AS160 _ TBC1D4 Antibody
- Known as:
- AS160 _ TBC1D4 Antibody
- Catalog number:
- AF1117a
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- AS160 _ TBC1D4 Antibody
Related genes to: AS160 _ TBC1D4 Antibody
- Gene:
- TBC1D4 NIH gene
- Name:
- TBC1 domain family member 4
- Previous symbol:
- -
- Synonyms:
- KIAA0603, AS160, DKFZp779C0666
- Chromosome:
- 13q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-29
- Date modifiied:
- 2015-11-18
Related products to: AS160 _ TBC1D4 Antibody
Related articles to: AS160 _ TBC1D4 Antibody
- Homozygous carriers of a loss-of-function variant in the sucrase-isomaltase (SI) gene (c.273_274delAG) are unable to digest sucrose and parts of starch. The variant is common only in Indigenous Arctic populations such as the Greenlandic Inuit and has been associated with a healthier metabolic profile. In a unique gene-diet intervention, we aimed to study whether the SI genotype modulates the effect of two different diets on glucose homeostasis and lipids. - Source: PubMed
Publication date: 2026/04/17
Senftleber NinnaChristensen Marie Mathilde BCarstensen BendixStæger Frederik FilipFrøst Michael BGillum Matthew PHansen TorbenJørgensen Marit E - Skeletal muscle glucose transporter 4 (GLUT4) translocation to the plasma membrane determines glucose uptake in response to insulin and exercise and is disrupted in insulin resistance, making its experimental measurement critical. Confocal light microscopy is widely used for this purpose because of its ability to provide quantitative, high-resolution spatial information from small tissue amounts. However, conventional immunofluorescence colocalization microscopy lacks sensitivity and specificity in the detection of GLUT4 translocation. We validated the use of exofacial epitope-specific GLUT4 antibodies to quantify sarcolemmal GLUT4 translocation in fixed, nonpermeabilized adult human and rodent muscle fibers. Across human, mouse, and rat muscles, these antibodies sensitively detected stimulus-induced GLUT4 translocation, and labeling was abolished in muscle-specific GLUT4-knockout muscle, confirming specificity. Importantly, this study includes the first unambiguous visualization of endogenous GLUT4 translocation in intact human skeletal muscle fibers after insulin stimulation and exercise. In TBC1D4-knockout rats, insulin-stimulated GLUT4 translocation was absent despite wild-type-level GLUT4 expression, confirming an essential role for TBC1D4 in this process. Thus, exofacial GLUT4 antibodies provide a straightforward, sensitive, and specific approach to quantify endogenous GLUT4 translocation in fixed adult skeletal muscle. - Source: PubMed
Persson Kaspar WFjeldsøe CasperFrandsen Lukas WKnudsen Jonas RKwak SeongEunWang HaiyanVoldstedlund Christian TLeandersson Magnus RWitczak Carol AWojtaszewski Jørgen F PRichter Erik ACartee Gregory DJensen Thomas E - Our previous work demonstrated that wild Ehrh. possesses notable in vitro hypoglycemic activity. This study further evaluated the effects of wild Ehrh. polyphenol extract (WPPE) on T2DM mice. WPPE treatment significantly lowered blood glucose, improved insulin resistance, and reduced hepatic oxidative stress and inflammation in T2DM mice. It could promote the production of short-chain fatty acids and regulate the relative abundance of T2DM-associated bacteria like and , and enhance hepatic glycogen synthesis through activation of the key gene involved in the PI3K/AKT/TBC1D4 pathway, resulting in hypoglycemic effect based on the gut-liver axis. These findings support WPPE as a promising dietary candidate for T2DM management. - Source: PubMed
Publication date: 2026/02/08
Cheng XinpengXie XingLuo ShiboXie QuanyuanXiang HaiyanPeng ChunyanDing QiaoFan HongbingLiu WeiZhang Lu - RNF186, which encodes a ring-finger domain-containing E3 ubiquitin-protein ligase, has previously been implicated in the regulation of lipid metabolic disorders associated with metabolic dysfunction-related fatty liver disease (MAFLD). However, the precise mechanism by which RNF186 influences glucose metabolism in the context of MAFLD remains unclear. In this study, we aimed to elucidate the role of RNF186 in the regulation of glucose metabolism, with a particular focus on skeletal muscle. - Source: PubMed
Publication date: 2025/11/28
Du JiangDu QizhangZhang YuxuanGao JingwenWang ChihengKou BeilinJiang YanZhao DunyongLin Juntang - Circulating proteins play essential roles in complex diseases, yet protein quantitative trait locus (pQTL) studies in non-European, isolated populations remain limited. We analyzed genotypes and plasma proteomics data (Olink Target 96 Inflammation and Cardiovascular II panels) from 3,707 Greenlandic individuals (mean age: 47.9 years; 54.5% female), using linear mixed models to account for relatedness and population structure. Among 177 proteins, we identified 251 primary pQTLs-235 additive (84 cis, 8 semi-cis, 12 semi-trans, and 131 trans) and 16 recessive (1 cis, 2 semi-trans, and 13 trans)-48 secondary pQTLs, and 70 (28%) novel associations. Several common pQTLs in Greenlanders explained a substantial proportion of variance in protein levels (>30% for interleukin [IL]-27, IgG Fc receptor II-b, IL-16, and Galectin-9) compared to Europeans. A novel cis pQTL for IL-6 (rs7802307) was associated with increased cardiovascular disease risk based on registry data. Associations between Arctic-enriched variants in CPT1A (rs80356779), HNF1A (rs2135845768), TBC1D4 (rs61736969), LDLR (rs730882082), and PCSK9 (rs4609471) and altered protein abundance provide mechanistic insights into cardiometabolic disease in this population. These findings underscore the importance of pQTL studies in genetically diverse populations. - Source: PubMed
Publication date: 2025/11/12
Stinson Sara EBalboa Renzo FAndersen Mette KStæger Frederik FHe ShixuBaun Thuesen Anne CathrineLin LongJørsboe EmilBjerregaard PeterLarsen Christina V LGrarup NielsJørgensen Marit EMoltke IdaAlbrechtsen AndersHansen Torben