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| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GIF |
| Uniprot No | P14174 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-115aa |
| 氨基酸序列 | PMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA |
| 预测分子量 | 41.3 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GIF重组蛋白研究的示例参考文献(注：以下文献为虚拟示例，仅供格式参考)：
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1. **文献名称**：《拟南芥GIF1重组蛋白的表达及其在叶片发育中的功能研究》
**作者**：张立等
**摘要**：本研究通过大肠杆菌表达系统成功纯化了拟南芥GIF1重组蛋白，并证实其通过与生长调控因子GRF相互作用，促进叶片细胞增殖，为植物发育机制提供了新见解。
2. **文献名称**：《GIF重组蛋白的神经保护活性及其机制》
**作者**：王敏、陈昊
**摘要**：利用哺乳动物细胞表达体系制备了人源GIF重组蛋白，实验表明该蛋白能显著抑制氧化应激诱导的神经元凋亡，提示其在神经退行性疾病治疗中的潜在价值。
3. **文献名称**：《毕赤酵母高效表达GIF重组蛋白的工艺优化》
**作者**：刘伟等
**摘要**：通过优化毕赤酵母表达系统的培养条件和诱导策略，将GIF重组蛋白的产量提升至1.2 g/L，为规模化生产奠定了基础。
4. **文献名称**：《GIF重组蛋白与肿瘤细胞生长抑制的关联分析》
**作者**：李明等
**摘要**：体外实验证实，重组表达的GIF蛋白可通过调控MAPK信号通路抑制多种肿瘤细胞系的增殖，为癌症靶向治疗提供了新方向。
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**说明**：以上文献为模拟示例，实际研究中请通过学术数据库(如PubMed、CNKI)检索真实文献。若需进一步协助文献检索，请提供更具体的研究方向或关键词。
GIF recombinant proteins, often associated with the Glutathione-Incorporating Factor (GIF) or similar functional motifs, are engineered through recombinant DNA technology to enable precise study and application in molecular and cellular biology. The development of recombinant protein technology in the late 20th century revolutionized biotechnology by allowing large-scale production of specific proteins in heterologous systems like *E. coli*, yeast, or mammalian cells. GIF proteins, typically characterized by domains facilitating interactions with glutathione or other biomolecules, are designed to enhance solubility, stability, or functional specificity.
These proteins often serve as critical tools in affinity purification, protein-protein interaction studies, or as fusion partners to improve expression yields. For instance, glutathione-S-transferase (GST)-tagged GIF variants are widely used in pull-down assays due to their high affinity for glutathione-coated matrices. Additionally, GIF recombinant proteins may incorporate functional elements like signal peptides or cleavage sites to support proper folding, post-translational modifications, or targeted delivery in therapeutic contexts.
In biomedical research, GIF-based constructs have been applied in drug discovery, vaccine development, and diagnostic assays, leveraging their modularity and adaptability. For example, engineered GIF proteins might act as carriers for antigen presentation or as scaffolds for enzyme immobilization. Recent advancements in synthetic biology and CRISPR-based editing further refine their design, enabling custom-tailored functionalities such as improved pharmacokinetics or reduced immunogenicity. Despite challenges in scalability and cost, GIF recombinant proteins remain pivotal in bridging basic research and industrial applications, underscoring their versatility in modern biotechnology.
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