Analytical Data
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Gene name
CRYAB
- Application
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Alternative Names
CRYAB；CRYA2；HSPB5;Alpha-crystallin B 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
P02511
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Expression Region
1-175aa
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AA Sequence
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK
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Molecular Weight
36.2kDa
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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
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Protein Description
CRYAB (αB-crystallin) is a member of the small heat shock protein family and plays a crucial role in cellular stress responses, particularly in protecting cells from various stresses such as oxidative damage, heat shock, and apoptosis. Due to its chaperone-like activity, CRYAB is essential for maintaining protein homeostasis and preventing the aggregation of denatured proteins. Its expression is upregulated in response to stressors, making it a vital player in cell survival mechanisms. Research has shown that CRYAB is involved in several pathological conditions, including cardiovascular diseases, neurodegenerative disorders, and cancer, where its dysregulation contributes to disease progression. The functional significance of CRYAB has prompted extensive studies into its structural properties and potential therapeutic applications. Recombinant CRYAB proteins are often utilized in experimental settings to explore its chaperone activity, interaction with client proteins, and effects on cellular functions. Understanding the structural and functional characteristics of CRYAB through recombinant technology can lead to novel strategies for enhancing its protective roles in stress-related diseases and contributing to the development of therapeutic interventions targeting CRYAB-associated pathways. Overall, the investigation of CRYAB as a recombinant protein not only enriches our understanding of cellular stress mechanisms but also opens up new avenues for clinical applications in improving stress resilience in cells.
