Analytical Data
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Gene name
HSPA4
- Application
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Alternative Names
HSP-A4; APG2; HS24/P52; RY; Hsp70; Hsp70RY; Heat shock 70-related protein APG-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 90% as determined by SDS-PAGE.
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Uniprot
P34932
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Expression Region
Ser258~Glu511
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Molecular Weight
32kDa
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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
HSPA4, also known as Heat Shock Protein 70 family member 4, is a crucial molecular chaperone involved in various cellular processes, including protein folding, assembly, and protection against stress-induced damage. Research on HSPA4 has gained significance due to its potential role in various diseases, particularly cancer, neurodegenerative disorders, and cardiovascular diseases. The overexpression of HSPA4 is often associated with tumor progression and drug resistance, making it a potential target for therapeutic interventions. Additionally, HSPA4 helps in the proper functioning of proteins under stressful conditions, which is vital for maintaining cellular homeostasis. The study of recombinant HSPA4 protein allows researchers to investigate its structure and function in controlled laboratory settings, providing insights into its biological mechanisms and potential applications in drug development. As a model for understanding the molecular pathways involving HSPA4, recombinant protein studies can facilitate the identification of new therapeutic targets, aiding in the development of strategies to manipulate its expression and activity for clinical benefits. Overall, the research on recombinant HSPA4 protein represents a promising avenue for advancing our understanding of stress response mechanisms in cells and their implications in human health and disease.
