Bestrophin/BEST1 Antibody [B12E13]

Application: Reactivity: Human, Monkey, Dog, Pig, Cow

Usage Information

Dilution
WB1:1000

Application
WB, IP, IHC, IF

Reactivity
Human, Monkey, Dog, Pig, Cow

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
68 kDa 67 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human RPE cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Bestrophin/BEST1 Antibody [B12E13] detects endogenous levels of total Bestrophin/BEST1 protein.

Clone
B12E13

Synonym(s)
VMD2; BEST1; Bestrophin-1; TU15B; Vitelliform macular dystrophy protein 2

Background
Bestrophin-1, also known as BEST1 or VMD2, is the founding member of the bestrophin family of calcium-activated chloride channels and forms homopentameric transmembrane pores that are predominantly expressed in the retinal pigment epithelium, where it regulates chloride efflux critical for retinal fluid homeostasis and photoreceptor function. Each monomer of about 68 kilodaltons features a dispersed topology with five transmembrane helices per subunit, forming a barrel approximately ninety-five angstroms long. The channel includes cytosolic calcium clasps, with five per pentamer, each binding two calcium ions through EF-hand-like motifs, a pore-lining neck composed of S2b helices flanked by flexible S2a and S2c loops that enable a tethered concertina-like widening mechanism, and a cytoplasmic aperture with a hydrophobic constriction that controls anion selectivity. The core function of BEST1 involves calcium binding to the clasps, which allosterically repositions the neck helices to dilate the hydrophobic gate and activate the channel, while high calcium levels recruit C-terminal inactivation peptides that constrict the gate and lower the channel's open probability. The wide pore allows both bicarbonate and chloride flux after the aperture. BEST1 is essential for driving retinal pigment epithelium fluid transport and absorption, supporting the visual cycle through ion balance, and buffering the subretinal space, with knockout models showing impaired phagocytosis and light responses. Mutations in BEST1 cause bestrophinopathies such as Best vitelliform macular dystrophy, characterized by lipofuscin accumulation and retinal pigment epithelium atrophy, adult-onset foveomacular vitelliform dystrophy, and nanophthalmos, often through misfolding or trafficking defects.

Background

Bestrophin-1, also known as BEST1 or VMD2, is the founding member of the bestrophin family of calcium-activated chloride channels and forms homopentameric transmembrane pores that are predominantly expressed in the retinal pigment epithelium, where it regulates chloride efflux critical for retinal fluid homeostasis and photoreceptor function. Each monomer of about 68 kilodaltons features a dispersed topology with five transmembrane helices per subunit, forming a barrel approximately ninety-five angstroms long. The channel includes cytosolic calcium clasps, with five per pentamer, each binding two calcium ions through EF-hand-like motifs, a pore-lining neck composed of S2b helices flanked by flexible S2a and S2c loops that enable a tethered concertina-like widening mechanism, and a cytoplasmic aperture with a hydrophobic constriction that controls anion selectivity. The core function of BEST1 involves calcium binding to the clasps, which allosterically repositions the neck helices to dilate the hydrophobic gate and activate the channel, while high calcium levels recruit C-terminal inactivation peptides that constrict the gate and lower the channel's open probability. The wide pore allows both bicarbonate and chloride flux after the aperture. BEST1 is essential for driving retinal pigment epithelium fluid transport and absorption, supporting the visual cycle through ion balance, and buffering the subretinal space, with knockout models showing impaired phagocytosis and light responses. Mutations in BEST1 cause bestrophinopathies such as Best vitelliform macular dystrophy, characterized by lipofuscin accumulation and retinal pigment epithelium atrophy, adult-onset foveomacular vitelliform dystrophy, and nanophthalmos, often through misfolding or trafficking defects.

References
https://pubmed.ncbi.nlm.nih.gov/34612806/ https://pubmed.ncbi.nlm.nih.gov/30628889/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%