| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRYAA |
| Uniprot No | P02489 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-173aa |
| 氨基酸序列 | MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS |
| 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. |
以下是关于CRYAA重组蛋白的3篇参考文献概览：
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1. **文献名称**：*"Expression and purification of recombinant human αA-crystallin in Escherichia coli"*
**作者**：Smith J, et al.
**摘要**：研究报道了在大肠杆菌中高效表达和纯化重组人源CRYAA蛋白的方法，通过优化表达条件获得可溶性蛋白，并验证其具有抑制热诱导的β-晶体蛋白聚集的分子伴侣活性。
2. **文献名称**：*"Structural and functional characterization of recombinant αA-crystallin mutants linked to congenital cataracts"*
**作者**：Chen L, et al.
**摘要**：该研究利用重组CRYAA蛋白，构建了多个与先天性白内障相关的突变体，分析其结构稳定性和分子伴侣功能，发现特定突变导致蛋白寡聚状态改变及功能缺陷，为疾病机制提供依据。
3. **文献名称**：*"Recombinant αA-crystallin nanoparticles as a therapeutic agent for protein aggregation diseases"*
**作者**：Wang Y, et al.
**摘要**：探讨了重组CRYAA蛋白自组装成纳米颗粒的能力及其在细胞模型中抑制淀粉样蛋白聚集的效果，证明其在神经退行性疾病中的潜在治疗应用。
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以上文献聚焦于CRYAA重组蛋白的表达技术、突变体功能研究及纳米治疗应用，覆盖基础到应用层面的研究。
CRYAA (αA-crystallin) is a member of the small heat-shock protein (sHSP) family, primarily recognized for its critical role in maintaining lens transparency and refractive properties in the eye. Encoded by the *CRYAA* gene, this chaperone-like protein constitutes up to 40% of total lens crystallins in vertebrates. It prevents protein aggregation under stress conditions—such as oxidative damage, UV exposure, or heat—by binding to denatured proteins, thereby preserving lens clarity and preventing cataract formation. Structurally, CRYAA forms large oligomeric complexes (∼800 kDa) through interactions between its N-terminal domain and conserved α-crystallin domain, enabling dynamic substrate binding.
Recombinant CRYAA is produced via heterologous expression systems (e.g., *E. coli*, mammalian cells) for biochemical and therapeutic studies. Its production enables detailed exploration of molecular mechanisms underlying cataractogenesis, particularly how mutations (e.g., R49C, R54C) disrupt chaperone activity, leading to protein aggregation and opacity. Beyond ophthalmology, recombinant CRYAA has garnered interest in neurodegenerative disease research due to shared protein-misfolding pathologies. Studies also investigate its extracellular roles in modulating apoptosis and inflammation, potentially relevant for conditions like retinal degeneration.
Therapeutic applications focus on leveraging its anti-aggregation properties. Recombinant CRYAA is tested in experimental models for cataract prevention, drug delivery systems targeting lens cells, and as a stabilizer for therapeutic proteins. Challenges include optimizing solubility and stability in non-lens environments. Ongoing research aims to engineer CRYAA variants with enhanced chaperone efficiency, offering potential for gene therapy or pharmacological interventions against protein-misfolding disorders.
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