Analytical Data
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Gene name
BEST4
- Application
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Alternative Names
VMD2L2; Vitelliform Macular Dystrophy 2-Like 2
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8NFU0
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Expression Region
Ile242~Met384
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Molecular Weight
20kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
BEST4 is a member of the bestrophin family of proteins, which are primarily expressed in the retina and play a crucial role in chloride channel activities. Initial studies have linked BEST4 to various cellular processes, including ion transport and regulation of cellular excitability. Research has shown that mutations in the BEST4 gene can lead to significant physiological consequences, contributing to conditions such as retinal dystrophies and other disorders like congenital chloride diarrhea. Recent investigations have focused on the biophysical properties and functional mechanisms of BEST4, aiming to elucidate its role in cellular homeostasis and retinal health. The protein is thought to be involved in the maintenance of retinal pigment epithelium (RPE) function, which is vital for photoreceptor cells. Given its significant roles in both normal physiological functions and disease states, studying BEST4’s structure and interactions at the molecular level is crucial for developing targeted therapeutic strategies aimed at addressing related pathologies. This research not only enhances our understanding of BEST4’s biological significance but also emphasizes the potential of bestrophins as therapeutic targets in genetic disorders and retinal diseases.
