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Human RBP4 Protein expressed in Human Cells - ABIN2002658
Colantuoni, Romano, Bensi, Santoro, Costanzo, Raugei, Cortese: Cloning and sequencing of a full length cDNA coding for human retinol-binding protein. in Nucleic acids research 1984
Show all 8 Pubmed References
Human RBP4 Protein expressed in Human - ABIN934773
Sharif, Hu, Klock, Hampton, Nigoghossian, Knuth, Matzen, Anderson, Trager, Uno, Glynne, Azarian, Caldwell, Brinker: Time-resolved fluorescence resonance energy transfer and surface plasmon resonance-based assays for retinoid and transthyretin binding to retinol-binding protein 4. in Analytical biochemistry 2009
Mouse (Murine) RBP4 Protein expressed in Human Cells - ABIN2007447
Quadro, Blaner, Hamberger, Van Gelder, Vogel, Piantedosi, Gouras, Colantuoni, Gottesman: Muscle expression of human retinol-binding protein (RBP). Suppression of the visual defect of RBP knockout mice. in The Journal of biological chemistry 2002
Show all 6 Pubmed References
Rat (Rattus) RBP4 Protein expressed in HEK-293 Cells - ABIN1344327
Casillas-Ramírez, Alfany-Fernández, Massip-Salcedo, Juan, Planas, Serafín, Pallàs, Rimola, Rodés, Peralta: Retinol-binding protein 4 and peroxisome proliferator-activated receptor-? in steatotic liver transplantation. in The Journal of pharmacology and experimental therapeutics 2011
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 (show APOA1 Proteins) and RBP4 (show POLR2D Proteins) in human rhegmatogenous retinal detachment associated with choroidal detachment reflects the severity of disease.
The overexpression of RBP4 (show POLR2D Proteins) increased cell proliferation, whereas siRNA-mediated RBP4 (show POLR2D Proteins) knockdown significantly decreased HTR8/SVneo cell proliferation via activation of PI3K (show PIK3CA Proteins)/AKT (show AKT1 Proteins) signaling.
High RBP4 (show POLR2D Proteins) expression is associated with hypertriglyceridemia.
We observed that knockdown of RBP4 (show POLR2D Proteins) can greatly suppress ovarian cancer cell migration and proliferation.
This study showed that the Levels of circulating RBP4 (show POLR2D Proteins) was significantly higher in Chronic Kidney Disease than in control.
Our results demonstrate that IR is associated with high circulating RBP4 (show POLR2D Proteins) and that suppressed RBP4 (show POLR2D Proteins) adipose tissue expression is accompanied by reduced GLUT4 (show SLC2A4 Proteins) expression in HD. Renal transplantation or HDF (show Vcan Proteins) are effective in lowering serum RBP4 (show POLR2D Proteins) levels.
Data suggest that serum levels of RBP4 (show POLR2D Proteins) and LGAL3BP are up-regulated after menopause when complicated by NAFLD (non-alcoholic fatty liver disease); RBP4 (show POLR2D Proteins) and LGAL3BP may serve as biomarkers of NAFLD in postmenopausal women. (RBP4 (show POLR2D Proteins) = retinol binding protein 4; LGAL3BP = galectin-3 binding protein (show LGALS3BP Proteins))
Elevated levels of RBP4 (show POLR2D Proteins) were not associated with an increased risk of ischemic stroke among women.
Study showed that dietary weight loss-induced changes in angiotensin-converting enzyme (show ACE Proteins) activity, free fatty acids and RBP4 (show POLR2D Proteins) independently contribute to weight regain prediction.
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 (show INS Proteins) 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 (show ESR1 Proteins), retinol-binding protein or follistatin (show FST Proteins) loci.
study found significant association of two diallelic polymorphisms in the porcine genes for leukaemia inhibitory factor (LIF (show LIF Proteins)) 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 (show PRLR Proteins) 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 (show ALB Proteins) and serum retinol-binding protein(sRBP) are not components of bovine interphotoreceptor matrix(IPM). Serum albumin (show ALB Proteins) 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 (show TLR4 Proteins).
New insights into ghrelin (show GHRL Proteins) cell physiology, and given the known functions of RBP4 and TTR (show TTR Proteins), support an emerging role for the ghrelin (show GHRL Proteins) 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 (show INS Proteins) resistance and heart failure by activating TLR4 (show TLR4 Proteins)/MyD88 (show MYD88 Proteins)-mediated inflammatory pathways. Potentially, lowering RBP4 might break the vicious cycle and improve both insulin (show INS Proteins) 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 (show CD4 Proteins)-positive T-lymphocyte in development of insulin (show INS Proteins) 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 support the model thatretinol binding protein 4 and retinoic acid precursors are present within the CSF (show CSF2 Proteins) 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