Analytical Data
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Gene name
HSPE1
- Application
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Alternative Names
10KDA chaperonin;Chaperonin 10 ;CPN10Early-pregnancy factor ;EPF
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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
2-102aa
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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
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Protein Description
The HSPE1, or Heat Shock Protein 10 (HSP10), is a vital component of the mitochondrial chaperonin complex, which plays a crucial role in protein folding, assembly, and import into mitochondria. HSP10 assists the chaperonin HSP60 in stabilizing unfolded or misfolded proteins, ensuring their proper conformation and functionality. The significance of HSPE1 in cellular stress response mechanisms has garnered considerable attention, as its expression is often upregulated under conditions of heat shock, oxidative stress, and various pathological states. Research has indicated that dysfunction of HSPE1 is implicated in several diseases, including neurodegenerative disorders and cancer, highlighting the need for a deeper understanding of its structure and function. Furthermore, the use of recombinant HSPE1 in therapeutic applications, such as in the development of vaccines and targeted therapies, presents a promising avenue for biomedical research. Despite its importance, comprehensive studies on HSPE1 remain limited, particularly regarding its interactions with other molecular partners and its role in cellular signaling pathways. Consequently, ongoing investigations are focused on elucidating the mechanistic aspects of HSPE1, including its potential as a biomarker for disease and a target for novel therapeutic strategies. The exploration of HSPE1's properties through recombinant protein technology not only advances our knowledge of mitochondrial chaperones but also opens new possibilities for innovation in treating diseases linked to protein misfolding and stress responses.
