Analytical Data
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Gene name
HSP100
- Application
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Alternative Names
Protein CLP
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Species
Trypanosoma cruzi
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15885
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Expression Region
1-138aa
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Molecular Weight
22.9 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
HSP100 proteins are a class of heat shock proteins that play a crucial role in protein quality control, specifically by assisting in the refolding or degradation of misfolded proteins. They are part of the cellular stress response, helping organisms survive under conditions such as heat shock, oxidative stress, and other adverse environmental factors. Research has highlighted their involvement in various cellular processes, such as protein disaggregation, which is vital for maintaining cellular homeostasis. HSP100 proteins have garnered attention in the fields of molecular biology and biomedical research due to their potential therapeutic implications. For instance, their chaperone activity has been studied in the context of neurodegenerative diseases, where the accumulation of misfolded proteins is a hallmark. Recent studies have also explored the recombinant expression of HSP100 proteins, aiming to harness their unique properties for applications in protein engineering, biotechnology, and as therapeutic agents. Understanding the mechanisms by which HSP100 proteins operate can offer insights into their roles in stress responses and their potential use in treating diseases associated with protein misfolding. Thus, ongoing research into HSP100 recombinant proteins holds promise for both fundamental biology and potential medical advancements.
