Analytical Data
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Gene name
HSPA8/HSC70
- Application
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Alternative Names
LAP1; HSC54; HSC70; HSC71; HSP71; HSPA10; NIP71; HSP73; Heat shock cognate 71 kDa protein; Lipopolysaccharide-associated protein 1; LPS-associated protein 1
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Species
Bovine
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P19120
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Expression Region
Asp534~Gly615
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Molecular Weight
11kDa
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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
HSPA8, also known as HSC70, is a heat shock protein that plays a crucial role in cellular stress responses, protein folding, and the transport of proteins across cellular membranes. It is a member of the HSP70 family, which is highly conserved across species and is essential for maintaining cellular homeostasis. Research has highlighted HSPA8's involvement in various cellular processes, including autophagy, apoptosis, and the management of misfolded proteins, making it a vital component in numerous physiological and pathological conditions. Abnormal expression of HSPA8 has been implicated in various diseases, including neurodegenerative disorders, cancer, and heart diseases, indicating its potential as a therapeutic target. The study of recombinant HSPA8 enables researchers to elucidate the protein's structure-function relationships, interaction with other cellular components, and its mechanistic pathways in disease contexts. Recombinant proteins provide a means to investigate the molecular mechanisms underlying HSPA8's functions and offer a platform for drug development aimed at modulating its activity. Moreover, understanding HSPA8's role in cell signaling and stress response can lead to novel strategies for enhancing cellular resilience against various stressors. Overall, the investigation of HSPA8/HSC70 as a recombinant protein is critical for advancing our knowledge of cellular biology and developing potential therapeutic interventions for diseases linked to protein homeostasis and cellular stress.
