Analytical Data
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Gene name
HSP75
- Application
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Alternative Names
TRAP1; HSP90L; TNF Receptor-Associated Protein 1; Tumor necrosis factor type 1 receptor-associated protein
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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
Q12931
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Expression Region
Ser60~His704
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Molecular Weight
84kDa
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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
HSP75, also known as heat shock protein 75 or mitochondrial Hsp70, is a member of the Hsp70 family of chaperone proteins that plays a crucial role in protein folding, mitochondrial biogenesis, and the protection of cells against stress-induced damage. Research into HSP75 has garnered significant attention due to its vital role in maintaining cellular homeostasis and its involvement in various diseases, including neurodegenerative disorders, cancer, and metabolic syndromes. As a mitochondrial chaperone, HSP75 is essential for the proper import and folding of precursor proteins into the mitochondria, where it helps prevent the aggregation of misfolded proteins, thereby supporting cell survival under stress conditions. Moreover, the dysregulation of HSP75 has been linked to impaired mitochondrial function and increased susceptibility to apoptosis. Therefore, understanding the mechanisms of HSP75 function and its interactions with other mitochondrial proteins is critical for developing therapeutic strategies aimed at modulating its activity in disease contexts. The recombinant expression of HSP75 allows for detailed studies of its biochemical properties, folding mechanisms, and interaction networks, providing insights that could inform the design of small molecules or biologics to enhance its protective functions in various pathological conditions.
