| 纯度 | >90%SDS-PAGE. |
| 种属 | Yersinia |
| 靶点 | AFP2 |
| Uniprot No | P30230 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-80aa |
| 氨基酸序列 | QKLCQRPSGTWSGVCGNNNACKNQCIRLEKARHGSCNYVFPAHKCICYFPC |
| 预测分子量 | 21.7kDa |
| 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. |
以下是关于重组AFP2蛋白的3篇代表性文献的简要概括(注：文献信息为示例性描述，具体内容请通过学术数据库核实)：
---
1. **文献名称**：*Production and characterization of recombinant human AFP2 in a mammalian expression system*
**作者**：Zhang Y. et al.
**摘要**：研究利用哺乳动物细胞(HEK293)表达重组AFP2蛋白，优化了纯化流程，并通过质谱和免疫印迹验证其结构正确性，证实其与天然AFP相似的糖基化修饰和抗原性。
2. **文献名称**：*AFP2 recombinant protein suppresses T-cell proliferation in hepatocellular carcinoma microenvironment*
**作者**：Tanaka K. et al.
**摘要**：探讨重组AFP2蛋白在肝癌免疫逃逸中的作用，发现其通过抑制T细胞活化和IL-2分泌促进肿瘤免疫抑制，为AFP2的免疫治疗靶向性提供依据。
3. **文献名称**：*Development of an AFP2-specific ELISA using recombinant protein for early cancer diagnosis*
**作者**：Wang L. et al.
**摘要**：基于重组AFP2蛋白建立高灵敏度的ELISA检测方法，临床样本验证显示其对早期肝癌的诊断特异性优于传统AFP检测，具有潜在临床应用价值。
---
**建议**：如需具体文献，可通过PubMed或Google Scholar检索关键词 *"recombinant AFP2 protein"* 或 *"AFP2 recombinant expression"*，并筛选近年发表的高影响力研究。
**Background of AFP2 Recombinant Protein**
AFP2. or Antifreeze Protein Type II, is a class of ice-binding proteins originally identified in cold-adapted organisms, such as Arctic fish, insects, and plants. These proteins play a critical role in survival at subzero temperatures by inhibiting ice crystal growth and recrystallization, thereby preventing cellular damage. AFP2. specifically, is characterized by its distinct structural fold and ice-binding surface, which enables it to interact with ice lattices through hydrogen bonding and hydrophobic interactions.
Recombinant AFP2 is produced via genetic engineering, where the gene encoding AFP2 is cloned into expression systems (e.g., bacterial, yeast, or mammalian cells) to enable large-scale production. This recombinant approach ensures high purity and consistency, overcoming challenges associated with extracting native AFP2 from low-yield natural sources.
Research on recombinant AFP2 has expanded due to its potential applications. In biomedicine, it is explored for cryopreservation of cells, tissues, and organs, improving viability during freezing and thawing. In the food industry, AFP2 could enhance the texture and shelf life of frozen products. Additionally, its unique properties inspire biomimetic materials for anti-icing surfaces.
Despite its promise, challenges remain, including optimizing expression yields, maintaining functional stability, and addressing cost-effectiveness. Ongoing studies focus on structural modifications to enhance ice-binding efficiency and adapt AFP2 for diverse industrial needs. Overall, recombinant AFP2 represents a bridge between natural adaptation mechanisms and innovative technological solutions in low-temperature environments.
×
