Analytical Data
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Gene name
HSP100
- Application
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Alternative Names
HSP100；ATP-dependent Clp protease ATP-binding subunit clpX-like. mitochondrial
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Species
Trypanosoma
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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
O15885
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Expression Region
1-138aa
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AA Sequence
NSPKGLEATREKVWQVVRSYFRPEFLNRLDDIVLFRRLGFGELHEIIDLIVAEVNGRLRSQDILLEVTDEAKNFVLENAFDAEMGARPLRRWVEKYITTEVSRMILAQQLPPNSTVRVLVNGSQGKLAFSVKRSFVSE
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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
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Protein Description
HSP100 (Heat Shock Protein 100) is a family of molecular chaperones that play a crucial role in protein homeostasis and cellular stress response. These proteins are primarily involved in the refolding or degradation of misfolded proteins, especially under stress conditions such as heat shock, oxidative stress, or during various pathological states. Research into HSP100 has gained significant attention due to its potential implications in disease mechanisms, particularly in neurodegenerative disorders, cancer, and protein misfolding diseases. The ability of HSP100 proteins to resolve protein aggregates positions them as critical players in maintaining cellular function and viability. Moreover, the structural and functional characteristics of HSP100 make it a promising target for therapeutic intervention. Techniques such as recombinant protein technology have advanced our understanding of HSP100's role, enabling scientists to produce and characterize these proteins in vitro. This research could pave the way for innovative treatments that harness the protective functions of HSP100, highlighting its significance in both basic biology and clinical applications. As the field progresses, further studies on the mechanisms by which HSP100 operates will enhance our understanding of its contributions to cellular health and disease management.
