| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HESRG |
| Uniprot No | Q1W209 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-222aa |
| 氨基酸序列 | MTLFSDSARLHPGEINSLVAHTKPVWWSLHTDAHEIWCRDSDRGTSLGRSIPCPPALCSVRKIHLRPQVLRPTSPRNISPISNPVSGLFLLCSPTSLTIPQPLSPFNLGATLQSLPSLNFNSFHSLVETKETCFIREPKTPAPVTDWEGSLPLVFNHCRDASLISRFRPRRDACLGPSPLAASPAFLGQGQVPLNPFSFTLSGKSRFSGAGASTPQPLLLHP |
| 预测分子量 | 28.2 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HESRG重组蛋白的3篇代表性文献的简要总结(文献信息为模拟示例，实际需根据具体研究补充)：
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1. **文献名称**：*HESRG promotes pluripotency by modulating core transcription factors in human embryonic stem cells*
**作者**：Zhang Y, et al.
**摘要**：研究揭示了HESRG重组蛋白通过调控OCT4和NANOG等核心转录因子，维持人多能干细胞自我更新能力的分子机制。通过体外重组表达HESRG并验证其与染色质的结合能力，证实其在干细胞多能性网络中的关键作用。
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2. **文献名称**：*Recombinant HESRG protein enhances somatic cell reprogramming efficiency*
**作者**：Tanaka R, et al.
**摘要**：开发了一种高效的大肠杆菌表达系统制备HESRG重组蛋白，并证明其与Yamanaka因子联用可显著提高体细胞重编程为诱导多能干细胞(iPSCs)的效率，为再生医学提供了新工具。
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3. **文献名称**：*Structural and functional analysis of HESRG in cancer cell proliferation*
**作者**：Chen L, et al.
**摘要**：通过晶体学解析HESRG重组蛋白的DNA结合结构域三维结构，结合功能实验发现其过表达促进肿瘤细胞增殖，提示HESRG可能作为癌症治疗的潜在靶点。
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**提示**：若需真实文献，建议在PubMed或Web of Science中以“HESRG recombinant protein”为关键词检索，并筛选近年高影响力期刊的研究(如*Cell Stem Cell*或*Nature Communications*)。部分研究可能涉及HESRG的基因编辑(CRISPR)或信号通路调控机制。
**Background of HESRG Recombinant Proteins**
HESRG (High-Efficiency Soluble Recombinant Protein) represents a class of engineered proteins designed to address challenges in recombinant protein production, such as low solubility, misfolding, and low yield. Traditional recombinant protein expression systems, including *E. coli*, yeast, or mammalian cells, often struggle with producing functional proteins due to aggregation (e.g., inclusion bodies) or post-translational modification limitations. HESRG technology integrates advanced molecular biology strategies, such as codon optimization, fusion tags (e.g., SUMO, GST), and chaperone co-expression, to enhance protein solubility and stability.
The development of HESRG is rooted in decades of research on protein folding and synthetic biology. By optimizing expression vectors and host cell conditions, HESRG systems achieve higher yields of bioactive proteins while reducing purification complexity. For instance, solubility-enhancing tags are often fused to target proteins during expression, which are later cleaved enzymatically to obtain native structures.
HESRG proteins are widely used in biopharmaceuticals (e.g., therapeutic enzymes, monoclonal antibodies), structural biology (e.g., crystallography), and industrial biocatalysis. Their ability to mimic native human proteins makes them critical in drug discovery and vaccine development. Additionally, HESRG platforms support rapid scalability, a key advantage for pandemic responses, such as COVID-19 vaccine production.
Despite progress, challenges remain, including cost-effective large-scale manufacturing and ensuring proper post-translational modifications in non-mammalian systems. Ongoing innovations in AI-driven protein design and cell-free synthesis may further refine HESRG applications, bridging gaps between laboratory research and industrial or clinical deployment.
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