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anti-Human RBP4 Anticorps:
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Human Monoclonal RBP4 Primary Antibody pour IHC (p), ELISA - ABIN534873
Ahn, Choi, Kim, Lee, Lee, Bang, Cho: Increased retinol-binding protein (RBP) 4 and anti-RBP4 antibody in alopecia areata. dans The British journal of dermatology 2011
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Human Polyclonal RBP4 Primary Antibody pour ELISA, WB - ABIN542493
Yang, Graham, Mody, Preitner, Peroni, Zabolotny, Kotani, Quadro, Kahn: Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes. dans Nature 2005
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Human Monoclonal RBP4 Primary Antibody pour ICC, FACS - ABIN969380
van Hoek, Dehghan, Zillikens, Hofman, Witteman, Sijbrands: An RBP4 promoter polymorphism increases risk of type 2 diabetes. dans Diabetologia 2008
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Human Polyclonal RBP4 Primary Antibody pour IHC, IHC (p) - ABIN4349659
Kelly, Kashyap, OLeary, Major, Schauer, Kirwan: Retinol-binding protein 4 (RBP4) protein expression is increased in omental adipose tissue of severely obese patients. dans Obesity (Silver Spring, Md.) 2010
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Human Monoclonal RBP4 Primary Antibody pour IHC (p), ELISA - ABIN519688
Petta, Tripodo, Grimaudo, Cabibi, Cammà, Di Cristina, Di Marco, Di Vita, Ingrao, Mazzola, Marchesini, Pipitone, Craxì: High liver RBP4 protein content is associated with histological features in patients with genotype 1 chronic hepatitis C and with nonalcoholic steatohepatitis. dans Digestive and liver disease : official journal of the Italian Society of Gastroenterology and the Italian Association for the Study of the Liver 2011
Human Monoclonal RBP4 Primary Antibody pour IHC (p), ELISA - ABIN562609
Artner, Hang, Mazur, Yamamoto, Guo, Lindner, Magnuson, Stein: MafA and MafB regulate genes critical to beta-cells in a unique temporal manner. dans Diabetes 2010
Dog (Canine) Polyclonal RBP4 Primary Antibody pour ELISA, WB - ABIN547821
Soares, Coelho, Sousa, Batalov, Conceição, Sales-Luís, Ritchie, Williams, Nievergelt, Schork, Saraiva, Buxbaum: Susceptibility and modifier genes in Portuguese transthyretin V30M amyloid polyneuropathy: complexity in a single-gene disease. dans Human molecular genetics 2005
Human Polyclonal RBP4 Primary Antibody pour ELISA, WB - ABIN1169042
Sung, Hong, Suh, Cho, Park, Bae, Park, Han, Song: Role of (-)-epigallocatechin-3-gallate in cell viability, lipogenesis, and retinol-binding protein 4 expression in adipocytes. dans Naunyn-Schmiedeberg's archives of pharmacology 2010
Mouse (Murine) Polyclonal RBP4 Primary Antibody pour ELISA, WB - ABIN1169044
Chiefari, Paonessa, Iiritano, Le Pera, Palmieri, Brunetti, Lupo, Colantuoni, Foti, Gulletta, De Sarro, Fusco, Brunetti: The cAMP-HMGA1-RBP4 system: a novel biochemical pathway for modulating glucose homeostasis. dans BMC biology 2009
Elevated serum levels of RBP4 at admission were associated with severity and prognosis of ischemic stroke patients.
SLC2A4, RBP4, PCK1, and PIK3R1 genes may be involved in the pathogenesis of GDM.
A mixed model approach identifies a functional variant in the RBP4 gene associated with HDL-C dyslipidemia the in Newfoundland and Labrador population.
RBP4 levels were significantly decreased and positively related with T in men with CAD. Higher RBP4 levels were associated with lower risk of CAD.
The present study shows that elevated plasma levels of RBP4 were associated with diabetic retinopathy and vision-threatening diabetic retinopathy in Chinese patients with type 2 diabetes, suggesting a possible role of RBP4 in the pathogenesis of diabetic retinopathy complications. Lowering RBP4 could be a new strategy for treating type 2 diabetes with diabetic retinopathy .
Excessive adiposity without co-morbidities is not associated with higher levels of circulating RBP4. Serum RBP4 cannot be considered as a direct predictive marker for impaired glucose metabolism. RBP4 possibly contributes to lipid metabolism.
Also during a high-fat diet challenge, elevated levels of RBP4 in the circulation failed to aggravate the worsening of systemic parameters of glucose and energy homeostasis. These findings show that liver-secreted RBP4 does not impair glucose homeostasis. We conclude that a modest increase of its circulating levels in mice, as observed in the obese, insulin-resistant state, is unlikely to be a causative factor for impaire
in older subjects, circulating RBP4 levels are mostly affected by kidney function and modestly by age, gender, and nutritional status, but not insulin resistance.
Single nucleotide polymorphism rs1501299 in the gene ADIPOQ (P=0.0010, OR=0.41, 95% C.I.:0.24-0.70) and rs7501331 in the gene BCMO1 (P=0.0106, OR=0.24, 95% C.I.:0.21-0.71), are significantly associated (the latter marginally significant) with the decrease of the polycystic ovary syndrome.
Childhood RBP4 serves as a risk factor for subsequent development of metabolic syndrome and its components, independent of pediatric obesity.
In Caucasians 65 years and older, RBP4 serum levels are associated with a number of components of metabolic syndrome.
Baseline RBP4 levels and MELD scores predicted 21-day (=10 mg/L) and 1-year (>/=25) mortality, respectively. In critically ill patients with underlying liver disease, with a link to eGFRs, INRs and TC levels, the baseline RBP4 may serve as a marker for short-term mortality.
our study provides clinical evidence revealing that the serum concentrations of RBP4 were elevated in NAFLD patients in a Chinese population. These findings indicated that RBP4 might be a noninvasive molecular biomarker that detects the presence of NAFLD in middle-aged and elderly population.
Vitreous levels of APOA1 and RBP4 in human rhegmatogenous retinal detachment associated with choroidal detachment reflects the severity of disease.
The overexpression of RBP4 increased cell proliferation, whereas siRNA-mediated RBP4 knockdown significantly decreased HTR8/SVneo cell proliferation via activation of PI3K/AKT signaling.
High RBP4 expression is associated with hypertriglyceridemia.
We observed that knockdown of RBP4 can greatly suppress ovarian cancer cell migration and proliferation.
This study showed that the Levels of circulating RBP4 was significantly higher in Chronic Kidney Disease than in control.
Our results demonstrate that IR is associated with high circulating RBP4 and that suppressed RBP4 adipose tissue expression is accompanied by reduced GLUT4 expression in HD. Renal transplantation or HDF are effective in lowering serum RBP4 levels.
Data suggest that serum levels of RBP4 and LGAL3BP are up-regulated after menopause when complicated by NAFLD (non-alcoholic fatty liver disease); RBP4 and LGAL3BP may serve as biomarkers of NAFLD in postmenopausal women. (RBP4 = retinol binding protein 4; LGAL3BP = galectin-3 binding protein)
There were no statistical differences between the BB genotype and the AB genotype of ESR2 locus in regard to the examined traits. However, a noticeable superiority (P < 0.01) of the BB genotype compared to the homozygous AA genotype, adding almost 2 piglets/litter in TNB and NBA trait, was found.
RBP4 has a role in adipogenesis of porcine preadipocytes through the insulin signaling pathways
Data show that there were two genotypes for RBP4 gene in Tibet pig, which did not have significant effect on the reproductive traits.
The aim of this work was to study the effects on litter size of variants of the porcine genes RBP4, ESR1 and IGF2, currently used in genetic tests for different purposes.
Response to selection for increased litter size could not be attributed to effects at the estrogen receptor, retinol-binding protein or follistatin loci.
study found significant association of two diallelic polymorphisms in the porcine genes for leukaemia inhibitory factor (LIF) and retinol-binding protein 4 (RBP4) with number of piglets born alive (NBA) in two German pig lines
The results showed that the polymorphic sites of both PRLR and RBP4 genes are closely related to litter size traits.
progesterone modulates uterine RBP4 mRNA and protein abundance in a time- and concentration-dependent manner.
Two novel single nucleotide polymorphisms (SNPs) and 4-bp deletion mutation of RBP4 gene in Chinese cattle
results suggest that retinol-binding protein 4 is transferred from maternal stores to calves through colostrum
Serum albumin and serum retinol-binding protein(sRBP) are not components of bovine interphotoreceptor matrix(IPM). Serum albumin and sRBP can not participate in binding and transport of visual cycle retinoids in IPM of bovine retina.
RBP4 is involved in all-trans retinoic acid-induced cleft palate.
RBP4-induced inflammation is largely mediated by TLR4.
New insights into ghrelin cell physiology, and given the known functions of RBP4 and TTR, support an emerging role for the ghrelin cell in blood glucose handling and metabolism.
Retinal degeneration in RBP4-Tg mice is RBP4-dependent and light-independent.
Rbp4-deficient mice accumulated retinol in the liver but it was undetectable in the serum, indicating an inverse relation between serum and liver retinol levels. RBP4 is critical for the mobilization of retinol from hepatic storage pools, and such mobilization is necessary for ocular development and visual function.
Hepatocytes Are the Principal Source of Circulating RBP4 in Mice
RBP4 may be a critical modulator promoting the vicious cycle of insulin resistance and heart failure by activating TLR4/MyD88-mediated inflammatory pathways. Potentially, lowering RBP4 might break the vicious cycle and improve both insulin resistance and cardiac hypertrophy.
Data (including data from studies in knockout mice) suggest that Rbp4 (plasma retinol-binding protein 4) is critical for antigen presentation and activation of CD4-positive T-lymphocyte in development of insulin resistance in mice obese due to high-fat diet.
A novel mechanism for circadian regulation of RBP4, but also a critical role of RBP4, acting as a hepatokine in the regulation of glucose metabolism by the circadian clock.
Elevated serum RBP4 raises BP.
These data show that decreasing circulating TTR levels or altering TTR-RBP4 binding could be a potential therapeutic approach for the treatment of type 2 diabetes.
findings suggest that RBP4 impaired in vivo adipogenesis, partly through the repression of the insulin pathway
The data implicate the involvement of chondrocytic Rbp4 in bone growth, particularly in the formation of the secondary ossification center of the limb.
Rbp4 and its membrane receptor STRA6 control adipogenesis by regulating cellular retinoid homeostasis and RARalpha activity.
STRA6 in tissues other than the eye appears to be the coupling of circulating holo-RBP levels to cell signaling, in turn regulating key processes such as insulin response.
expression of RBPR2 in liver and fat suggests a possible role in mediating established metabolic actions of RBP4 in those tissues
TTR blocks the ability of holo-retinol-binding protein to associate with STRA6 and thereby effectively suppresses both STRA6-mediated retinol uptake and STRA6-initiated cell signaling.
Suggest that RBP4 may be involved in the dyslipidemia associated with polycystic ovary syndrome in nonobese adolescents and that there may be an independent relationship between RBP4 and triglycerides but not between RBP4 and insulin resistance.
PPARgamma- and PPARalpha-mediated signaling controls RBP4 gene expression and releases in brown adipose tissue
these data support the model thatretinol binding protein 4 and retinoic acid precursors are present within the CSF and used for synthesis of retinoic acid, which promotes embryonic neuroepithelial survival
YSL-expressed Rbp4 plays a role in formation of both yolk extension and liver bud, the latter may also require migration of liver progenitor cells
STRA6 deficiency lead to accumulation of RBP-4 bound vitamin A and developmental abnormalities.
This protein belongs to the lipocalin family and is the specific carrier for retinol (vitamin A alcohol) in the blood. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin which prevents its loss by filtration through the kidney glomeruli. A deficiency of vitamin A blocks secretion of the binding protein posttranslationally and results in defective delivery and supply to the epidermal cells.
, plasma retinol-binding protein
, retinol-binding protein 4
, retinol-binding protein 4, interstitial
, retinol-binding protein 4, plasma
, Plasma retinol-binding protein
, retinol binding protein 4, cellular
, serum retinol binding protein