Analytical Data
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Gene name
HSPBP1
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简介
HSPBP1 protein regulates HSPA1A chaperone activity by inducing conformational changes in the ATP-binding domain and disrupting ATP binding. This interference inhibits the STUB1-mediated ubiquitination process and blocks chaperone-assisted degradation of immature CFTR. HSPBP1 Protein, Human (E88G, His) is the recombinant human-derived HSPBP1 protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
HSPBP1; Hsp70-binding protein 1; HspBP1; Heat shock protein-binding protein 1; Hsp70-binding protein 2; HspBP2; Hsp70-interacting protein 1; Hsp70-interacting protein 2
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Species
Human
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NZL4
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Expression Region
R84-R359, E88G
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Protein Length
Partial
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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
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Protein Description
HSPBP1 (Heat Shock Protein 70-Binding Protein 1) is an important protein that plays a critical role in cellular stress responses, particularly in the context of heat shock and protein folding. It serves as a co-chaperone for HSP70, a well-known heat shock protein, enhancing its ability to refold denatured proteins and facilitating their degradation. Research into HSPBP1 has gained attention due to its involvement in various cellular processes, including protein quality control, apoptosis, and cellular signaling pathways. Dysregulation of HSPBP1 has been linked to several pathological conditions, including cancer and neurodegenerative diseases, making it a potential biomarker and therapeutic target. The recombinant expression of HSPBP1 allows for detailed studies of its functional mechanisms, interactions with other proteins, and its role in modulating the activity of HSP70 in different stress conditions. Furthermore, understanding how HSPBP1 contributes to the cellular heat shock response can offer insights into developing strategies for enhancing cell survival under stress and for creating novel treatments for diseases related to protein misfolding. As such, the study of recombinant HSPBP1 not only sheds light on basic biological processes but also holds promise for translational applications in medicine.
