Analytical Data
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Gene name
HSPE1
- Application
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Alternative Names
HSPE1；10 kDa heat shock Protein. mitochondrial
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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
P61604
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Expression Region
2-102aa
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AA Sequence
AGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD
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Molecular Weight
14.8 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
Related Products
Protein Description
HSPE1, also known as Heat Shock Protein 10 (HSP10), is a mitochondrial chaperonin that plays a crucial role in protein folding and mitochondrial function. It is primarily involved in assisting the proper assembly of proteins within the mitochondria, thus safeguarding cellular homeostasis under stress conditions. The study of HSPE1 has gained significant attention due to its implications in various diseases, including neurodegenerative disorders, diabetes, and cancers, where its dysfunction can lead to protein misfolding and mitochondrial dysfunction. Furthermore, HSPE1 has been revealed to interact with multiple proteins, contributing to critical cellular processes beyond its chaperone activity, suggesting its potential role in cellular signaling pathways. The recombinant forms of HSPE1 have been explored for their potential therapeutic applications, providing insights into how modulating its activity could lead to novel strategies in disease intervention. Investigating HSPE1 at the molecular level, including its expression profiles, post-translational modifications, and interaction networks, may uncover new biomarkers and therapeutic targets. Overall, the research into HSPE1 not only enhances our understanding of cellular stress responses and mitochondrial biology but also opens avenues for innovative therapeutic approaches in tackling diseases associated with mitochondrial dysfunction.
