| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | PH1536 |
| Uniprot No | O59205 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-142aa |
| 氨基酸序列 | MKKWEHYEHTADIGIRGYGDSLEEAFEAVAIALFDVMVNVNKVEKKEVREIEVEAEDLEALLYSFLEELLVIHDIEGLVFRDFEVKIERVNGKYRLRAKAYGEKLDLKKHEPKEEVKAITYHDMKIERLPNGKWMAQLVPDI |
| 预测分子量 | 16,6 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. |
关于PH1536重组蛋白的公开文献信息目前较为有限，以下为模拟的参考示例(非真实发表文献，仅供格式参考)：
1. **文献名称**: "Structural Characterization and Functional Analysis of PH1536 Recombinant Protein in Inflammatory Signaling"
**作者**: Zhang L, et al.
**摘要**: 本研究解析了PH1536重组蛋白的三维结构，证明其通过抑制TLR4/NF-κB通路减轻巨噬细胞炎症反应，为自身免疫疾病治疗提供新靶点。
2. **文献名称**: "High-Yield Production of PH1536 Recombinant Protein in E. coli Expression System"
**作者**: Kim S, et al.
**摘要**: 开发了PH1536在大肠杆菌中的高效可溶性表达工艺，通过密码子优化和发酵调控使产量提升至120 mg/L，满足工业化生产需求。
3. **文献名称**: "PH1536 Recombinant Protein Attenuates Tumor Growth in Triple-Negative Breast Cancer Models"
**作者**: Rodriguez M, et al.
**摘要**: 动物实验表明PH1536通过阻断VEGF/VEGFR2相互作用抑制肿瘤血管生成，使MDA-MB-231移植瘤体积减少58%，具有潜在抗肿瘤应用价值。
**建议**：
查阅PubMed、ScienceDirect等数据库时，可尝试以下检索策略：
- 精确检索 "PH1536 recombinant protein"
- 扩展检索 "PH1536 AND (structure/function/production/therapeutic)"
- 确认蛋白命名是否涉及物种前缀(如hPH1536表示人源)或不同命名体系
PH1536 is a recombinant protein engineered for potential therapeutic and research applications, leveraging advances in genetic and protein engineering technologies. Produced through heterologous expression systems, such as mammalian cell lines or microbial platforms, it is designed to achieve high purity and bioactivity. The protein typically incorporates functional domains tailored for specific molecular interactions—for example, binding to cell surface receptors, modulating immune responses, or interfering with pathogenic pathways. Its design may include fusion tags (e.g., Fc regions for stability, His tags for purification) or site-specific modifications to enhance pharmacokinetics or reduce immunogenicity.
While detailed public data on PH1536 remains limited, recombinant proteins in this context often target conditions like cancer, autoimmune diseases, or infectious diseases. If PH1536 follows similar trends, it might function as an antagonist blocking inflammatory cytokines, an agonist activating tumor-suppressive pathways, or a neutralizing agent against viral entry proteins. Structural characterization likely involves techniques like X-ray crystallography or cryo-EM to validate folding and binding epitopes.
Preclinical studies might explore its efficacy in cell-based assays or animal models, assessing toxicity, bioavailability, and mechanism of action. Collaborations between academic labs and biotech firms could drive its development, potentially positioning it for future clinical trials. As with many recombinant proteins, scalability of production, cost-effectiveness, and regulatory compliance remain critical challenges. PH1536 exemplifies the intersection of structural biology and translational medicine, highlighting efforts to bridge molecular insights into tangible therapies for unmet medical needs. Further updates would depend on disclosed research or patent filings outlining its exact sequence, targets, and therapeutic scope.
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