Analytical Data
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Gene name
EPG
- Application
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Alternative Names
EPG；Epigen
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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
Q6UW88-2
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Expression Region
24-95aa
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AA Sequence
AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA
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Molecular Weight
8 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
EPG (Eukaryotic Protein General) chaperones are integral in maintaining protein homeostasis within eukaryotic cells, playing a critical role in protein folding, transport, and degradation. Their study has gained prominence due to their involvement in numerous cellular processes, particularly in response to environmental stressors, which can lead to misfolded proteins and aggregation. EPGs aid in the proper assembly of multi-protein complexes, ensuring cellular functionality and response to stress. Dysregulation of these chaperones is linked to various diseases, including neurodegenerative disorders and cancers, highlighting their potential as therapeutic targets. Recent advancements in structural biology and biochemistry have enabled researchers to elucidate the mechanisms by which EPGs interact with substrates and co-chaperones, providing insights into their roles in cellular stress responses. Understanding the intricate dynamics of EPGs is crucial for developing strategies to enhance protein quality control in cells, which could have significant implications for treating diseases linked to protein misfolding and aggregation. This growing body of research aims to uncover the fundamental principles governing EPG function and their impact on cellular health, opening avenues for innovative therapeutic interventions.
