Analytical Data
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Gene name
Hsp104
- Application
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Alternative Names
Clpb;Skd3;Mitochondrial disaggregase
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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
P31539
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Expression Region
Partial
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AA Sequence
Tag type will be determined during the manufacturing process.
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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
Hsp104 is a powerful chaperone protein found primarily in yeast and other organisms, known for its role in protein disaggregation and refolding under stress conditions. Discovered in the context of heat shock response, Hsp104 acts as a critical element in the cellular response to proteotoxic stress, helping to maintain protein homeostasis and prevent the aggregation of misfolded proteins. Its unique structure and ATPase activity enable Hsp104 to extract polypeptides from aggregated forms, thereby facilitating the recovery of functional proteins. Given its importance in cellular stress management, researchers have been keen to explore Hsp104's potential applications in biotechnology and medicine, particularly in relation to diseases associated with protein misfolding and aggregation, such as Alzheimer's and Huntington's diseases. The ability to harness Hsp104 for therapeutic purposes hinges not only on understanding its molecular mechanisms but also on optimizing its use in various systems, including engineered strains for improved performance in protein production. The recombinant production of Hsp104 has become a focal point in this research, as it allows for the detailed study of its functional properties and interactions. Overall, the study of recombinant Hsp104 has profound implications for advancing our knowledge of protein dynamics in cells and developing novel strategies to combat protein misfolding diseases.
