Analytical Data
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Gene name
HSP70/HSPA1A
- Application
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Alternative Names
Allergen: Alt a 3
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Species
Alternaria alternata
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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
P78983
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Expression Region
1-152aa
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Molecular Weight
20.2 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, specifically the HSPA1A gene, encodes a heat shock protein that plays a crucial role in cellular stress responses and protein homeostasis. This molecular chaperone is known to assist in the proper folding of nascent polypeptides, prevent aggregation, and facilitate the degradation of misfolded proteins, thereby maintaining cellular integrity. Given its involvement in various biological processes, including cell proliferation, differentiation, and apoptosis, HSP70 has garnered significant attention in the fields of cancer research, neurodegenerative diseases, and immunology. Elevated levels of HSP70 are often observed in tumor cells, which use the protein to promote survival and resistance to therapy, making it a potential target for cancer treatment. Additionally, its role in modulating immune responses has led to investigations into its application in vaccine development and therapeutic strategies for autoimmune diseases. The recombinant production of HSP70/HSPA1A enables detailed functional studies and the exploration of its therapeutic potential. By providing a consistent and abundant source of the protein, researchers can further elucidate its mechanisms of action and assess its utility in clinical applications. The growing understanding of HSP70’s multifaceted roles in health and disease underscores the importance of ongoing research into this protein, as it offers promising avenues for novel treatment strategies and insights into fundamental biological processes.
