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anti-Human MLXIPL Anticorps:
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Human Polyclonal MLXIPL Primary Antibody pour ChIP, ICC - ABIN152902
Wang, Botolin, Xu, Christian, Mitchell, Jayaprakasam, Nair, Nair, Peters, Peters, Busik, Busik, Olson, Jump: Regulation of hepatic fatty acid elongase and desaturase expression in diabetes and obesity. dans Journal of lipid research 2006
Show all 97 Pubmed References
Human Polyclonal MLXIPL Primary Antibody pour ICC, IF - ABIN152903
Proszkowiec-Weglarz, Humphrey, Richards: Molecular cloning and expression of chicken carbohydrate response element binding protein and Max-like protein X gene homologues. dans Molecular and cellular biochemistry 2008
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Polyclonal MLXIPL Primary Antibody pour ChIP, IF - ABIN540821
Erhuma, Salter, Sculley, Langley-Evans, Bennett: Prenatal exposure to a low-protein diet programs disordered regulation of lipid metabolism in the aging rat. dans American journal of physiology. Endocrinology and metabolism 2007
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Polyclonal MLXIPL Primary Antibody pour IF, WB - ABIN540822
Letexier, Pinteur, Large, Fréring, Beylot: Comparison of the expression and activity of the lipogenic pathway in human and rat adipose tissue. dans Journal of lipid research 2003
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Human Polyclonal MLXIPL Primary Antibody pour IHC, IHC (p) - ABIN446286
Butcher, Torrecilla, Young, Kong, Mistry, Bottrill, Tobin: N-methyl-D-aspartate receptors mediate the phosphorylation and desensitization of muscarinic receptors in cerebellar granule neurons. dans The Journal of biological chemistry 2009
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Human Monoclonal MLXIPL Primary Antibody pour ICC, ELISA - ABIN1724913
Hurtado del Pozo, Vesperinas-García, Rubio, Corripio-Sánchez, Torres-García, Obregon, Calvo: ChREBP expression in the liver, adipose tissue and differentiated preadipocytes in human obesity. dans Biochimica et biophysica acta 2011
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Human Polyclonal MLXIPL Primary Antibody pour ICC, IF - ABIN4298323
Kaushik, Shojaie, Panzitt, Sonavane, Venghatakrishnan, Manikkam, Zaslavsky, Putluri, Vasu, Zhang, Khan, Lloyd, Szafran, Dasgupta, Bader, Stossi, Li, Samanta, Cao, Tsouko, Huang, Frigo, Chan, Edwards et al.: Inhibition of the hexosamine biosynthetic pathway promotes castration-resistant prostate cancer. ... dans Nature communications 2016
Human Monoclonal MLXIPL Primary Antibody pour ICC, IF - ABIN4298333
Ly, Maekawa, Yoshida, Liu, Muratani, Ishii: RNA-Sequencing Analysis of Paternal Low-Protein Diet-Induced Gene Expression Change in Mouse Offspring Adipocytes. dans G3 (Bethesda, Md.) 2019
we provide evidence that the rs1051943 A allele creates a functional miR-1322 binding site in ChREBP 3'-UTR and post-transcriptionally down-regulates its expression, possibly associated with levels of plasma lipids and glucose.
The expression levels of ChREBP and several cytokines (TNF-alpha, IL-1beta, and IL-6) were up-regulated in type 2 diabetes mellitus patients.
AKT2 drives de novo lipogenesis in adipocytes by stimulating ChREBPbeta transcriptional activity and that cold induces the AKT2-ChREBP pathway in brown adipose tissue to optimize fuel storage and thermogenesis.
ChREBP regulates gene transcription related to glucose and lipid metabolism. Findings from knockout mice and human subjects suggest that ChREBP helps to induce hepatic steatosis, dyslipidemia, and glucose intolerance. [review]
ChREBP and FGF21 constitute a signaling axis likely conserved in humans that mediates an essential adaptive response to fructose ingestion that may participate in the pathogenesis of NAFLD and liver fibrosis.
The results of this population-based study provide evidence for a relationship between lipid regulatory gene polymorphisms including GCKR (rs780094), GCKR (rs1260333), FADS (rs174547), and MLXIPL (rs3812316) with dyslipidemia in an Iranian population.
Data (including data from studies using tissues/cells from transgenic mice) suggest that ChREBPalpha up-regulates expression and activity of NRF2, initiating mitochondrial biogenesis in beta-cells; induction of NRF2 is required for ChREBPalpha-mediated effects and for glucose-stimulated beta-cell proliferation. [NRF2 = nuclear factor (erythroid-derived 2)-like 2 protein]
ChREBP was initially studied as a master regulator of lipogenesis in liver and fat tissue, it is now clear that ChREBP functions as a central metabolic coordinator in a variety of cell types in response to environmental and hormonal signals, with wide implications in health and disease.
A nutrient-sensitive mTOR/ChREBP regulated transcriptional network could be a novel target to improve beta cell survival and glucose homeostasis in diabetes.
these findings support a carbohydrate-mediated, ChREBP-driven mechanism that contributes to hepatic insulin resistance.
results indicated that the age and total cholesterol concentrations were independent influential factors of ChREBP methylation and DNMT1 variants could probably influence LDL-C to further modify ChREBP DNA methylation
p = 6.69 x 10(-9) ] on chr7 at the carbohydrate-responsive element-binding protein-encoding (MLXIPL) gene locus displayed significant protective characteristics, while another variant rs6982502 [0.76 (0.68-0.84); p = 5.31 x 10(-7) ] on chr8 showed similar but weaker properties.
ChREBP role in non-alcoholic fatty liver disease.The involvement of ChREBP in FASN promoter histone modification.
This cross-sectional study suggests that MLXIPL rs3812316 genotypes may be associated with Triglyceride levels. there were significantly different genotype distributions in two TG categories: (1) subjects with normal TG values had a significantly higher G allele frequency than those with elevated TG levels
The results revealed the novel mechanism by which HNF-4alpha promoted ChREBP transcription in response to glucose, and also demonstrated that ChREBP-alpha and HNF-4alpha synergistically increased ChREBP-beta transcription.
High glucose-mediated induction of PDGF-C via ChREBP in mesangial cells contributes to the development of glomerular mesangial expansion in diabetes.
Diet-induced obesity increases basal expression of ChREBPbeta, which may increase the risk of developing hepatic steatosis, and fructose-induced activation is independent of gluconeogenesis.
Evaluation of the conservation of ChREBP and MondoA sequences demonstrate that MondoA is better conserved and potentially mediates more ancient function in glucose metabolism.
Metformin down-regulates high-glucose-induced TXNIP transcription by inactivating ChREBP and FOXO1 in endothelial cells, partially through AMP-activated protein kinase activation
Data suggest that expression of ChREBPbeta isoform is up-regulated in pancreatic beta-cells in response to elevated levels of glucose (i.e., hyperglycemic conditions).
ChREBP activity might be required or dispensable for HCC growth.
The mRNA and protein levels of ChREBP were significantly elevated in the kidneys of diabetic mice.
The ChREBP is required for coordinated induction of glycolytic and lipogenic mRNAs.
observed that Myc and ChREBP cooperatively up-regulated virtually all ribosomal protein genes
Adenoviral ChREBP Overexpression Causes Higher Triglyceride Contents with Altered Lipid Composition. ChREBP Overexpression Lowers Plasma Triglyceride Levels by Modulating Angptl3 and Fgf21 Levels. These findings suggest that ChREBP may reciprocally regulate liver and plasma triglyceride levels
ChREBP plays a key role in the dietary fructose transport as well as conversion into lactate and glucose through direct transcriptional control of genes involved in fructose transport, fructolysis, and gluconeogenesis.
ChREBP and SHP control the regulation of hepatic microsomal triglyceride transfer protein expression and VLDL Secretion. Adenoviral Overexpression of ChREBP and SHP Respectively Increased and Decreased Mttp Expression.
The acute increase in circulating FGF21 following fructose gavage was absent in ChREBP knockout mice. Induction of ChREBP-beta and its glycolytic, fructolytic, and lipogenic gene targets were attenuated in FGF21 knockout mice fed high-fructose diets.
Data, including data from studies in knockout mice, suggest that ChREBP is involved in coordinate regulation of sucrose and fructose absorption/metabolism by modulating gene expression in intestinal mucosa and liver.
Authors have identified a previously unappreciated negative feedback loop by which glucose-induced ChREBP-beta downregulates ChREBP-alpha-signaling providing new insight into the physiological role of islet ChREBP-beta and into the regulation of glucose-induced gene expression.
loss of adipose-ChREBP is sufficient to cause insulin resistance potentially by regulating AT glucose transport.
Glucose-challenged Chrebp-/- mice exhibit a marked reduction in FGF21 production.
Study identify O-GlcNAcylation on Ser514 in the C-terminus of ChREBP and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function. Ser514 phosphorylation enhances ChREBP O-GlcNAcylation, maintaining the transcriptional activity of ChREBP; Ser839 O-GlcNAcylation is essential for its heterodimerization, DNA-binding activity, and nuclear export.
Data suggest that triiodothyronine and high glucose signal coordinately to up-regulate ChREBP, Ucp1, Glut4, and Fasn in brown adipocytes; ChREBP plays role as a central regulator of brown adipocyte activity/energy metabolism. (ChREBP = carbohydrate-responsive element-binding protein; Ucp1 = uncoupling protein-1; Glut4 = facilitated glucose transporter-4; Fasn = fatty acid synthase, type-I)
findings suggest that a previously unknown link exists between ChREBP and the regulation of cholesterol synthesis that affects liver injury.
findings also identified a role for ChREBP in regulating SREBP2-dependent cholesterol metabolism.
a high complex carbohydrate diet selectively increases hepatic ChREBPbeta expression, which associates with hepatic steatosis but not insulin resistance. In contrast, a high fat diet reduces adipose ChREBP, which associates with inflammation and insulin resistance.
This gene encodes a basic helix-loop-helix leucine zipper transcription factor of the Myc/Max/Mad superfamily. This protein forms a heterodimeric complex and binds and activates, in a glucose-dependent manner, carbohydrate response element (ChoRE) motifs in the promoters of triglyceride synthesis genes. The gene is deleted in Williams-Beuren syndrome, a multisystem developmental disorder caused by the deletion of contiguous genes at chromosome 7q11.23.
MLX interacting protein-like
, carbohydrate response element binding protein variant 1
, carbohydrate response element binding protein variant 2
, Williams-Beuren syndrome chromosomal region 14 protein homolog
, carbohydrate responsive element binding protein
, williams-Beuren syndrome chromosomal region 14 protein homolog
, MLX-interacting protein-like
, Mlx interactor
, WS basic-helix-loop-helix leucine zipper protein
, Williams Beuren syndrome chromosome region 14
, Williams-Beuren syndrome chromosome region 14 protein 1
, Williams-Beuren syndrome chromosome region 14 protein 2
, carbohydrate response element binding protein
, carbohydrate-responsive element-binding protein
, class D basic helix-loop-helix protein 14
, williams-Beuren syndrome chromosomal region 14 protein
, MLX interacting protein-like beta
, MLX interactor
, Williams-Beuren syndrome chromosome region 14 homolog
, putative hepatic transcription factor
, WBSCR14 protein-like
, Williams-Beuren syndrome chromosomal region 14 protein