Analytical Data
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Gene name
Alpha-crystallin B chain/CRYAB
- Application
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Alternative Names
CRY-AB; CRYA-B; CRYA2; CTPP2; HSPB5; Heat shock protein beta-5; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P23927
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Expression Region
Met1~Lys175
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Molecular Weight
24kDa
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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
Alpha-crystallin B chain (CRYAB) is a member of the small heat shock protein family, primarily expressed in the lens and various other tissues. It plays a crucial role in maintaining cellular homeostasis under stress conditions by acting as a molecular chaperone, preventing protein aggregation and facilitating proper protein folding. Recent studies have highlighted its importance not only in ocular health but also in neuroprotection, as CRYAB is implicated in various neurodegenerative diseases such as Alzheimer's and Parkinson's. The recombinant production of CRYAB has gained attention for its potential therapeutic applications, as it allows for a detailed investigation of its chaperone function and interaction with misfolded proteins. Through biophysical techniques and biochemical assays, researchers are exploring the structural properties of CRYAB and its mechanisms of action under pathological conditions. Moreover, understanding how CRYAB functions at a molecular level could pave the way for developing novel treatment strategies for diseases characterized by protein misfolding and aggregation. In summary, the research on recombinant CRYAB not only enriches our knowledge of cellular stress responses but also holds promise for therapeutic innovations in tackling related diseases.
