Analytical Data
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基因名
HSPBP1
- Application
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别名
HSPBP1;HSPBP;Hsp70-binding Protein 1
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9NZL4
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表达区间
1-362aa
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氨基酸序列
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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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
