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BEST1 encodes a member of the bestrophin gene family.
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Dog (Canine) Monoclonal Bestrophin 1 Primary Antibody for ICC, IHC (fro) - ABIN152509
Klimanskaya, Hipp, Rezai, West, Atala, Lanza: Derivation and comparative assessment of retinal pigment epithelium from human embryonic stem cells using transcriptomics. in Cloning and stem cells 2005
Show all 26 Pubmed References
Human Polyclonal Bestrophin 1 Primary Antibody for WB - ABIN521346
Kuo, Abdullaev, Hyzinski-García, Mongin: Effects of alternative splicing on the function of bestrophin-1 calcium-activated chloride channels. in The Biochemical journal 2014
Bestrophin 1 (dBest1) as the Drosophila Cl(swell) channel
bestrophin-1 chloride current is dually regulated by calcium and cell volume
These results revealed that the disease-causing mechanism of BEST1 mutations is centered on the indispensable role of BESTROPHIN1 in mediating the long speculated Ca(2 (show CA2 Antibodies)+)-dependent Cl(-) current in retinal pigment epithelium.
We describe a highly recognizable and reproducible retinal phenotype associated with a specific BEST1 mutation-p.Ala243Val in vitelliform macular dystrophy.
We have shown that the two novel combinations of compound heterozygous mutations p.R141H/p.M325T and p.R141H/p.I201T in the BEST1 gene can also lead to the autosomal recessive bestrophinopathy phenotype.
The findings in this family emphasize the previously noted variability of clinical manifestations in BEST1-associated autosomal dominant vitreoretinochoroidopathy (ADVIRC) and the relevance of FAF (show FANCF Antibodies) and NIA imaging. Cystoid macular edema and vascular leakage can be successfully treated using dorzolamide.
For patients with Best vitelliform macular dystrophy, single heterozygous BEST1 mutations were identified in 13 patients and compound heterozygous mutations were found in 3 patients. For patients with autosomal recessive bestrophinopathy, biallelic mutations were found in 13 probands and single mutant alleles in six patients. Overall, 36 disease-causing variants (20 novel mutations) of the BEST1 gene were identified.
Mutation in BEST1 has variable penetrance and expressivity, and can be uniocular.
We identified 7 BEST1 variants, 2 of which were new in 9 cases of Japanese patients with autosomal recessive bestrophinopathy.
Of the 225 genetic tests performed, 150 were for recessive IRD (show SCRIB Antibodies), and 75 were for dominant IRD (show SCRIB Antibodies). A positive molecular diagnosis was made in 70 (59%) of probands with recessive IRD (show SCRIB Antibodies) and 19 (26%) probands with dominant IRD (show SCRIB Antibodies). Thirty-two novel variants were identified; among these, 17 sequence changes in four genes were predicted to be possibly or probably damaging including: ABCA4 (show ABCA4 Antibodies) (14), BEST1 (2), PRPH2 (show PRPH2 Antibodies) (1), and TIMP3 (show TIMP3 Antibodies)
We describe the atypical phenotype and high intrafamilial variability associated with a new mutation in the BEST1 gene in an Italian family affected with Best vitelliform macular dystrophy.
A clinical picture similar to autosomal recessive bestrophinopathy can also be caused by a single heterozygous mutation in the BEST1 gene, such as the c.614T>C (p.I205T) variant in this family.
Data suggest that the ion channels CaV1.3 (show CACNA1D Antibodies), bestrophin-1 and maxiK (show KCNMA1 Antibodies) were identified as players in the regulation of photoreceptor outer segments (POS) phagocytosis by the retinal pigment epithelium (RPE (show RPE Antibodies)).
Best1-mediated astrocytic glutamate (show GRIN1 Antibodies) activates the synaptic N-methyl-D-aspartate receptor (show GRIN1 Antibodies) (NMDAR (show GRIN1 Antibodies)) and modulates NMDAR (show GRIN1 Antibodies)-dependent synaptic plasticity.
Bestrophin-1 functions as an intracellular Cl channel which helps to accumulate and to release Ca(2 (show CA2 Antibodies)+) from stores by conducting the counterion for Ca(2 (show CA2 Antibodies)+).
Best1, located at the microdomains near the synaptic junctions, has a significantly high permeability to glutamate (show GRIN1 Antibodies) in vivo.
Results show that different mutations in Best1 cause differential effects on its localization and that this effect varies with the presence or absence of wild-type (WT) Best1.
Astrocytic glutamate (show GRIN1 Antibodies) via Best1 channel targets and activates synaptic NMDA receptors.
Upon activation of protease activated receptor 1 (PAR1 (show F2R Antibodies)), an increase in intracellular Ca2 (show CA2 Antibodies)+ concentration leads to an opening of Best1 channels and subsequent release of glutamate (show GRIN1 Antibodies) in cultured astrocytes.
Ultrastructural analyses demonstrate that TREK-1 (show KCNK2 Antibodies) is preferentially localized at cell body and processes, whereas Best1 is mostly found in microdomains of astrocytes near synapses.
study reports that tonic inhibition in the cerebellum is due to GABA being released from glial cells by permeation through the Bestrophin 1 anion channel
SOX9 (show SOX9 Antibodies), through interaction with microphthalmia-associated transcription factor (MITF (show MITF Antibodies)) and OTX2 (show OTX2 Antibodies), regulates BEST1 expression in the retinal pigment epithelium.
Bestrophin-1 knock-down increases phagocytosis in primary porcine RPE (show RPE Antibodies) cells.
Retinal pigment epithelium bestrophin-1 possibly conducts Cl(-) as counter ion for Ca(2 (show CA2 Antibodies)+) uptake into cytosolic Ca(2 (show CA2 Antibodies)+) stores.
examined the quaternary structure of native best-1 and found that it migrates as a single species with a Stokes radius of 7.3 nm, sedimentation coefficient (S20 (show RPS20 Antibodies),w) of 4.9, and partial specific volume (nu) of 0.80 ml/g
This gene encodes a member of the bestrophin gene family. This small gene family is characterized by proteins with a highly conserved N-terminus with four to six transmembrane domains. Bestrophins may form chloride ion channels or may regulate voltage-gated L-type calcium-ion channels. Bestrophins are generally believed to form calcium-activated chloride-ion channels in epithelial cells but they have also been shown to be highly permeable to bicarbonate ion transport in retinal tissue. Mutations in this gene are responsible for juvenile-onset vitelliform macular dystrophy (VMD2), also known as Best macular dystrophy, in addition to adult-onset vitelliform macular dystrophy (AVMD) and other retinopathies. Alternative splicing results in multiple variants encoding distinct isoforms.
, bestrophin 1
, Bestrophin 1
, Best disease
, vitelliform macular dystrophy protein 2
, best macular dystrophy
, vitelliform macular dystrophy 2 homolog
, vitelliform macular dystrophy protein 2 homolog
, vitelliform macular dystrophy (Best disease, bestrophin)