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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 - ABIN2131515
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
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 show that decreasing circulating TTR (show TTR Proteins) levels or altering TTR (show TTR Proteins)-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 (show INS Proteins) pathway
Childhood obesity may be associated with variations in RBP4 (show POLR2D Proteins) gene. The presence of selective SNPs in the RBP4 (show POLR2D Proteins) gene may account for metabolic complications.
Low levels of vitamin A, E and RBP4 (show POLR2D Proteins) at the time of renal cell carcinoma (show MOK Proteins) diagnosis are associated with a poorer prognosis after surgery.
RBP4 (show POLR2D Proteins) is some 6-fold lower when active TB patients have chronic energy deficiency (CED (show TGFB1 Proteins)) than when BMI is >25 kg/m sq; however, free fatty acids were not associated with CED (show TGFB1 Proteins) in active TB patients, which may be a type 2 error or represent an energy impasse where infection and the host's metabolic needs are in competition.
Data show that the tissue-specific expression pattern of human transgenic retinol binding protein 4 (hRBP4orf) was roughly the same as that of mouse Rbp4 (show POLR2D Proteins).
Elevated levels of RBP4 (show POLR2D Proteins) are associated with higher cardiovascular mortality among men with type 2 diabetes.
RBP4 (show POLR2D Proteins) and retinol levels were increased approximately twofold in patients with chronic kidney disease.
RBP4 (show POLR2D Proteins) level was associated with increased arterial stiffness in young subjects with family history of type 2 diabetes.
Retinol-binding protein 4 is able to function as biomarker to distinguish severe pre-eclampsia from normal pregnancy. More importantly, these results may shed light on the role of Retinol-binding protein 4 in the pathogenesis in pre-eclampsia.
The production of the two adipokines, chemerin and RBP-4, is strongly associated with obesity in patients with NAFLD.
High level of RBP4 (show POLR2D Proteins) is associated with obesity.
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.
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.
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