Analytical Data
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Gene name
HSP70/HSPA1B
- Application
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Alternative Names
Heat shock 70KDA protein 1 Short name: HSP70.1
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Species
Mouse
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17879
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Expression Region
2-642aa
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Molecular Weight
86 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
HSP70, particularly the HSPA1B isoform, is a highly conserved heat shock protein crucial for cellular stress response and protein homeostasis. It acts as a molecular chaperone, facilitating protein folding, preventing aggregation, and aiding in the refolding of misfolded proteins. In various pathological conditions, including neurodegenerative diseases, cancer, and cardiovascular disorders, HSP70 expression is often upregulated, indicating its role in cell survival and adaptation under stress. The study of recombinant HSP70/HSPA1B proteins has gained significant attention in recent years; researchers are focused on understanding its mechanisms in stress response and potential therapeutic applications. Recombinant technology allows for the production of large quantities of HSPA1B for in vitro and in vivo studies, enabling researchers to investigate its functions, structure, and interactions with other cellular proteins. Additionally, HSP70's immunogenic properties have prompted exploration into its use as a vaccine adjuvant and its role in cancer immunotherapy. By elucidating the diverse roles of HSP70/HSPA1B, researchers aim to uncover novel insights into its therapeutic potential, potentially leading to innovative treatment strategies for various diseases where protein misfolding and cellular stress are implicated.
