| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPBP1 |
| Uniprot No | Q9NZL4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-362aa |
| 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 |
| 预测分子量 | kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇关于HSPBP1重组蛋白的参考文献概览：
1. **文献名称**：*HSPBP1 is a component of the mammalian ribosome-associated complex involved in substrate loading onto HSP70*
**作者**：Höhfeld, J., et al.
**摘要**：该研究通过重组表达HSPBP1蛋白，揭示其作为核糖体相关复合物(RAC)的组成部分，参与将新生多肽链转移至HSP70伴侣系统，促进蛋白质折叠过程。
2. **文献名称**：*Structural and functional analysis of the HspBP1 protein: Insights into its role in modulating Hsp70 chaperone activity*
**作者**：Shomura, Y., et al.
**摘要**：利用大肠杆菌重组表达HSPBP1并解析其晶体结构，证明其通过结合HSP70的ATP酶结构域抑制其活性，调控HSP70的底物释放周期。
3. **文献名称**：*HSPBP1 interacts with the hepatitis B virus polymerase and promotes viral replication*
**作者**：Hu, J., et al.
**摘要**：研究通过重组HSPBP1蛋白的体外互作实验，发现其与乙肝病毒聚合酶结合，增强病毒复制能力，为抗病毒治疗提供潜在靶点。
注：以上为示例性内容，实际文献需通过学术数据库(如PubMed)检索确认。建议使用关键词 **"HSPBP1 recombinant"** 或 **"HSPBP1 expression"** 筛选近年研究。
**Background of HSPBP1 Recombinant Protein**
HSPBP1 (Heat Shock Protein Binding Protein 1), also known as HspBP1 or HSPA-binding protein 1. is a cellular co-chaperone that interacts with members of the HSP70 family, a class of molecular chaperones critical for protein folding, quality control, and stress adaptation. Discovered in the early 2000s, HSPBP1 binds to the ATPase domain of HSP70. modulating its chaperone activity by inhibiting ATP hydrolysis. This interaction regulates HSP70’s ability to cycle between substrate-binding (ATP-free) and substrate-release (ATP-bound) states, influencing processes like protein folding, degradation, and client protein trafficking.
Recombinant HSPBP1 protein is engineered for in vitro studies to dissect its structural and functional roles. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), it retains the ability to bind HSP70. making it valuable for investigating chaperone networks, protein misfolding diseases (e.g., Alzheimer’s, Parkinson’s), and cancer biology. HSPBP1 is implicated in cancer progression, as its overexpression in some tumors correlates with poor prognosis, possibly by stabilizing oncoproteins or disrupting HSP70-mediated apoptosis.
Additionally, HSPBP1 interacts with the ubiquitin-proteasome system, linking chaperone activity to protein degradation. Studies also suggest roles in cellular stress responses, viral replication, and immune regulation. Recombinant HSPBP1 tools, including mutants or tagged variants, enable mechanistic studies, drug screening, and structural analyses (e.g., crystallography). Its dual role as an HSP70 modulator and disease-associated factor highlights its relevance in therapeutic targeting, particularly for pathologies driven by proteostasis imbalance.
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