- Antibody Pair
Related genes to: SULT1A1 (Human) IP-WB Antibody Pair
- Gene:
- SULT1A1 NIH gene
- Name:
- sulfotransferase family 1A member 1
- Previous symbol:
- STP, STP1
- Synonyms:
- P-PST
- Chromosome:
- 16p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1993-08-23
- Date modifiied:
- 2016-10-05
Related products to: SULT1A1 (Human) IP-WB Antibody Pair
Related articles to: SULT1A1 (Human) IP-WB Antibody Pair
- Positron emission tomography (PET) tracers targeting amyloid-β (Aβ) are central to the diagnosis and staging of Alzheimer's disease (AD). However, growing evidence indicates that these tracers can engage off-target molecules, complicating signal interpretation. Sulfotransferases (SULTs) have been experimentally identified as binding partners of 11C-Pittsburgh Compound-B (PiB), but whether the clinically used fluorinated PiB derivatives interact with brain-expressed SULTs has not been explored. - Source: PubMed
Publication date: 2026/09/19
Miccoli LudovicoFullone RosaDelli Pizzi StefanoTomaiuolo FedericaSensi Stefano LFloresta GiuseppeGranzotto Alberto - Severe tuberculosis (STB) imposes a substantial disease burden, yet reliable biomarkers for distinguishing STB from mild/moderate tuberculosis (MTB) remain scarce. This study aimed to identify and independently validate plasma protein biomarkers associated with tuberculosis severity. - Source: PubMed
Publication date: 2026/09/14
Hu YifanXue YuShu WeiRen WeicongLi RuiMa ZichunLiu RuichaoPang YuLi Liang - Female pattern hair loss (FPHL) is the most common cause of hair loss in women, yet therapeutic responses remain highly variable. A substantial proportion of patients experience persistent hair thinning or limited hair density improvement despite standard therapies, and current guidelines provide limited guidance for managing patients with poor therapeutic response. - Source: PubMed
Publication date: 2026/07/20
Li HaoyuZhang XinYang HanLi JiaxinYang Jing - To investigate the causal relevance of melatonin metabolism, which provides the biological basis for circulating melatonin levels, to specific depression symptom subtypes, we performed a targeted systematic review of melatonin metabolism pathways in the human brain and liver. Using two-sample Mendelian randomization (MR), we assessed the causal effects of metabolism pathways and/or individual genes on major depressive disorder (MDD) and nine symptom subtypes derived from Patient Health Questionnaire-9 (PHQ-9). Instrumental variables (IVs) were expression quantitative trait loci (eQTL) for eight individual genes, one synthesis route, and three degradation routes. Results were assessed using Bayesian colocalization and phenome-wide association analyses. At the pathway-level, the genetically proxied synthesis-route signal was associated with PHQ-9 Assessment 5 (PHQ9A5, OR: 0.89, 95% CI: 0.85-0.93), but sensitivity analyses suggested this association was primarily driven by TPH1 and may reflect serotonin-related biology. In contrast, higher brain melatonin degradation raised the risk of both PHQ9A1 (OR: 1.03, 95% CI: 1.02-1.04) and PHQ9A7 (OR: 1.03, 95% CI: 1.02-1.03). Within degradation, up-regulation of the kynurenine sub-pathway increased the odds of PHQ9A3 (OR: 1.05, 95% CI: 1.02-1.07), PHQ9A4 (OR = 1.04, 95% CI: 1.02-1.06) and PHQ9A7 (OR: 1.05, 95% CI: 1.02-1.07). Gene-level analyses were largely concordant, except for SULT1A1, whose higher expression was genetically protective for PHQ9A3 but risk-increased for PHQ9A1 and PHQ9A4. Overall, these results demonstrate that melatonin metabolism exerts symptom-specific and pathway-specific causal effects on depression. A stratified view of melatonin's role may help optimize the application of exogenous melatonin supplementation. - Source: PubMed
Publication date: 2026/07/30
Wang YuanbiWen WenChen HanshengJin YangyangCao JiechengChen WenzhongCai LeiHe Lin - During development, entry of any substances from the circulation into the brain is tightly regulated by a series of blood-brain interfaces. Notably, the choroid plexuses, which form the blood-cerebrospinal fluid barrier, serve as a key interface for molecular exchange in early life. Control mechanisms within the choroid plexuses include efflux transporters and conjugating enzymes, such as glutathione S-transferases and UDP-glucuronosyltransferases, which have been shown to play key roles in safeguarding the developing brain. Sulphotransferases are another family of conjugating enzymes reported to be highly expressed in the choroid plexus in humans and rats during development. However, their activity and functional significance in the central nervous system remain poorly understood. In the present study, sulphotransferase activity was measured in the lateral and fourth ventricle choroid plexus from rats at embryonic Day 19 and postnatal Day (P)1, 3, 8 and 30. Activity was correlated with expression of isoenzymes by RT-qPCR. Inhibition studies were performed by co-incubating a prototypical sulphotransferase substrate with a potential substrate or inhibitor. Finally, assays in freshly isolated live tissue were conducted to assess sulphoconjugation under more physiologically relevant conditions. Results showed that both sulphotransferase activity and expression of Sult1a1 in the choroid plexus were markedly increased at P1 to P3. This distinct temporal pattern suggests age- and tissue-specific roles of choroidal sulphotransferase activity during the early postnatal period. Interactions with xenobiotics and neuroendocrine factors further suggest that these enzymes may contribute to multiple processes during this critical window, including protection against potentially harmful substances and regulation of neurotransmitters. Furthermore, the observed modulation of choroidal sulphotransferase activity by various exogenous substances suggests that developmental exposure could disrupt sulphotransferase-mediated biological processes, with potential consequences for normal neurodevelopment. - Source: PubMed
Qiu FionaStrazielle NathalieDenuziere AnneGhersi-Egea Jean-François