Analytical Data
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Gene name
HSP10
- Application
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Alternative Names
HSPE1;10 kDa heat shock Protein. mitochondrial
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Species
Saccharomyces cerevisiae
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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
P38910
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Expression Region
2-106aa
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AA Sequence
STLLKSAKS IVPLMDRVLV QRIKAQAKTA SGLYLPEKNV EKLNQAEVVA VGPGFTDANG NKVVPQVKVG DQVLIPQFGG STIKLGNDDE VILFRDAEIL AKIAKD
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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, or Heat Shock Protein 10, is a crucial molecular chaperone that plays a significant role in protein folding and cellular stress response. It is part of the chaperonin family, which assists in the proper folding of newly synthesized proteins and the refolding of denatured proteins, thus maintaining cellular homeostasis. The study of HSP10 has gained considerable attention due to its implications in various biological processes and diseases, including neurodegenerative disorders, cancer, and inflammation. Research has shown that dysregulation of chaperone functions, including that of HSP10, can lead to the accumulation of misfolded proteins, contributing to cellular dysfunction and pathology. Furthermore, HSP10 has been identified as a potential biomarker and therapeutic target, prompting investigations into its recombinant form for both basic and applied research. Producing and characterizing recombinant HSP10 allows scientists to explore its functional properties, interaction with other proteins, and potential as a therapeutic agent. Additionally, recombinant HSP10 can be employed in protein aggregation studies and may provide insights into the mechanisms underlying various diseases. Given its pivotal role in maintaining protein quality control, ongoing research on HSP10 is crucial for advancing our understanding of cell biology and developing novel therapeutic strategies.
