Analytical Data
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Gene name
HSPB8
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简介
The HSPB8 protein exhibits temperature-dependent chaperone activity and functions as a monomer in its molecular form.It interacts with other cellular proteins to form complexes critical for cellular homeostasis.HSPB8 Protein, Human (His) is the recombinant human-derived HSPB8 protein, expressed by E.coli , with C-6*His labeled tag.
- Application
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Alternative Names
Heat shock protein beta-8; HspB8; Alpha-crystallin C chain; E2-induced gene 1 protein; Protein kinase H11; Small stress protein-like protein HSP22; HSPB8; CRYAC; E2IG1; HSP22
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Species
Human
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Source
E. coli
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Tag
C-6*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9UJY1
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Expression Region
M1-T196
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AA Sequence
MADGQMPFSCHYPSRLRRDPFRDSPLSSRLLDDGFGMDPFPDDLTASWPDWALPRLSSAWPGTLRSGMVPRGPTATARFGVPAEGRTPPPFPGEPWKVCVNVHSFKPEELMVKTKDGYVEVSGKHEEKQQEGGIVSKNFTKKIQLPAEVDPVTVFASLSPEGLLIIEAPQVPPYSTFGESSFNNELPQDSQEVTCT
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Protein Length
Full Length
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Molecular Weight
23.0 kDa
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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, a member of the small heat shock protein (sHSP) family, plays a critical role in cellular protection against stress-induced damage and protein misfolding, often associated with neurodegenerative diseases and various forms of cellular stress. Initially identified for its involvement in the cellular response to heat shock, HSPB8 has garnered attention for its functions in the regulation of proteostasis, aggregation of misfolded proteins, and facilitation of autophagy. Its chaperone-like activity, along with its capacity to interact with other proteins involved in cellular stress response pathways, positions HSPB8 as a potential therapeutic target for conditions such as Alzheimer's disease, amyotrophic lateral sclerosis, and other pathologies linked to protein misfolding. Recent studies have focused on the recombinant expression and purification of HSPB8 to clarify its molecular mechanisms and functional role in vivo and in vitro. By generating large quantities of pure HSPB8 protein, researchers aim to investigate its structural characteristics, interactions with client proteins, and its efficacy in modulating stress responses in cells. The findings from these studies contribute to a deeper understanding of the protein's role in neuroprotection and present opportunities for the development of novel therapeutic strategies that leverage HSPB8's protective properties against cellular stress and neurodegeneration. Overall, the exploration of HSPB8 recombinant protein serves as a pivotal step in unraveling its biological significance and its potential application in combating diseases characterized by protein aggregation and cellular stress.
