Analytical Data
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Gene name
HSPA2
- Application
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Alternative Names
HSP-A2; Heat shock-related 70 kDa protein 2
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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 95% as determined by SDS-PAGE.
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Uniprot
P54652
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Expression Region
Lys529~Gln615
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Molecular Weight
14kDa
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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
HSPA2, a member of the heat shock protein 70 (HSP70) family, plays a crucial role in various cellular processes, including protein folding, protection against stress, and regulation of apoptosis. Specifically, HSPA2 is predominantly expressed in testicular germ cells and is essential for male fertility, as it participates in the maturation of sperm and the regulation of spermatogenesis. Recent studies have indicated that HSPA2 may also have implications in cancer biology, particularly in tumor progression and resistance to therapy, due to its role in modulating cellular stress responses. The investigation of HSPA2 recombinant proteins offers insights into its functional mechanisms and potential therapeutic applications. By expressing HSPA2 in a recombinant system, researchers can study its interactions with client proteins, identify its post-translational modifications, and evaluate its chaperone activity in vitro. Furthermore, the recombinant HSPA2 can be utilized in the development of diagnostic tools and targeted therapies for conditions associated with its dysregulation. Thus, the study of HSPA2 recombinant proteins not only enhances our understanding of its biological significance but also paves the way for innovative strategies in both reproductive health and oncology. Ultimately, the research on HSPA2 and its recombinant forms holds promise for advancing our knowledge of cellular stress responses and developing novel therapeutic interventions.
