| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | inaX |
| Uniprot No | P01567 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-189aa |
| 氨基酸序列 | MARSFSLLMVVLVLSYKSICSLGCDLPQTHSLRNRRALILLAQMGRISPFSCLKDRHEFRFPEEEFDGHQFQKTQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNDLEACVIQEVGVEETPLMNEDFILAVRKYFQRITLYLMEKKYSPCAWEVVRAEIMRSFSFSTNLKKGLRRKD |
| 预测分子量 | 22,1 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inaX重组蛋白的3篇参考文献示例(注：以下内容为模拟生成，实际文献需通过学术数据库检索确认)：
1. **《Cloning and expression of recombinant inaX protein in Escherichia coli》**
- 作者：Zhang Y. et al.
- 摘要：研究报道了从丁香假单胞菌(Pseudomonas syringae)中克隆inaX基因，并在大肠杆菌中成功表达功能性重组inaX蛋白，验证了其冰核活性及低温稳定性。
2. **《Self-assembly of recombinant inaX protein for bio-nanomaterial applications》**
- 作者：Lee S. et al.
- 摘要：通过重组表达纯化inaX蛋白，发现其可在体外自组装形成纳米纤维结构，展示了在生物传感器或组织工程中的潜在应用价值。
3. **《Optimization of fermentation conditions for high-yield inaX recombinant protein production》**
- 作者：Wang H. et al.
- 摘要：系统研究了诱导温度、IPTG浓度和培养时间对inaX重组蛋白表达量的影响，优化后蛋白产量提升3倍，为规模化生产提供依据。
建议通过PubMed或Google Scholar以关键词“inaX recombinant protein”、“Ice nucleation protein expression”检索最新文献以获取准确信息。
InaX is a recombinant protein engineered through advanced genetic and biotechnological approaches, designed to address specific challenges in molecular biology, diagnostics, and therapeutic development. Derived from the ice nucleation protein (INP) family—originally identified in environmental bacteria like *Pseudomonas syringae*—InaX leverages the unique properties of its parent protein, which naturally facilitates ice crystal formation at high temperatures. Researchers have repurposed this scaffold for its ability to display functional domains, peptides, or antigens on its surface, making it a versatile tool for protein engineering.
The development of InaX stems from the growing demand for stable, customizable proteins that retain functionality under diverse conditions. By modifying the INP gene sequence, scientists optimized InaX for enhanced solubility, stability, and compatibility with heterologous expression systems (e.g., *E. coli*), enabling cost-effective large-scale production. Its modular structure allows fusion with target molecules—such as enzymes, antibodies, or vaccine antigens—without disrupting their activity. This flexibility has broadened its applications in biosensing, targeted drug delivery, vaccine design, and synthetic biology. For instance, InaX-based biosensors exploit its surface-display capability to detect pathogens or biomarkers, while its use in vaccines improves antigen presentation to immune cells.
Recent studies highlight InaX’s potential in nanotechnology and material science, where its self-assembling properties aid in creating functionalized nanoparticles or bioactive coatings. Ongoing research focuses on refining its design to minimize immunogenicity and improve tissue-specific targeting, paving the way for clinical translation. As a bridge between natural protein behavior and engineered functionality, InaX exemplifies the convergence of bioinspiration and precision biotechnology.
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