纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | CRYBA4 |
Uniprot No | P53673 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-196aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMTLQCTKSAGPWKMVVWDEDGFQGRRHEFT AECPSVLELGFETVRSLKVLSGAWVGFEHAGFQGQQYILERGEYPSWDAW GGNTAYPAERLTSFRPAACANHRDSRLTIFEQENFLGKKGELSDDYPSLQ AMGWEGNEVGSFHVHSGAWVCSQFPGYRGFQYVLECDHHSGDYKHFREWG SHAPTFQVQSIRRIQQ |
预测分子量 | 25 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CRYBA4重组蛋白的3篇模拟参考文献(基于常见研究主题构建):
1. **《重组人CRYBA4蛋白在大肠杆菌中的高效表达与纯化》**
- 作者:Li, X., Wang, Y., & Chen, J.
- 摘要:本研究成功构建了CRYBA4基因的重组质粒,并利用大肠杆菌表达系统实现高效可溶性表达。通过亲和层析技术纯化获得高纯度蛋白,经圆二色谱分析证实其具有正确的β-折叠结构,为后续功能研究奠定基础。
2. **《CRYBA4突变体重组蛋白的稳定性及其在白内障发生中的作用》**
- 作者:Smith, A.R., Johnson, B., & Kumar, S.
- 摘要:通过体外模拟CRYBA4常见致病突变(如R21C),发现突变体重组蛋白的热稳定性和溶解度显著降低。细胞实验表明突变体易形成聚集体,提示其可能通过破坏晶状体纤维细胞稳态导致先天性白内障。
3. **《CRYBA4/CRYBA1重组蛋白复合物的体外组装与分子互作研究》**
- 作者:Zhang, H., Liu, T., & Wang, F.
- 摘要:利用重组表达的CRYBA4和CRYBA1蛋白,证实两者在体外可自发形成异源二聚体。表面等离子共振(SPR)分析显示结合亲和力达nM级别,揭示了β-晶状体蛋白家族成员间的协同作用机制。
(注:以上文献为示例性内容,实际研究需查询具体数据库。)
**Background of CRYBA4 Recombinant Protein**
CRYBA4 (βA4-crystallin) is a member of the βγ-crystallin superfamily, primarily expressed in the ocular lens, where it contributes to lens transparency and refractive properties. As a structural protein, CRYBA4 plays a critical role in maintaining lens integrity by stabilizing cellular proteins and preventing aggregation, which is essential for proper light transmission. Mutations in the *CRYBA4* gene have been linked to congenital cataracts and other lens disorders, underscoring its importance in ocular health.
Recombinant CRYBA4 protein is produced using biotechnological methods, such as expression in *E. coli* or mammalian cell systems, enabling controlled production of the purified protein for research. This engineered protein retains the functional domains of native CRYBA4. including its Greek key motifs, which facilitate structural stability and interactions with other crystallins. Researchers utilize recombinant CRYBA4 to study its biophysical properties, folding mechanisms, and role in cataractogenesis.
Studies involving CRYBA4 recombinant protein have advanced understanding of lens pathophysiology, particularly in modeling how mutations disrupt protein solubility and promote aggregation—a hallmark of cataract formation. Additionally, it serves as a tool for screening potential therapeutic compounds aimed at preventing or reversing crystallin aggregation. Beyond ophthalmology, CRYBA4 has been explored in non-ocular tissues, suggesting broader roles in cellular stress response and apoptosis regulation.
Overall, CRYBA4 recombinant protein is a vital resource for deciphering molecular mechanisms of lens-related diseases and developing targeted interventions, bridging structural biology with clinical applications.
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