Analytical Data
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Gene name
CRYAA
- Application
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Alternative Names
CRYAA；CRYA1；HSPB4;Alpha-crystallin A chain
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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
P02489
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Expression Region
1-173aa
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AA Sequence
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS
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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
CRYAA, or Alpha-crystallin A, is a small heat shock protein primarily found in the lens of the eye, playing a crucial role in maintaining lens transparency and protecting against cellular stress. Research has indicated that CRYAA possesses chaperone-like activities, which help prevent protein aggregation, a common feature in various age-related diseases, including cataracts and neurodegenerative disorders. The significance of studying recombinant CRYAA stems from its potential therapeutic applications in ocular health and broader implications for protein misfolding diseases. Advanced methods for recombinant protein expression and purification have enabled scientists to produce functional CRYAA in significant quantities, facilitating detailed structural and functional studies. These investigations aim to uncover the molecular mechanisms underlying its protective roles in the eye and other tissues. Additionally, recombinant CRYAA could be explored for use in drug delivery systems or as a therapeutic agent to mitigate cellular stress responses. As scientists continue to dissect the multifaceted nature of CRYAA, the hope is that their findings will pave the way for innovative strategies to combat age-related diseases and enhance our understanding of protein dynamics in cellular contexts.
