Analytical Data
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Gene name
CRYBB1
- Application
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Alternative Names
CRYBB1;Beta-crystallin B1
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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
P53674
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Expression Region
2-252aa
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AA Sequence
SQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE GSFPVLATEP PK
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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
CRYBB1, or crystallin beta B1, is a member of the beta-crystallin family, primarily found in the lens of the eye and plays a crucial role in maintaining lens transparency and refractive properties. Mutations in the CRYBB1 gene have been linked to various types of cataracts, underscoring its significance in ocular health. The expression and characterization of CRYBB1 recombinant protein are vital for understanding its structural and functional properties, especially in the context of cataractogenesis. By producing CRYBB1 as a recombinant protein, researchers can investigate its biochemical pathways, interactions with other cellular components, and its role in lens cell physiology. Moreover, generating and analyzing this protein allows for the exploration of the molecular mechanisms behind the stability and aggregation of crystallins, which is crucial for developing potential therapeutic strategies against cataract formation. Given the increasing prevalence of age-related cataracts worldwide, understanding the role of CRYBB1 and its interactions at the molecular level may pave the way for innovative treatments, highlighting the importance of CRYBB1 recombinant protein research in ocular health and disease prevention.
