| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRYAB |
| Uniprot No | P02511 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-175aa |
| 氨基酸序列 | MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK |
| 预测分子量 | 36.2kDa |
| 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3篇关于CRYAB重组蛋白的参考文献及其摘要概括：
1. **《Recombinant αB-crystallin protects cells against oxidative stress-induced apoptosis》**
- 作者：Liu, S., Li, J., & Wang, C.
- 摘要：研究报道了通过大肠杆菌表达系统成功制备重组CRYAB蛋白，并验证其通过抑制ROS积累和线粒体途径凋亡，减轻氧化应激诱导的细胞损伤，为神经退行性疾病治疗提供潜在策略。
2. **《Expression and chaperone-like activity of human αB-crystallin in E. coli》**
- 作者：Bhattacharyya, J., & Srinivas, V.
- 摘要：通过优化表达条件实现人源CRYAB蛋白的高效可溶性表达，证明其具有热稳定性和分子伴侣功能，能在体外抑制热诱导的酶聚集，为白内障机制研究奠定基础。
3. **《Recombinant αB-crystallin reduces inflammation in experimental autoimmune myocarditis》**
- 作者：Morrison, L.E., et al.
- 摘要：在小鼠心肌炎模型中，注射重组CRYAB蛋白显著降低促炎细胞因子(如TNF-α、IL-6)水平，抑制心肌组织炎性浸润，提示其免疫调节功能及心血管疾病治疗潜力。
注：以上文献信息为模拟示例，实际引用需以具体论文数据为准。建议通过PubMed或Web of Science检索最新研究。
**Background of CRYAB Recombinant Protein**
CRYAB (αB-Crystallin), a member of the small heat shock protein (sHSP) family, is a multifunctional molecular chaperone encoded by the *CRYAB* gene. It plays a critical role in maintaining cellular homeostasis by preventing the aggregation of misfolded proteins under stress conditions, such as heat, oxidative stress, or ischemia. Structurally, CRYAB forms large oligomeric complexes that interact with partially unfolded proteins, stabilizing cellular structures and promoting cell survival. It is highly expressed in the lens of the eye, where it contributes to transparency and refractive properties, but is also found in non-ocular tissues, including cardiac and skeletal muscle, highlighting its systemic importance.
Mutations in *CRYAB* are linked to human pathologies, such as cataracts, cardiomyopathies, and neurodegenerative diseases. Recombinant CRYAB protein, produced via bacterial or mammalian expression systems, retains these chaperone functions and is widely used in research to study protein misfolding disorders, including Alzheimer’s disease and ALS. Its therapeutic potential is being explored for conditions involving cellular stress, inflammation, or apoptosis. For instance, recombinant CRYAB demonstrates anti-inflammatory and anti-apoptotic effects in models of ischemic injury and autoimmune diseases.
In cancer biology, CRYAB exhibits dual roles, either suppressing tumor progression by stabilizing oncoprotein clients or promoting metastasis through pro-survival signaling. This complexity underscores the need for context-specific studies. Recombinant CRYAB also serves as a tool for structural studies to dissect its oligomerization dynamics and substrate-binding mechanisms. Despite challenges in delivery and stability, its versatility positions it as a promising candidate for biomedical applications, bridging fundamental research and therapeutic innovation. Ongoing studies aim to optimize its production and elucidate its pleiotropic roles in health and disease.
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