| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HVA |
| Uniprot No | Q00975 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 262 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HVA(假设为植物逆境相关蛋白，如大麦LEA蛋白)重组蛋白的模拟参考文献示例，供参考：
---
1. **"Heterologous Expression of HVA1 Gene in Arabidopsis Confers Tolerance to Water Stress"**
- **作者**: Xu, D., Duan, X., & Wang, B.
- **摘要**: 本研究通过将大麦HVA1基因在拟南芥中异源表达，证明重组HVA1蛋白能显著增强植物对干旱和高盐胁迫的耐受性，可能通过稳定细胞膜结构和保护酶活性实现。
2. **"Purification and Characterization of Recombinant HVA22 Protein from Pichia pastoris"**
- **作者**: Chen, L., Zhang, H., & Li, W.
- **摘要**: 报道了一种利用毕赤酵母系统高效表达和纯化重组HVA22蛋白的方法，并通过体外实验验证其抗氧化活性，为后续功能研究提供基础。
3. **"Crystal Structure Analysis of HVA1 Protein Reveals Its Hydrophilic Protective Mechanism"**
- **作者**: Zhang, Y., Wang, J., & Liu, R.
- **摘要**: 通过X射线晶体学解析HVA1蛋白的三维结构，发现其表面高度亲水性，可能通过结合水分子和保护细胞结构在逆境中发挥作用。
4. **"Recombinant HVA Protein as a Biostimulant for Crop Improvement"**
- **作者**: Kumar, S., & Singh, A.
- **摘要**: 探索重组HVA蛋白作为生物刺激素在作物中的田间应用，显示其能提高玉米和小麦在缺水条件下的产量和生物量。
---
**注意**：以上文献信息为模拟示例，实际研究需通过学术数据库(如PubMed、Web of Science)检索关键词“HVA recombinant protein”或“HVA1 protein expression”获取真实文献。
**Background of HVA Recombinant Protein**
HVA (Hordeum vulgare abscisic acid [ABA]-induced) recombinant proteins are derived from barley (*Hordeum vulgare*), where the native HVA genes encode stress-responsive proteins critical for plant adaptation to environmental challenges such as drought, salinity, and cold. These proteins belong to the Group 3 Late Embryogenesis Abundant (LEA) family, characterized by their hydrophilic, unstructured nature and protective roles during cellular dehydration.
The interest in HVA recombinant proteins stems from their potential in biotechnological applications. By leveraging recombinant DNA technology, HVA genes are cloned and expressed in heterologous systems like *E. coli*, yeast, or plant cell cultures. This allows large-scale production of HVA proteins for functional studies or commercial use. Recombinant HVA proteins retain their biophysical properties, including membrane stabilization, ion-binding capacity, and chaperone-like activity, which help mitigate abiotic stress damage in cells.
In agriculture, transgenic crops engineered to express HVA genes exhibit enhanced stress tolerance, offering a sustainable strategy to improve crop resilience under climate change. Beyond agriculture, HVA proteins are explored in biomedical research for their anti-apoptotic properties and potential in stabilizing biomolecules during lyophilization or extreme storage conditions.
Challenges in HVA recombinant production include optimizing expression yields, ensuring proper post-translational modifications in non-plant systems, and addressing regulatory hurdles for transgenic applications. Despite these, HVA proteins remain a promising tool for both agricultural innovation and industrial biotechnology, bridging plant stress biology with engineered solutions for global sustainability challenges.
×
