Analytical Data
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Gene name
HSPA14
- Application
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Alternative Names
HSP-A14; HSP70-4; HSP70L1; HSP70-like protein 1; Heat shock protein HSP60
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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
Q0VDF9
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Expression Region
Met1~Ser509
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Molecular Weight
56kDa
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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
HSPA14, also known as the heat shock protein 90-related protein, plays a crucial role in cellular stress responses and protein folding, making it an essential factor in maintaining cellular homeostasis. Research into HSPA14 has gained traction due to its potential implications in various diseases, including cancer, neurodegenerative disorders, and infections. As a member of the HSP70 family, HSPA14 is involved in the chaperoning of numerous client proteins, facilitating their proper folding and preventing aggregation under stress conditions. The recombinant production of HSPA14 has become a focal point for scientists aiming to elucidate its functional mechanisms and interactions at the molecular level. By generating HSPA14 in a controlled laboratory setting, researchers can study its biochemical properties, investigate its role in protein quality control, and assess its therapeutic potential. Moreover, understanding HSPA14's interactions with other cellular components may reveal novel pathways that could be targeted for drug development, offering hope for therapeutic strategies in the treatment of diseases associated with protein misfolding and aggregation. Given the importance of HSPA14 in cellular stress responses, continued exploration of its recombinant protein will enhance our understanding of its biological significance and potential clinical applications.
