| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRYGS |
| Uniprot No | P22914 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-178aa |
| 氨基酸序列 | SKTGTKITFYEDKNFQGRRYDCDCDCADFHTYLSRCNSIKVEGGTWAVYERPNFAGYMYILPQGEYPEYQRWMGLNDRLSSCRAVHLPSGGQYKIQIFEKGDFSGQMYETTEDCPSIMEQFHMREIHSCKVLEGVWIFYELPNYRGRQYLLDKKEYRKPIDWGAASPAVQSFRRIVE |
| 预测分子量 | 47.9kDa |
| 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 **CRYGS重组蛋白** 的参考文献示例，内容基于模拟学术研究场景构建，实际文献需通过数据库查询获取：
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1. **文献名称**: *Structural Insights into Human γS-Crystallin and Its Cataract-Associated Mutants*
**作者**: Smith A, et al.
**摘要**: 通过重组表达人源CRYGS蛋白，利用X射线晶体学解析其三维结构，并分析白内障相关突变体(如R23T)对蛋白质构象稳定性和聚集倾向的影响，揭示了突变导致晶状体浑浊的分子机制。
2. **文献名称**: *Biophysical Characterization of Recombinant CRYGS under Thermal Stress*
**作者**: Johnson B, et al.
**摘要**: 研究重组CRYGS蛋白在热应激条件下的构象变化，发现其在高温下易形成聚集体，可能与年龄相关性白内障的病理过程相关，并探讨分子伴侣对维持其溶解度的作用。
3. **文献名称**: *Functional Analysis of CRYGS in a Zebrafish Cataract Model*
**作者**: Lee C, et al.
**摘要**: 利用重组CRYGS蛋白在斑马鱼模型中研究其功能，发现CRYGS缺失导致晶状体发育异常，而过表达突变体(如G18V)可诱导类似人类白内障的表型，验证其在晶状体透明度中的关键作用。
4. **文献名称**: *Interaction of γS-Crystallin with αA-Crystallin: Implications for Lens Transparency*
**作者**: Wang D, et al.
**摘要**: 通过体外重组蛋白结合实验，证明CRYGS与αA-晶状体蛋白存在特异性相互作用，αA可抑制CRYGS的热聚集，揭示了二者协同维持晶状体透明性的分子机制。
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**注意**：以上文献为示例，实际研究中请通过 **PubMed、Web of Science** 等平台检索真实文献。建议使用关键词“CRYGS recombinant protein”“γS-crystallin structure/function”等进一步筛选。
CRYGS (Crystallin Gamma S) is a member of the γ-crystallin family, a group of structural proteins predominantly expressed in the vertebrate eye lens. These proteins play a critical role in maintaining lens transparency and refractive index by forming tightly packed, soluble oligomers. Unlike α- and β-crystallins, γ-crystallins are monomeric and highly stable, contributing to the short-range order necessary for lens clarity. CRYGS, specifically, is expressed in the developing and mature lens, with mutations linked to inherited cataracts, highlighting its functional importance.
Recombinant CRYGS protein is produced using biotechnological systems (e.g., bacterial or mammalian expression platforms) to study its structure-function relationships and pathological mechanisms. Its recombinant form allows precise manipulation, enabling researchers to investigate how specific mutations (e.g., those causing protein aggregation or misfolding) disrupt lens homeostasis. This is vital for understanding cataractogenesis, as destabilized crystallins form light-scattering aggregates, a hallmark of cataracts—the leading cause of blindness worldwide.
Structural studies using recombinant CRYGS have revealed its conserved Greek key motif, a β-sandwich fold critical for stability and solubility. However, certain mutations destabilize this architecture, promoting aggregation. Recombinant protein models help screen small molecules or chaperones that could rescue mutant CRYGS function, offering therapeutic avenues. Additionally, CRYGS has been explored beyond ophthalmology; its thermal stability and compact structure make it a candidate for biomaterial engineering.
Despite progress, challenges remain, such as mimicking the lens’s reducing environment in vitro or addressing post-translational modifications. Nonetheless, recombinant CRYGS remains a key tool for dissecting cataract pathology and developing targeted interventions, bridging molecular biology with clinical ophthalmology.
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