Analytical Data
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Gene name
CRYBA4
- Application
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Alternative Names
CRYBA4;Beta-crystallin A4
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P53673
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Expression Region
1-196aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMTLQCTKSAGPWKMVVWDEDGFQGRRHEFT AECPSVLELGFETVRSLKVLSGAWVGFEHAGFQGQQYILERGEYPSWDAW GGNTAYPAERLTSFRPAACANHRDSRLTIFEQENFLGKKGELSDDYPSLQ AMGWEGNEVGSFHVHSGAWVCSQFPGYRGFQYVLECDHHSGDYKHFREWG SHAPTFQVQSIRRIQQ
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Molecular Weight
25 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
The CRYBA4 gene encodes a member of the crystallin family of proteins, which are predominantly found in the eye lens and play crucial roles in maintaining lens transparency and refractive index. Recent studies have suggested that CRYBA4 may also be involved in cellular stress response and protection against oxidative damage. Mutations or dysregulation of CRYBA4 have been associated with various ocular diseases, including congenital cataracts and other forms of lens opacification. As such, recombinant CRYBA4 protein is of particular interest for both basic biological research and potential therapeutic applications. By producing and characterizing this protein, researchers aim to elucidate its structure-function relationships, examine its molecular interactions, and understand its role in lens biology. Additionally, the study of CRYBA4 can provide insights into the mechanisms underlying lens clarity and the pathogenesis of cataracts. Consequently, recombinant CRYBA4 serves as a valuable tool for exploring new avenues in ocular research and developing targeted strategies for preventing or treating lens-related disorders.
