| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | HSP18.1 |
| Uniprot No | P19243 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-158aa |
| 氨基酸序列 | MSLIPSFFSGRRSNVFDPFSLDVWDPLKDFPFSNSSPSASFPRENPAFVSTRVDWKETPEAHVFKADLPGLKKEEVKVEVEDDRVLQISGERSVEKEDKNDEWHRVERSSGKFLRRFRLPENAKMDKVKASMENGVLTVTVPKEEIKKAEVKSIEISG |
| 预测分子量 | 34.1kDa |
| 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HSP18.1重组蛋白的3篇模拟参考文献(注：文献信息为示例，实际引用需核实)：
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1. **文献名称**：*Recombinant HSP18.1 from Pisum sativum exhibits chaperone activity in vitro*
**作者**：Lee GJ, Roseman AM, Vierling E
**摘要**：本研究在大肠杆菌中重组表达了豌豆HSP18.1蛋白，证实其具有体外分子伴侣功能，可抑制热诱导的溶菌酶聚集，并依赖ATP水解调控底物结合与释放。
2. **文献名称**：*Structural insights into the oligomeric plasticity of HSP18.1 under stress conditions*
**作者**：Sun Y, Chen C, Zhang H
**摘要**：通过冷冻电镜解析HSP18.1的动态寡聚结构，发现其在热应激下形成多聚体以保护细胞蛋白，为小热休克蛋白的应激响应机制提供结构依据。
3. **文献名称**：*HSP18.1 overexpression enhances thermotolerance in transgenic Arabidopsis*
**作者**：Wang L, Liu J, Zhu JK
**摘要**：过表达重组HSP18.1的拟南芥表现出显著耐热性提升，表明该蛋白通过稳定膜结构和蛋白酶体活性参与植物热胁迫应答。
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**提示**：实际研究中建议通过PubMed或Web of Science检索具体文献，并关注HSP18.1的物种来源(如植物、微生物等)及研究方向(结构、功能、应用)。
HSP18.1 is a member of the small heat shock protein (sHSP) family, a class of molecular chaperones ubiquitously found across organisms. sHSPs are characterized by their low molecular weight (12–43 kDa) and a conserved α-crystallin domain that enables them to stabilize partially unfolded proteins under stress conditions. HSP18.1. specifically, has been studied in plants such as *Arabidopsis thaliana*, where it plays a critical role in thermotolerance. During heat stress, HSP18.1 expression is upregulated, and the protein assembles into oligomers to prevent aggregation of denatured cellular proteins, aiding in cellular recovery post-stress.
Recombinant HSP18.1 is produced using heterologous expression systems (e.g., *E. coli*), where the gene encoding HSP18.1 is cloned into expression vectors, induced by IPTG, and purified via affinity chromatography. This recombinant form retains its chaperone activity, making it a valuable tool for in vitro studies on protein folding, stress response mechanisms, and interactions with client proteins.
Research on HSP18.1 has broader implications. In agriculture, understanding its function could enhance crop resilience to climate-induced heat stress. In biomedicine, sHSPs are linked to diseases like Alzheimer’s, where protein aggregation is pathological. Studying HSP18.1’s chaperone mechanisms may inform therapeutic strategies. Despite its compact size, HSP18.1 exemplifies the intricate balance between structural simplicity and functional versatility in stress adaptation.
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