Analytical Data
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Gene name
HSPA5
- Application
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Alternative Names
MIF2; BIP; GRP78; Immunoglobulin heavy chain-binding protein; Glucose Regulated Protein 78; Binding Immunoglobulin Protein; Endoplasmic reticulum lumenal Ca binding grp78
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Species
Mouse
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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
P20029
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Expression Region
Gln261~Glu470
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Molecular Weight
25kDa
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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
HSPA5, also known as binding immunoglobulin protein (BiP), is a member of the heat shock protein 70 (HSP70) family and plays a crucial role in the endoplasmic reticulum (ER) stress response and protein folding processes. It functions as a chaperone, ensuring proper protein folding and preventing the aggregation of misfolded proteins. Dysregulation of HSPA5 has been linked to various diseases, including cancer, neurodegenerative disorders, and metabolic syndrome, making it a significant target for therapeutic intervention. Research into recombinant HSPA5 proteins has gained momentum as scientists seek to elucidate its role in cellular homeostasis and stress responses. Producing HSPA5 as a recombinant protein allows for detailed studies of its biochemical properties, interaction with client proteins, and functional mechanisms in stress pathways. Additionally, recombinant HSPA5 can serve as a potential biomarker for disease progression and a target for drug development, particularly in conditions characterized by ER stress. The ability to study HSPA5 in a controlled laboratory setting enhances our understanding of its physiological functions and the implications of its dysregulation in various pathologies.
