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
Rat
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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
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Expression Region
Gln260~Glu469
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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 BiP (Binding Immunoglobulin Protein), is a member of the heat shock protein 70 (HSP70) family and plays a crucial role in maintaining protein homeostasis within the endoplasmic reticulum (ER). It is involved in folding nascent polypeptides, preventing protein aggregation, and facilitating the degradation of misfolded proteins through ER-associated degradation (ERAD). Research into HSPA5 has increased due to its implications in various diseases, including neurodegenerative disorders, diabetes, and certain cancers, where ER stress and the unfolded protein response (UPR) are often activated. Elevated levels of HSPA5 have been associated with the progression of tumors, making it a potential biomarker and therapeutic target. The recombinant production of HSPA5 protein is critical for functional studies and for understanding its molecular mechanisms and interactions with other cellular proteins. This research not only aids in elucidating the role of HSPA5 in normal physiology but also highlights its potential as a target for therapeutic intervention in diseases characterized by ER stress. Given the increasing recognition of the UPR's significance in health and disease, the development of recombinant HSPA5 provides a vital tool for further exploration of its functions and could lead to novel strategies for modulating ER stress responses in various pathological contexts.
