| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRYZ |
| Uniprot No | Q08257 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-329aa |
| 氨基酸序列 | ATGQKLMRA VRVFEFGGPE VLKLRSDIAV PIPKDHQVLI KVHACGVNPV ETYIRSGTYS RKPLLPYTPG SDVAGVIEAV GDNASAFKKG DRVFTSSTIS GGYAEYALAA DHTVYKLPEK LDFKQGAAIG IPYFTAYRAL IHSACVKAGE SVLVHGASGG VGLAACQIAR AYGLKILGTA GTEEGQKIVL QNGAHEVFNH REVNYIDKIK KYVGEKGIDI IIEMLANVNL SKDLSLLSHG GRVIVVGSRG TIEINPRDTM AKESSIIGVT LFSSTKEEFQ QYAAALQAGM EIGWLKPVIG SQYPLEKVAE AHENIIHGSG ATGKMILLL |
| 预测分子量 | 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. |
以下为基于CRYZ重组蛋白研究领域常见方向的模拟参考文献示例(建议通过学术数据库验证具体文献)：
1. **《Recombinant Human ζ-Crystallin: Expression in E. coli and Enzymatic Characterization》**
- 作者：Smith J, et al.
- 摘要：研究通过大肠杆菌系统表达CRYZ重组蛋白，优化纯化条件并分析其NADPH依赖的酮还原酶活性，证实其在类固醇代谢中的潜在作用。
2. **《Structural Insights into CRYZ’s Role in Cataract Formation via X-ray Crystallography》**
- 作者：Li X, Wang Y.
- 摘要：解析CRYZ重组蛋白的晶体结构，揭示其与氧化应激中谷胱甘肽结合的分子机制，为白内障发病机制提供结构依据。
3. **《CRYZ Recombinant Protein Attenuates Neuroinflammation in a Mouse Model of Alzheimer’s Disease》**
- 作者：Chen R, et al.
- 摘要：在小鼠模型中验证CRYZ重组蛋白通过抑制NF-κB通路减轻神经炎症，提示其在神经退行性疾病治疗中的潜力。
4. **《Functional Rescue of CRYZ Mutation by Recombinant Gene Therapy in Zebrafish》**
- 作者：Garcia M, et al.
- 摘要：利用重组CRYZ蛋白在斑马鱼模型中纠正基因突变导致的视网膜变性，为遗传性眼病治疗提供新策略。
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**注意**：以上文献名为示例性概括，实际研究需检索PubMed、Web of Science等平台(可尝试关键词："recombinant CRYZ protein"、"zeta-crystallin expression")。如需具体文献协助，请提供更详细的研究方向。
CRYZ (zeta-crystallin) is a member of the crystallin protein family, initially identified for its structural role in maintaining lens transparency in the eye. However, unlike α- and β-crystallins primarily associated with ocular function, CRYZ exhibits dual roles as both a structural protein and a metabolic enzyme. It functions as a quinone oxidoreductase, catalyzing NADPH-dependent reductions of quinones and other carbonyl compounds, implicating it in cellular detoxification and antioxidant defense pathways. This enzymatic activity extends its biological relevance beyond the lens, with expression observed in the liver, kidney, and brain.
Recombinant CRYZ protein is engineered using genetic cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems to ensure proper folding and post-translational modifications. Its recombinant form retains enzymatic activity, enabling studies on substrate specificity, catalytic mechanisms, and interactions with cofactors. Researchers leverage recombinant CRYZ to explore its role in metabolic disorders, neurodegenerative diseases, and age-related cataracts. For instance, CRYZ deficiency has been linked to impaired redox homeostasis in diabetes, while its neuroprotective potential in Parkinson’s disease models is under investigation.
Pharmaceutically, CRYZ is studied as a therapeutic target or biomarker due to its involvement in oxidative stress pathways. Structural analyses of recombinant CRYZ provide insights into ligand binding sites, guiding drug design for conditions like cancer or mitochondrial dysfunction. Its unique combination of structural stability and enzymatic versatility makes it a valuable tool for both basic research and translational applications, bridging gaps between crystallin biology and metabolic disease mechanisms.
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