| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLUB4 |
| Uniprot No | P14614 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-303aa |
| 氨基酸序列 | QLFGPNVNPWHNPRQGGFRECRFDRLQAFEPLRRVRSEAGVTEYFDEKNEQFQCTGTFVIRRVIEPQGLLVPRYSNTPGMVYIIQGRGSMGLTFPGCPATYQQQFQQFLPEGQSQSQKFRDEHQKIHQFRQGDIVALPAGVAHWFYNEGDAPVVALYVFDLNNNANQLEPRQKEFLLAGNNNREQQMYGRSIEQHSGQNIFSGFNNELLSEALGVNALVAKRLQGQNDQRGEIIRVKNGLKLLRPAFAQQQEQAQQQEQAQAQYQVQYSEEQQPSTRCN |
| 预测分子量 | 39.5 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GLUB4重组蛋白的模拟参考文献示例(注：部分为虚构文献，仅供参考格式)：
1. **文献名称**: "Heterologous expression and purification of barley GLB4 protein in a prokaryotic system"
**作者**: Müller T, et al.
**摘要**: 本研究成功将大麦来源的GLB4基因克隆至大肠杆菌表达系统，优化了重组蛋白的可溶性表达条件，并通过亲和层析获得高纯度蛋白，证实其具有与天然蛋白相似的免疫原性。
2. **文献名称**: "Cryo-EM structure of recombinant GLUB4 reveals its role in seed nutrient storage"
**作者**: Zhang Y, et al.
**摘要**: 利用冷冻电镜解析了重组GLUB4蛋白的三维结构，揭示了其独特的球形结构域，并发现其与植物种子中氮元素储存及释放机制密切相关。
3. **文献名称**: "Functional characterization of recombinant GLUB4 in enhancing abiotic stress tolerance in rice"
**作者**: Kim H, et al.
**摘要**: 在转基因水稻中过表达重组GLUB4蛋白，显著提高了植株在盐胁迫和低温环境下的存活率，表明其在植物抗逆基因工程中的潜在应用价值。
4. **文献名称**: "Scale-up production of bioactive GLUB4 using Pichia pastoris and its application in agricultural biostimulants"
**作者**: Costa L, et al.
**摘要**: 开发了基于毕赤酵母的GLUB4重组蛋白大规模生产工艺，验证其作为叶面喷施生物刺激素可促进作物根系发育及养分吸收效率。
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**注意**：以上文献为示例性质，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。若需特定领域文献，建议结合具体研究背景调整关键词。
GLUb4. a member of the grass pollen allergen family, is a calcium-binding protein originally identified in *Lolium perenne* (perennial ryegrass). Functionally, it belongs to the expansin superfamily, which is associated with cell wall loosening during plant growth and pollen tube elongation. Its recombinant form, GLUb4 recombinant protein, is engineered using heterologous expression systems like *E. coli* or yeast to produce purified, biologically active molecules for research and industrial applications.
Interest in GLUb4 stems from its dual role as an allergen and a potential biotechnological tool. As an allergen, it triggers IgE-mediated immune responses in sensitized individuals, making it a target for allergy diagnostics and immunotherapy development. Recombinant GLUb4 allows standardized allergen production, overcoming variability issues in natural pollen extracts. Structurally, the protein contains two conserved domains: an N-terminal domain with homology to pollen allergens and a C-terminal domain resembling carbohydrate-binding modules. Calcium-binding capacity in its N-terminal region is critical for its biological activity.
Biotechnologically, GLUb4's cell wall-modifying properties have potential applications in biofuel production and agriculture. Its ability to disrupt plant cell wall polysaccharides could enhance enzymatic saccharification of biomass for bioethanol. Recombinant versions are also explored in transgenic crops to modify cell wall architecture, though this remains experimental. Challenges in recombinant production include maintaining proper folding and post-translational modifications, often addressed through codon optimization or eukaryotic expression systems.
Research on GLUb4 recombinant protein bridges allergology, plant physiology, and industrial biotechnology, offering insights into allergen-immune interactions and sustainable bioresource utilization. Ongoing studies focus on structure-function relationships and hypoallergenic variants for therapeutic use.
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