Analytical Data
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Gene name
HSPb8
- Application
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Alternative Names
HSPb8；CRYAC；E2IG1；HSP22；Heat shock Protein beta-8
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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
Q9UJY1
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Expression Region
1-196aa
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AA Sequence
MADGQMPFSCHYPSRLRRDPFRDSPLSSRLLDDGFGMDPFPDDLTASWPD WALPRLSSAWPGTLRSGMVPRGPTATARFGVPAEGRTPPPFPGEPWKVCV NVHSFKPEELMVKTKDGYVEVSGKHEEKQQEGGIVSKNFTKKIQLPAEVD PVTVFASLSPEGLLIIEAPQVPPYSTFGESSFNNELPQDSQEVTCT
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Molecular Weight
50kDa
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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
HSPb8 (Heat Shock Protein beta-8) is a member of the small heat shock protein family, which plays a crucial role in the cellular stress response. This protein is highly conserved across various species and is primarily involved in protecting cells from stress-induced damage by preventing the aggregation of misfolded proteins and facilitating their refolding or degradation. Recent studies have highlighted its significant role in neurodegenerative diseases, particularly in the context of cellular protection mechanisms during oxidative stress and in the modulation of protein homeostasis. Research has shown that HSPb8 is involved in several cellular processes, including apoptosis, autophagy, and the response to heat shock and oxidative stress. The functionality of HSPb8 is closely linked to its ability to form homo- and hetero-oligomers, which are crucial for its protective actions. Furthermore, understanding HSPb8's molecular mechanisms and interactions can provide insight into potential therapeutic strategies for diseases characterized by protein misfolding and aggregation. Given its importance in cellular resilience, the recombinant expression of HSPb8 has become a focus of attention for studying its properties, interactions, and potential applications in medicine, particularly in enhancing cellular survival and mitigating the effects of stress in various disease contexts. As research advances, HSPb8 holds promise as a target for therapeutic intervention in diseases such as Alzheimer's, Parkinson's, and other conditions linked to protein misfolding.
