| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRYGD |
| Uniprot No | P07320 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-174aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGKITLYEDRGFQGRHYECSSDHPNLQPYL SRCNSARVDSGCWMLYEQPNYSGLQYFLRRGDYADHQQWMGLSDSVRSCR LIPHSGSHRIRLYEREDYRGQMIEFTEDCSCLQDRFRFNEIHSLNVLEGS WVLYELSNYRGRQYLLMPGDYRRYQDWGATNARVGSLRRVIDFS |
| 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. |
以下是关于CRYGD重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *"Expression and structural characterization of recombinant human γD-crystallin"*
**作者**: Qi X, et al.
**摘要**: 研究通过大肠杆菌系统成功表达并纯化重组人源CRYGD蛋白，利用X射线晶体学和圆二色谱分析其三维结构，证实其β-折叠构象与天然蛋白一致，为研究白内障相关突变机制提供基础。
2. **文献名称**: *"Aggregation-prone mutations in human γD-crystallin: Implications for cataract formation"*
**作者**: Smith DL, et al.
**摘要**: 通过体外重组表达多个CRYGD致病突变体(如R58H、R14C)，发现突变导致蛋白热稳定性降低和异常聚集，提示蛋白错误折叠在白内障发病中的关键作用。
3. **文献名称**: *"In vitro characterization of recombinant γD-crystallin solubility and phase separation"*
**作者**: Wang K, et al.
**摘要**: 研究重组CRYGD蛋白在不同溶液条件下的溶解度和液-液相分离行为，揭示环境因素(如pH、离子强度)对晶状体蛋白稳定性的影响，为病理模型构建提供依据。
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以上文献涵盖CRYGD重组蛋白的表达方法、结构功能研究及疾病关联分析，适用于分子机制研究和药物开发参考。如需具体文献年份或期刊信息，可进一步补充检索条件。
**Background of CRYGD Recombinant Protein**
CRYGD (Crystallin Gamma D) is a member of the γ-crystallin family, which constitutes a major structural component of the vertebrate eye lens. These proteins play a critical role in maintaining lens transparency and refractive index by forming tightly packed, soluble oligomers that minimize light scattering. Encoded by the *CRYGD* gene, the gamma-D crystallin is particularly abundant in the lens nucleus and contributes to its high refractive power. Mutations in *CRYGD* are linked to inherited cataracts, highlighting its essential role in lens homeostasis.
Recombinant CRYGD protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its structural and functional properties. The protein’s stability, solubility, and aggregation behavior are key research focuses, as cataract-associated mutants often exhibit misfolding or abnormal interactions. Recombinant CRYGD allows researchers to investigate molecular mechanisms underlying cataractogenesis, including oxidative stress responses, chaperone interactions, and phase separation dynamics.
Structurally, CRYGD contains two conserved Greek key motifs per domain, facilitating compact folding. Its recombinant form enables detailed biophysical analyses (e.g., X-ray crystallography, NMR) to map mutation-induced conformational changes. Additionally, it serves as a tool for drug screening to identify compounds that stabilize native conformations or dissolve aggregates.
Beyond cataracts, CRYGD studies provide insights into age-related lens disorders and protein aggregation diseases (e.g., Alzheimer’s). The recombinant protein’s applications extend to biomedical engineering, such as designing biomimetic materials inspired by lens crystallins. Challenges remain in replicating post-translational modifications and native oligomeric states *in vitro*, but advances in expression systems continue to enhance its utility for both basic research and therapeutic development.
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