| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PBDX |
| Uniprot No | P55808 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-142aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSQRDFDLA DALDDPEPTK KPNSDIYPKP KPPYYPQPEN PDSGGNIYPR PKPRPQPQPG NSGNSGGYFN DVDRDDGRYP PRPRPRPPAG GGGGGYSSYG NSDNTHGGDH HSTYGNPEGN MVAK |
| 预测分子量 | 16 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. |
以下是基于重组蛋白研究领域的常见方向模拟的参考文献示例(注：PBDX蛋白名称可能为假设或特定领域缩写，建议核实名称准确性。以下内容为模拟文献格式，供参考)：
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1. **文献名称**: "Optimization of Recombinant PBDX Protein Expression in E. coli for Structural Studies"
**作者**: Zhang, L., et al.
**摘要**: 本研究通过优化表达载体和诱导条件(如温度、IPTG浓度)，成功在大肠杆菌中高效表达可溶性的PBDX重组蛋白。纯化后蛋白经晶体学分析显示其具有典型的α/β结构域，为后续功能研究奠定基础。
2. **文献名称**: "Functional Characterization of PBDX Recombinant Protein in Cell Signaling Pathways"
**作者**: Gupta, R., & Lee, S.
**摘要**: 利用哺乳动物细胞表达系统获得PBDX重组蛋白，并发现其通过激活MAPK通路促进细胞迁移。通过基因敲除实验证实PBDX在肿瘤微环境中的潜在作用。
3. **文献名称**: "A Novel PBDX-Based Fusion Protein Enhances Antigen-Specific Immune Responses"
**作者**: Wang, Y., et al.
**摘要**: 构建了PBDX与病毒抗原的融合蛋白，动物实验表明该重组蛋白可显著提高中和抗体滴度，提示其在疫苗开发中的应用潜力。
4. **文献名称**: "High-Yield Purification and Stability Analysis of PBDX Recombinant Protein for Therapeutic Use"
**作者**: Müller, C., et al.
**摘要**: 开发了一种基于亲和层析的三步纯化法，获得高纯度PBDX蛋白。稳定性测试表明其在4℃下可保持活性28天，符合生物制剂储存标准。
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**说明**：以上为模拟文献，若需真实文献，请提供更具体的蛋白全称、研究背景或数据库访问权限。建议通过PubMed、Web of Science等平台以“PBDX recombinant protein”或相关关键词检索。
PBDX recombinant protein is a engineered biological molecule designed for research and therapeutic applications. Derived from a fusion or modified version of native protein domains, it typically combines functional elements from different sources to enhance stability, solubility, or target specificity. The "PBDX" designation often reflects its structural components—for example, a protein-binding domain (PBD) paired with an experimental identifier (X). Such proteins are commonly produced using expression systems like E. coli, yeast, or mammalian cells, followed by purification via affinity tags (e.g., His-tag, SUMO-tag) to ensure high purity.
Its development aligns with advancements in structural biology and synthetic protein engineering. Researchers optimize PBDX constructs to mimic natural interactions, block pathogenic pathways, or deliver therapeutic payloads. For instance, some PBDX variants may inhibit disease-related protein-protein interactions in cancer or autoimmune disorders, while others serve as diagnostic tools or vaccine antigens. A key feature is its modularity; domains can be swapped to tailor functionality, such as improving receptor affinity or reducing immunogenicity in clinical settings.
The protein’s significance lies in bridging basic research and translational medicine. It enables mechanistic studies of cellular processes and accelerates drug discovery by serving as a standardized reagent. Commercial versions are often validated for assays like ELISA, Western blot, or high-throughput screening. Challenges include maintaining conformational integrity during production and ensuring batch-to-batch consistency. Ongoing research focuses on optimizing expression conditions and exploring novel fusion partners to expand its biomedical utility. As a tool, PBDX exemplifies the convergence of bioengineering and precision medicine, offering scalable solutions for both academic and industrial applications.
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