Analytical Data
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Gene name
CRYBA2
- Application
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Alternative Names
CRYBA2Beta-crystallin A2; Beta-A2 crystallin
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P53672
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Expression Region
1-197aa
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AA Sequence
MSSAPAPGPAPASLTLWDEEDFQGRRCRLLSDCANVCERGGLPRVRSVKVENGVWVAFEYPDFQGQQFILEKGDYPRWSAWSGSSSHNSNQLLSFRPVLCANHNDSRVTLFEGDNFQGCKFDLVDDYPSLPSMGWASKDVGSLKVSSGAWVAYQYPGYRGYQYVLERDRHSGEFCTYGELGTQAHTGQLQSIRRVQH
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Molecular Weight
47.3 kDa
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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
CRYBA2 (Cryable Circadian Regulator 2) is a member of the beta-crystallin family, primarily expressed in the eye, specifically in the lens and retina. Its role extends beyond merely being a structural protein, as it has been implicated in various cellular processes, including maintaining lens transparency and regulating apoptosis in retinal cells. Research has shown that CRYBA2 may play a critical role in the pathophysiology of certain eye diseases, such as cataracts and age-related macular degeneration. The reconstitution of CRYBA2 protein is essential for elucidating its functional mechanisms and interactions with other proteins involved in ocular health. Recombinant CRYBA2 protein can be produced using various expression systems, allowing scientists to study its biochemical properties, structural characteristics, and cellular functions in detail. Understanding the role of CRYBA2 at the molecular level can provide insights into potential therapeutic targets for preventing or treating eye disorders. Furthermore, the study of CRYBA2 contributes to the broader field of crystallin biology, shedding light on the evolutionary adaptations and functional diversification of crystallin proteins in vertebrates. This underscores the significance of CRYBA2 not only in ocular physiology but also in understanding the intricate network of protein interactions that maintain cellular homeostasis in the eye. Therefore, the research around the recombinant CRYBA2 protein holds promise for advancing knowledge in ocular biology and addressing age-related vision impairments.
