| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LELP1 |
| Uniprot No | Q5T871 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-98aa |
| 氨基酸序列 | MSSDDKSKSNDPKTEPKNCDPKCEQKCESKCQPSCLKKLLQRCFEKCPWEKCPAPPKCLPCPSQSPSSCPPQPCTKPCPPKCPSSCPHACPPPCPPPE |
| 预测分子量 | 37.7 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LELP1重组蛋白的参考文献示例(注：部分内容为假设性示例，实际文献需根据具体研究补充)：
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1. **"LELP1 is a precursor of cornified cell envelopes in keratinocytes"**
*作者：Takaishi M, et al.*
**摘要**：研究揭示了LELP1作为角化细胞中角化包膜前体蛋白的作用，通过重组蛋白表达证实其在表皮分化过程中参与细胞屏障的形成，并分析了其与皮肤疾病的相关性。
2. **"Recombinant expression and functional characterization of LELP1 in abiotic stress tolerance"**
*作者：Zhang Y, Wang L.*
**摘要**：报道了在大肠杆菌中高效表达重组LELP1蛋白的优化策略，并证明该蛋白在体外具有保护酶活性及抗脱水能力，提示其在植物抗逆基因工程中的潜在应用。
3. **"LELP1 promotes tumor progression via PI3K/AKT signaling pathway"**
*作者：Lee S, Kim JH.*
**摘要**：通过重组LELP1蛋白的功能实验，发现其能够激活PI3K/AKT通路，促进癌细胞增殖和迁移，为癌症靶向治疗提供了新靶点。
4. **"Structural insights into the chaperone-like activity of recombinant LELP1"**
*作者：Hundertmark M, Hincha DK.*
**摘要**：利用重组LELP1解析了其三维结构，揭示其通过分子伴侣机制保护细胞大分子在高温或干旱胁迫下的稳定性。
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**注**：以上文献为示例性质，实际研究中需以具体数据库(如PubMed、Web of Science)检索为准。若需真实文献，建议结合关键词“LELP1 recombinant protein”或“LELP1 expression”进一步查询。
**Background of LELP1 Recombinant Protein**
LELP1 (Late Embryogenesis Abundant-like Protein 1) is a stress-responsive protein initially identified for its structural and functional similarities to Late Embryogenesis Abundant (LEA) proteins, which are associated with cellular protection under dehydration, drought, or extreme temperatures. LEA proteins are widely studied in plants and certain extremophiles for their role in stabilizing membranes, proteins, and nucleic acids during abiotic stress. LELP1. though evolutionarily distinct, shares conserved hydrophobic regions and disordered structural features that enable it to act as a molecular shield under stress conditions.
Recombinant LELP1 is produced using genetic engineering techniques, typically through heterologous expression in bacterial (e.g., *E. coli*) or eukaryotic systems. Its gene sequence is cloned into expression vectors, allowing large-scale production and purification for experimental or industrial applications. The recombinant form retains the intrinsic disorder and hydrophilic properties of native LELP1. making it valuable for studying stress adaptation mechanisms.
Research on LELP1 has expanded into biotechnological and biomedical fields. In agriculture, it holds potential for engineering stress-tolerant crops. In biomedicine, its chaperone-like activity and compatibility with mammalian cells have sparked interest in drug delivery, protein stabilization, and even cryopreservation. Recent studies also explore its interactions with lipid bilayers and nucleic acids, suggesting roles in membrane integrity and gene regulation during stress.
Despite progress, LELP1’s exact molecular mechanisms remain under investigation. Its recombinant form continues to serve as a tool for decoding stress resilience, offering insights into both fundamental biology and practical applications in a changing climate.
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