| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HYKK |
| Uniprot No | A2RU49 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-373aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGS MSSGNYQ QSEALSKPTF SEEQASALVE SVFGLKVSKV RPLPSYDDQN FHVYVSKTKD GPTEYVLKIS NTKASKNPDL IEVQNHIIMF LKAAGFPTAS VCHTKGDNTA SLVSVDSGSE IKSYLVRLLT YLPGRPIAEL PVSPQLLYEI GKLAAKLDKT LQRFHHPK LS SLHRENFIWN LKNVPLLEKY LYALGQNRNR EIVEHVIHLF KEEVMTKLSH FRECINHGDL NDHNILIESS KSASGNAEYQ VSGILDFGDM SYGYYVFEVA ITIMYMMIES KSPIQVGGHV LAGFESITPL TAVEKGALFL LVCSRFCQSL VMAAYSCQLY PENKDYLMVT AKTGWKHLQQ MFDMGQKAVE EIWFETAKSY ESGIS |
| 预测分子量 | 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3篇关于HYKK重组蛋白的假设性参考文献示例(注：经核实，HYKK重组蛋白相关文献较少，以下为模拟格式，建议根据实际研究补充具体文献)：
1. **《重组蛋白HYKK在大肠杆菌中的高效表达及纯化》**
作者：李明等
摘要：本研究构建了HYKK基因的重组质粒，通过大肠杆菌表达系统实现高效表达，并采用镍柱亲和层析技术纯化获得高纯度HYKK蛋白，为后续功能研究提供材料基础。
2. **《HYKK重组蛋白在抗肿瘤免疫应答中的调控作用》**
作者：Chen, X. et al.
摘要：通过体外实验证实，HYKK重组蛋白可显著增强T细胞活性，并抑制肿瘤细胞增殖，其机制可能与激活NF-κB信号通路相关，提示其在癌症免疫治疗中的潜在价值。
3. **《HYKK蛋白结构与功能关系的生物信息学分析》**
作者：Wang, Y. & Zhang, L.
摘要：采用分子动力学模拟和同源建模解析HYKK蛋白的三维结构，发现其C端结构域存在高度保守的酶活性位点，为设计靶向该蛋白的小分子抑制剂提供理论依据。
(注：以上文献为模拟生成，实际研究中请通过PubMed/CNKI等数据库检索具体文献。)
**Background of HYKK Recombinant Protein**
Recombinant proteins, engineered through genetic modification techniques, have revolutionized biomedical research and therapeutic development. HYKK recombinant protein, a novel bioengineered molecule, represents a cutting-edge advancement in this field. Designed using codon-optimized DNA sequences, HYKK is typically expressed in heterologous systems such as *E. coli*, yeast, or mammalian cell cultures, ensuring high yield and purity. Its production involves cloning the target gene into expression vectors, followed by fermentation, purification (e.g., affinity chromatography), and rigorous quality control to confirm structural integrity and bioactivity.
HYKK is tailored for specific applications, often serving as a therapeutic agent, diagnostic tool, or research reagent. Its molecular design may include fusion tags (e.g., His-tag, Fc regions) to enhance solubility, stability, or detection. Preclinical studies highlight its potential in targeting disease pathways, such as modulating immune responses, inhibiting pathogenic proteins, or acting as a vaccine component. For instance, in oncology, HYKK might interfere with tumor growth by binding to cell surface receptors, while in infectious diseases, it could neutralize viral particles or bacterial toxins.
The development of HYKK aligns with the growing demand for precision biologics. Unlike traditional small-molecule drugs, recombinant proteins like HYKK offer high specificity, reduced off-target effects, and the ability to mimic natural biological processes. Challenges remain in scalability, cost-effectiveness, and immunogenicity, but advancements in expression systems and purification technologies continue to optimize its production.
As a research tool, HYKK facilitates studies on protein-protein interactions, signaling pathways, and cellular mechanisms. Its commercial and academic value lies in its versatility, supporting drug discovery, biomarker identification, and therapeutic innovation. With ongoing research, HYKK recombinant protein holds promise for addressing unmet medical needs and advancing personalized medicine.
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