Analytical Data
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Gene name
HSPBP1
- Application
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Alternative Names
HSPBP1;HSPBP;Hsp70-binding Protein 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
1-362aa
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AA Sequence
MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG LLQMAITAGS EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL RVLSQPMPPT AGEAEQAADQ QEREGALELL ADLCENMDNA ADFCQLSGMH LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA AIQEQVLGLG ALRKLLRLLD RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR AMQQQVQKLK VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT CFSSPADDSM DR
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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 co-chaperone that interacts with heat shock proteins, particularly HSP70, playing a crucial role in protein folding, translocation, and degradation processes within the cell. The significance of HSPBP1 has been underscored by its involvement in various cellular stress responses and its potential links to several diseases, including neurodegeneration and cancer. Recent studies have highlighted its regulatory functions in influencing the activity of HSP70, modulating protein homeostasis, and preventing aggregation of misfolded proteins. Researchers have been investigating HSPBP1 as a potential therapeutic target due to its central role in chaperone-mediated cellular mechanisms. Recombinant HSPBP1 protein has been expressed and purified to study its structure-function relationship, understand its interaction with HSP70, and explore its effects on client protein folding. This work is vital for deciphering the molecular pathways underlying cellular stress responses and may lead to novel strategies for treating diseases associated with protein misfolding and aggregation. By elucidating the mechanisms of HSPBP1 action, scientists aim to unlock new avenues for intervention in pathological states, emphasizing the protein's relevance to both fundamental biology and potential clinical applications.
