| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRYGN |
| Uniprot No | Q8WXF5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-182aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMAQRSG KITLYEGKHF TGQKLEVFGD CDNFQDRGFM NRVNSIHVES GAWVCFNHPD FRGQQFILEH GDYPDFFRWN SHSDHMGSCR PVGMHGEHFR LEIFEGCNFT GQCLEFLEDS PFLQSRGWVK NCVNTIKVYG DGAAWSPRSF GAEDFQLSSS LQSDQGPEEA TTKPATTQPP FLTANL |
| 预测分子量 | 23 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. |
以下为模拟生成的关于CRYGN重组蛋白的参考文献示例(非真实文献，仅供格式参考)：
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1. **标题**: *Recombinant Expression and Purification of Human CRYGN in E. coli*
**作者**: Zhang L., et al.
**摘要**: 本研究利用大肠杆菌表达系统成功克隆并表达了人源CRYGN重组蛋白，通过His标签亲和层析纯化获得高纯度蛋白，并验证其二级结构稳定性，为后续功能研究提供基础。
2. **标题**: *CRYGN's Role in Cellular Oxidative Stress Response: Structural Insights*
**作者**: Patel R., Kim H.
**摘要**: 通过X射线晶体学解析CRYGN重组蛋白的三维结构，发现其与硫氧还蛋白存在相互作用，实验表明CRYGN可能通过调节氧化还原通路保护细胞免受ROS损伤。
3. **标题**: *CRYGN Recombinant Protein Attenuates Cataract Formation in Mouse Models*
**作者**: Gomez S., et al.
**摘要**: 在遗传性白内障小鼠模型中，注射重组CRYGN蛋白显著延缓晶状体浑浊进程，提示其潜在治疗价值。研究采用哺乳动物细胞表达系统获得功能性CRYGN。
4. **标题**: *CRYGN Interaction Network Analysis via Yeast Two-Hybrid Screening*
**作者**: Watanabe T., et al.
**摘要**: 利用酵母双杂交技术筛选CRYGN重组蛋白的相互作用蛋白，鉴定出多个与细胞凋亡和自噬相关的靶点，为揭示其在眼部疾病中的分子机制提供线索。
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**提示**：以上内容为模拟生成，实际文献请通过PubMed、Web of Science或专业数据库检索。
CRYGN, also known as gammaN-crystallin, is a member of the crystallin protein family predominantly expressed in the vertebrate eye lens. Crystallins are essential for maintaining lens transparency and refractive index, critical for focusing light onto the retina. Among crystallins, γ-crystallins (including CRYGN) are small, stable structural proteins enriched in the lens nucleus, contributing to its high refractive power and long-term durability.
The CRYGN gene encodes a β-sheet-rich protein with a molecular weight of approximately 20-25 kDa. Its structure includes two conserved Greek key motifs, a hallmark of crystallins, which facilitate tight packing and resistance to denaturation. While primarily lens-specific, low levels of CRYGN expression have been detected in non-ocular tissues, though its role there remains unclear.
Recombinant CRYGN refers to the protein produced via genetic engineering techniques, typically using bacterial (e.g., E. coli) or mammalian expression systems. This allows large-scale production for research and therapeutic applications. Recombinant CRYGN retains the biophysical properties of native protein, including solubility, stability, and light-scattering minimization, making it valuable for studying lens biology and cataract formation. Mutations in crystallins, including CRYGN, are linked to congenital cataracts, a leading cause of childhood blindness. Recombinant CRYGN enables in vitro analysis of such mutations, aiding in understanding disease mechanisms.
Beyond ophthalmology, recombinant CRYGN has potential in biotechnology due to its stability and compact structure. It serves as a model for designing engineered proteins with enhanced thermal or chemical resistance. Ongoing research explores its role in cellular stress responses and extracellular matrix interactions, broadening its relevance in biomedicine.
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