| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | GT-1 |
| Uniprot No | Q9FX53 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-406aa |
| 氨基酸序列 | MFISDKSRPTDFYKDDHHNSSTTSTTRDMMIDVLTTTNESVDLQSHHHHNHHNHHLHQSQPQQQILLGESSGEDHEVKAPKKRAETWVQDETRSLIMFRRGMDGLFNTSKSNKHLWEQISSKMREKGFDRSPTMCTDKWRNLLKEFKKAKHHDRGNGSAKMSYYKEIEDILRERSKKVTPPQYNKSPNTPPTSAKVDSFMQFTDKGFDDTSISFGSVEANGRPALNLERRLDHDGHPLAITTAVDAVAANGVTPWNWRETPGNGDDSHGQPFGGRVITVKFGDYTRRIGVDGSAEAIKEVIRSAFGLRTRRAFWLEDEDQIIRCLDRDMPLGNYLLRLDDGLAIRVCHYDESNQLPVHSEEKIFYTEEDYREFLARQGWSSLQVDGFRNIENMDDLQPGAVYRGVR |
| 预测分子量 | 48.7 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GT-1重组蛋白的3篇参考文献(文献为虚拟示例，仅供参考)：
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1. **文献名称**: *"Functional Characterization of GT-1 Recombinant Protein in Plant Stress Response"*
**作者**: Zhang, Y. et al. (2015)
**摘要**: 研究通过原核表达系统纯化GT-1重组蛋白，发现其能够特异性结合植物胁迫响应基因的启动子区域(如盐胁迫相关基因)，并增强转基因拟南芥对非生物胁迫的耐受性，揭示了GT-1在植物抗逆中的转录调控作用。
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2. **文献名称**: *"Production and Structural Analysis of GT-1: A Key Transcription Factor in Light Signaling Pathways"*
**作者**: Liu, H. et al. (2018)
**摘要**: 本文利用昆虫细胞表达系统高效制备GT-1重组蛋白，通过X射线晶体学解析其三维结构，发现其DNA结合域的保守性，并验证其通过结合光响应元件(如G-box)调控光信号下游基因的表达。
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3. **文献名称**: *"GT-1 Recombinant Protein Enhances Antiviral Immunity in Mammalian Cells"*
**作者**: Chen, L. et al. (2020)
**摘要**: 研究在大肠杆菌中表达并纯化GT-1重组蛋白，证明其可通过激活干扰素信号通路(如IRF3磷酸化)增强哺乳动物细胞对RNA病毒的抗性，为开发基于GT-1的免疫调节剂提供了实验依据。
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4. **文献名称**: *"Optimization of GT-1 Recombinant Protein Expression in Yeast for Industrial Applications"*
**作者**: Wang, Q. et al. (2022)
**摘要**: 通过优化毕赤酵母表达系统的培养条件(如诱导温度、pH)，显著提高了GT-1重组蛋白的产量和稳定性，并验证其在体外酶活性实验中作为生物催化剂的潜力，为规模化生产奠定了基础。
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注：以上文献为模拟内容，实际研究中请根据具体研究方向在学术数据库(如PubMed、Web of Science)检索真实文献。
The GT-1 recombinant protein is a biologically engineered molecule designed for research and therapeutic applications, derived from the functional domains of natural proteins associated with immune regulation or cellular signaling. Its development stems from advances in genetic engineering and structural biology, which enable precise modification of protein sequences to enhance stability, solubility, or target specificity. GT-1 typically incorporates domains such as receptor-binding regions or enzymatic motifs, optimized through codon usage adaptation for high-yield expression in host systems like *E. coli*, yeast, or mammalian cells.
Originally inspired by studies on immune checkpoint proteins or growth factors, GT-1 aims to modulate specific pathways—for instance, enhancing antitumor responses by interfering with immunosuppressive signals or promoting tissue repair. Its recombinant nature allows scalability for industrial production while minimizing batch-to-batch variability. Characterization involves techniques like SDS-PAGE, Western blot, and surface plasmon resonance (SPR) to confirm purity, folding, and binding affinity.
Preclinical studies highlight its potential in disease models, such as cancer immunotherapy or inflammatory disorders, though clinical translation requires further validation of safety and efficacy. Collaborations between academic labs and biotech firms often drive its development, reflecting the growing emphasis on targeted biologics. As a research tool, GT-1 facilitates mechanistic studies of protein interactions, while its therapeutic iteration aligns with trends in personalized medicine. Challenges include optimizing pharmacokinetics and minimizing immunogenicity, common hurdles in recombinant protein therapeutics. Ongoing refinements in fusion tags or PEGylation strategies aim to address these limitations, positioning GT-1 as a versatile candidate in both biomedical research and drug development pipelines.
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