Analytical Data
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Gene name
HSP10/EPF
- Application
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Alternative Names
HSPE1; CPN10; EPF; GROES; Chaperonin 10; Early Pregnancy Factor; 10 kDa heat shock protein, mitochondrial
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P61604
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Expression Region
Ala2~Asp102
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Molecular Weight
17kDa
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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
HSP10 (Heat Shock Protein 10) and EPF (Extracellular Protein Factor) are two important proteins that have garnered significant research interest due to their roles in cellular stress responses and protein folding. HSP10 is a mitochondrial chaperonin that assists in the proper folding of newly synthesized polypeptides, while EPF is known to provide protective functions in various cellular processes, including immunity and adaptation to environmental stressors. The study of HSP10/EPF recombinant proteins has gained momentum, particularly in the context of understanding their molecular mechanisms and potential therapeutic applications. Recent advancements in recombinant DNA technology have enabled researchers to produce these proteins in higher quantities and with increased purity, facilitating in vitro and in vivo studies. Investigating the interactions between HSP10 and EPF may reveal new insights into their complementary roles in protein maturation and stress response pathways. Additionally, the development of recombinant forms of these proteins could lead to novel therapeutic strategies for diseases associated with protein misfolding and aggregation, such as neurodegenerative disorders. Overall, the exploration of HSP10/EPF recombinant proteins holds promise not only for fundamental biological research but also for the advancement of clinical applications aimed at enhancing cellular resilience and function.
