Analytical Data
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Gene name
HSPBP1
- Application
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Alternative Names
FES1; Hsp70 Interacting Protein; Hsp70 Binding Protein,Cytoplasmic Cochaperone 1; Heat shock protein-binding protein 1; Hsp70-interacting protein 1
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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
Q6IMX7
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Expression Region
Ser198~Asp352
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Molecular Weight
21kDa
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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
HSPBP1 (Heat Shock Protein 70 Binding Protein 1) is a crucial co-chaperone in the heat shock protein (HSP) family, primarily known for its role in regulating the activity of HSP70. HSPs play a significant role in protein folding, repair, and cellular stress response, making them vital for maintaining cellular homeostasis. Research indicates that HSPBP1 facilitates the ATPase activity of HSP70, thereby enhancing its chaperone functions and influencing various cellular processes, including protein maturation, degradation, and translocation. Abnormalities in HSPBP1 expression have been linked to several pathophysiological conditions such as cancer, neurodegenerative diseases, and cardiovascular disorders, highlighting its potential as a therapeutic target. The recombinant protein advanced in studies allows for the exploration of HSPBP1's interactions with HSP70 and other client proteins under various stress conditions, aiming to unveil its mechanistic role in protein quality control and cellular resilience. Understanding the functional dynamics of HSPBP1 in cellular stress response may pave the way for novel strategies in treating diseases associated with protein misfolding and aggregation.
