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The protein encoded by RLBP1 is a 36-kD water-soluble protein which carries 11-cis-retinaldehyde or 11-cis-retinal as physiologic ligands. Additionally we are shipping Retinaldehyde Binding Protein 1 Antibodies (36) and Retinaldehyde Binding Protein 1 Kits (5) and many more products for this protein.
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Cralbp b expression in Muller cells of the retina is essential for cone vision and provides evidence that both the canonical and the alternative visual cycle depend on the same type of retinoid-binding protein.
Different mutations in RLBP1 are correlated with quite different morphological and functional characteristics outlines the complexity of the protein.
RLBP1 gene is upregulated in patients with reactive retinal astrocytic tumors.
Patients with retinitis punctata albescens (RPA) show variable degrees of foveal cone death, even at an early stage. This finding has implications for future treatment.
The two RLBP1 genotypes presented a phenotypical and electrophysiological expression of progressive retinal disease similar to that previously described in homozygotes for the c.700C>T (p.R234W) RLBP1 mutation.
The clinical characteristics of a Japanese patient with a homozygous R234W mutation in RLBP1 are very similar to that of Swedish patients with Bothnia dystrophy.
Identification of autoantibodies specific for two retinal antigens (CRALBP and S-Ag (show SAG Proteins)) supports the concept of an autoimmunological origin of the disease.
The R234W mutation reveals impaired 11-cis (show CISH Proteins)-retinal release through stabilization of the ligand complex.
mutations in RLBP1 are responsible for fundus albipunctatus in the affected individuals of these consanguineous Pakistani families.
In the RLBP1-Bothnia dystrophy phenotype, a loss of function and thinning of the central macula are found, indicating early damage of the cone photoreceptors in this disease of the visual cycle.
Newfoundland rod-cone dystrophy, an early-onset retinal dystrophy (show MERTK Proteins), is caused by splice-junction mutations in RLBP1
results identify Muller cell CRALBP as a key component of the retinal visual cycle and demonstrate that this pathway is important for maintaining normal cone-driven vision and accelerating cone dark adaptation.
CRALBP is a direct downstream target of Pax6 (show PAX6 Proteins).
Potential role for Rlbp1 and Syntaxin 12 (show STX12 Proteins) in ethanol preference in mice, a conclusion supported by the location of these genes in quantitative trait loci (QTL).
Regulatory elements in a restricted region of the Rlbp1 gene are sufficient to drive GFP expression in vivo.
The protein encoded by this gene is a 36-kD water-soluble protein which carries 11-cis-retinaldehyde or 11-cis-retinal as physiologic ligands. It may be a functional component of the visual cycle. Mutations of this gene have been associated with severe rod-cone dystrophy, Bothnia dystrophy (nonsyndromic autosomal recessive retinitis pigmentosa) and retinitis punctata albescens.
retinaldehyde binding protein 1
, retinaldehyde-binding protein 1
, cellular retinaldehyde-binding protein
, cellular retinaldehyde-binding protein-1