| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | CRYgF |
| Uniprot No | Q9CXV3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-174aa |
| 氨基酸序列 | MGKITFYEDR SFQGRHYECS TDHSNLQPYF SRCNSVRVDS GCWMLYEQPN FAGCQYFLRR GDYPDYQQWM GFSDSVRSCH LIPHSTSHRI RIYEREDYRG QMVEITDDCS HLQDRFHFSD FHSFHVMEGY WVLYEMPNYR GRQYLLRPGE YRRYHDWGAM NARVGSLRRI MDFY |
| 预测分子量 | 21,2 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CRYgF重组蛋白的3篇模拟参考文献及摘要概括：
---
1. **文献名称**：*Structural Stability and Aggregation of Recombinant CRYgF in Cataract Pathogenesis*
**作者**：Zhang, Y. et al. (2018)
**摘要**：本研究通过大肠杆菌系统重组表达人源CRYgF蛋白，分析了其突变体(如W43R)在溶液中的聚集行为。结果表明，突变导致CRYgF的β-折叠结构破坏，在模拟老化条件下(高温、氧化应激)易形成不溶性聚集体，可能与先天性白内障的发生密切相关。
---
2. **文献名称**：*Optimization of CRYgF Recombinant Expression in Prokaryotic Systems*
**作者**：Lee, S. et al. (2019)
**摘要**：通过比较不同表达载体(如pET系列)和诱导条件，优化了CRYgF在大肠杆菌中的可溶性表达。研究显示，低温诱导(18℃)结合分子伴侣共表达显著提高蛋白产量，并通过圆二色谱验证重组蛋白具有天然构象，为后续功能研究奠定基础。
---
3. **文献名称**：*CRYgF Recombinant Protein as a Nanocarrier for Drug Delivery*
**作者**：Chen, H. et al. (2021)
**摘要**：利用重组CRYgF的自组装特性，开发了一种新型药物递送系统。实验证明，CRYgF在生理条件下可形成均一纳米颗粒，负载抗炎药物后能靶向穿透眼部屏障，为晶状体相关疾病的局部治疗提供了潜在策略。
---
注：以上文献为模拟示例，实际研究中需检索具体数据库(如PubMed)获取真实参考文献。
**Background of CRYgF Recombinant Protein**
CRYgF, a recombinant protein derived from the γ-crystallin family, plays a critical role in maintaining lens transparency and refractive properties in the eye. γ-Crystallins are structural proteins predominantly expressed in the vertebrate eye lens, contributing to its optical clarity and elasticity. Among these, CRYgF (Gamma-F Crystallin) is notable for its high solubility and stability, which are essential for preventing protein aggregation—a key factor in cataract formation.
The recombinant CRYgF protein is engineered using advanced molecular cloning techniques, often expressed in *E. coli* or mammalian cell systems to ensure proper folding and post-translational modifications. Its production enables researchers to study lens biology, protein misfolding diseases, and mechanisms underlying cataractogenesis. Additionally, CRYgF serves as a model for investigating molecular interactions that stabilize proteins under physiological stress, such as oxidative damage or UV exposure.
Beyond ophthalmology, CRYgF has applications in biotechnology, including drug delivery systems and nanotechnology, owing to its compact structure and resistance to denaturation. Studies also explore its potential in regenerative medicine, particularly in lens regeneration therapies. However, challenges remain in optimizing its production yield and functional consistency for clinical use.
Overall, CRYgF recombinant protein bridges fundamental research and therapeutic innovation, offering insights into both ocular pathologies and protein engineering strategies. Its study underscores the importance of crystallins in cellular homeostasis and disease, highlighting opportunities for targeted interventions in age-related and genetic eye disorders.
×
