| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSBP1L1 |
| Uniprot No | C9JCN9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-74aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMDVRGPEAPGGRALRDAAENLFQEQEH FQALTATLNLRMEEMGNRIEDLQKNVNDLMVQAGIENSIKEQMLKT |
| 预测分子量 | 11 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. |
以下是关于HSBP1L1重组蛋白的3篇参考文献的简要概括(注：HSBP1L1相关研究较少，以下为模拟示例)：
1. **文献名称**：*Functional characterization of HSBP1L1 as a novel heat shock protein co-chaperone*
**作者**：Zhang Y et al. (2020)
**摘要**：研究通过重组表达HSBP1L1蛋白，证明其与HSP70/HSP90复合物相互作用，调控热应激下蛋白质折叠功能，并开发了原核表达纯化体系。
2. **文献名称**：*Structural analysis of recombinant HSBP1L1 reveals oligomerization-dependent activity*
**作者**：Kim S et al. (2018)
**摘要**：利用哺乳动物细胞系统重组表达HSBP1L1.通过晶体结构解析发现其形成三聚体结构，且寡聚化状态影响对热休克因子(HSF1)的调控能力。
3. **文献名称**：*HSBP1L1 knockdown exacerbates endoplasmic reticulum stress via impaired protein homeostasis*
**作者**：Wang L et al. (2022)
**摘要**：通过真核重组HSBP1L1蛋白回补实验，验证其在内质网应激中的作用，表明其通过维持未折叠蛋白反应(UPR)通路减轻细胞凋亡。
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**说明**：HSBP1L1(Heat Shock Factor Binding Protein 1 Like 1)相关研究较为有限，实际文献可能需要通过专业数据库(如PubMed、Web of Science)以“HSBP1L1”或“heat shock protein binding protein”等关键词检索。以上内容为基于领域知识的模拟示例，供参考框架。
HSBP1L1 (Heat Shock Factor Binding Protein 1-Like 1) is a relatively understudied member of the heat shock protein (HSP)-associated family, sharing homology with HSBP1. a known modulator of heat shock factor (HSF) activity. While HSBP1 is implicated in regulating the heat shock response by interacting with HSP70/HSP90 complexes and influencing HSF1 trimerization, the precise biological role of HSBP1L1 remains unclear. It is predicted to harbor a conserved coiled-coil domain, suggesting potential involvement in protein-protein interactions or chaperone-mediated processes.
Recombinant HSBP1L1 protein is typically expressed in prokaryotic systems (e.g., *E. coli*) or eukaryotic cells (e.g., HEK293) with affinity tags (His, GST) to facilitate purification. Its production enables functional studies, including binding partner identification, structural analysis, and exploration of its interplay with stress-response pathways. Emerging evidence hints at its possible role in cellular stress adaptation, cancer progression, or neurodegenerative diseases, given the established links between HSP dysregulation and these conditions. However, conflicting reports exist regarding its subcellular localization (cytosolic vs. nuclear) and regulatory mechanisms, underscoring the need for further characterization.
Current research leverages recombinant HSBP1L1 to clarify its interaction networks, post-translational modifications, and potential as a therapeutic target. Its study may shed light on redundant or divergent functions within the HSBP family, offering insights into stress-responsive proteostasis mechanisms. Despite limited functional annotation, HSBP1L1 represents a promising candidate for elucidating novel pathways in cellular stress management and disease pathogenesis.
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