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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
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
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
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
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.
RBP4 (show POLR2D Proteins) is involved in all-trans retinoic acid-induced cleft palate.
the 1.5A resolution structures of human holo-RBP4 (show POLR2D Proteins) and of the protein saturated with palmitic and lauric acid and discuss the interaction of the fatty acids and retinol with the protein, are reported.
Circulating RBP4 (show POLR2D Proteins) levels may not be associated with nonalcoholic fatty liver disease.
Plasma PEDF (show SERPINF1 Proteins) and RBP4 (show POLR2D Proteins) identified insulin (show INS Proteins) resistance in subjects with no prior diagnosis of diabetes.
Serum RBP4 (show POLR2D Proteins) level was significantly higher and closely associated with blood pressure in prehypertensive Chinese.
Conclusion RBP4 (show POLR2D Proteins) may be used as a predictive factor of diabetic nephropathy patients complicated with silent cerebral infarction (SCI) and is positively correlated with cognitive dysfunction. RBP4 (show POLR2D Proteins)/Lp-PLA2 (show Lp-PLA2 Proteins)/Netrin-1 (show NTN1 Proteins) pathway activation may be one of the occurrence mechanisms in diabetic nephropathy complicated with SCI.
these data demonstrate a key role of STRA6 and RBP4 (show POLR2D Proteins) in the maintenance of colon cancer self-renewal and that this pathway is an important link through which consumption of HFD contributes to colon carcinogenesis.
Data suggest that, in subjects with chronic kidney disease, renal function is inversely related to serum RBP4 (show POLR2D Proteins) levels; as GFR (show RAPGEF5 Proteins) decreases, the relationship between RBP4 (show POLR2D Proteins) and insulin (show INS Proteins) resistance is attenuated. (GFR (show RAPGEF5 Proteins) = glomerular filtration rate, a measure of kidney function)
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