| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GERP |
| Uniprot No | Q9BZR9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-551aa |
| 氨基酸序列 | MAENWKNCFE EELICPICLH VFVEPVQLPC KHNFCRGCIG EAWAKDSGLV RCPECNQAYN QKPGLEKNLK LTNIVEKFNA LHVEKPPAAL HCVFCRRGPP LPAQKVCLRC EAPCCQSHVQ THLQQPSTAR GHLLVEADDV RAWSCPQHNA YRLYHCEAEQ VAVCQYCCYY SGAHQGHSVC DVEIRRNEIR KMLMKQQDRL EEREQDIEDQ LYKLESDKRL VEEKVNQLKE EVRLQYEKLH QLLDEDLRQT VEVLDKAQAK FCSENAAQAL HLGERMQEAK KLLGSLQLLF DKTEDVSFMK NTKSVKILMD RTQTCTSSSL SPTKIGHLNS KLFLNEVAKK EKQLRKMLEG PFSTPVPFLQ SVPLYPCGVS SSGAEKRKHS TAFPEASFLE TSSGPVGGQY GAAGTASGEG QSGQPLGPCS STQHLVALPG GAQPVHSSPV FPPSQYPNGS AAQQPMLPQY GGRKILVCSV DNCYCSSVAN HGGHQPYPRS GHFPWTVPSQ EYSHPLPPTP SVPQSLPSLA VRDWLDASQQ PGHQDFYRVY GQPSTKHYVT S |
| 预测分子量 | 61,4 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GERP重组蛋白的虚构参考文献示例(非真实文献，仅供格式参考)：
1. **《重组蛋白GERP的结构与功能分析》**
作者：Zhang L. et al.
摘要：研究通过X射线晶体学解析了GERP重组蛋白的三维结构，揭示了其与DNA结合的活性位点，并验证了其在基因调控中的潜在作用。
2. **《高效表达GERP重组蛋白的工程菌株构建》**
作者：Kim S., Patel R.
摘要：优化了大肠杆菌表达系统中GERP重组蛋白的产量，通过密码子偏好性改造和发酵条件调控，使蛋白产率提升至1.2 g/L。
3. **《GERP重组蛋白在神经退行性疾病模型中的应用》**
作者：Chen H. et al.
摘要：在小鼠模型中验证了GERP重组蛋白对α-突触核蛋白聚集的抑制作用，表明其可能成为帕金森病治疗的候选分子。
4. **《基于GERP的进化保守性区域预测工具开发》**
作者：Smith J., Wang Y.
摘要：结合GERP重组蛋白的保守性评分，开发了一种新型生物信息学算法，用于识别基因组中功能性非编码区域。
(注：以上文献为模拟示例，实际研究中请通过学术数据库检索相关论文。)
**Background of Genetically Engineered Recombinant Proteins (GERPs)**
Genetically Engineered Recombinant Proteins (GERPs) are synthetic proteins produced through recombinant DNA technology, a cornerstone of modern biotechnology. This process involves isolating a target gene encoding a specific protein, modifying it *in vitro*, and inserting it into a host organism (e.g., bacteria, yeast, or mammalian cells) for expression. The host’s cellular machinery then synthesizes the protein, which is harvested and purified for various applications.
The development of GERPs traces back to the 1970s, with breakthroughs like the creation of synthetic insulin in 1978—the first recombinant protein approved for medical use. Advances in molecular biology, such as PCR, CRISPR-based gene editing, and high-throughput sequencing, have since refined the precision, efficiency, and scalability of protein engineering.
GERPs are pivotal in biotechnology and medicine. They enable the production of therapeutics (e.g., monoclonal antibodies, vaccines, and hormones), industrial enzymes, and research tools. Unlike naturally extracted proteins, GERPs offer advantages like consistency, scalability, and reduced contamination risks. Custom modifications (e.g., fusion tags, stability enhancements, or altered binding affinities) further expand their utility.
Challenges persist, including optimizing expression systems for complex proteins requiring post-translational modifications (e.g., glycosylation). Researchers leverage diverse host systems—*E. coli* for simplicity, mammalian cells for human-like modifications—to address these needs.
GERPs also drive innovation in synthetic biology and personalized medicine, with applications in targeted cancer therapies, regenerative medicine, and sustainable biomanufacturing. Ongoing advancements in AI-driven protein design and modular cloning systems promise to accelerate their development, making GERPs indispensable in solving global health and industrial challenges.
In summary, GERPs represent a fusion of genetic engineering and industrial biotechnology, revolutionizing how proteins are designed, produced, and utilized across sectors.
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