| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRYBA2 |
| Uniprot No | P53672 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-197aa |
| 氨基酸序列 | MSSAPAPGPAPASLTLWDEEDFQGRRCRLLSDCANVCERGGLPRVRSVKVENGVWVAFEYPDFQGQQFILEKGDYPRWSAWSGSSSHNSNQLLSFRPVLCANHNDSRVTLFEGDNFQGCKFDLVDDYPSLPSMGWASKDVGSLKVSSGAWVAYQYPGYRGYQYVLERDRHSGEFCTYGELGTQAHTGQLQSIRRVQH |
| 分子量 | 47.3 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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3条关于重组人CRYBA2蛋白的模拟参考文献示例(内容为虚拟合成，仅供格式参考)：
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1. **文献名称**: Expression and characterization of recombinant human βA2-crystallin in Escherichia coli
**作者**: Smith J, et al.
**摘要**: 研究报道了在大肠杆菌中成功表达并纯化重组人CRYBA2蛋白。通过圆二色谱和动态光散射分析，证实其二级结构完整且呈寡聚态，为研究其在晶状体中的稳定性提供了基础。
2. **文献名称**: CRYBA2 mutation screening in congenital cataracts and structural analysis of mutant protein
**作者**: Wang L, et al.
**摘要**: 本研究在先天性白内障患者中发现CRYBA2基因突变，通过重组表达突变体蛋白发现其异常聚集倾向，提示突变可能通过破坏蛋白溶解度导致晶状体浑浊。
3. **文献名称**: Interaction of βA2-crystallin with αA-crystallin in lens transparency maintenance
**作者**: Gupta R, et al.
**摘要**: 利用重组CRYBA2和αA-晶体蛋白进行体外结合实验，证实两者通过疏水相互作用形成复合物，阐明了CRYBA2依赖伴侣蛋白维持晶状体透明性的分子机制。
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**说明**：以上文献为模拟生成，实际研究需检索PubMed/Google Scholar等数据库(关键词：recombinant CRYBA2、βA2-crystallin)。真实研究多聚焦于蛋白结构解析、白内障相关突变及分子伴侣互作领域。
Human βA2-crystallin (CRYBA2) is a member of the βγ-crystallin superfamily, primarily expressed in the ocular lens. It plays a critical role in maintaining lens transparency and refractive function by forming structural proteins that ensure long-term stability of lens fiber cells. Encoded by the *CRYBA2* gene, this protein contributes to the assembly of crystallin heteromers, which prevent protein aggregation under physiological stress. Mutations in *CRYBA2* are associated with congenital cataracts, highlighting its importance in lens homeostasis.
Recombinant human CRYBA2 is produced via genetic engineering, typically using bacterial or mammalian expression systems. Its recombinant form enables detailed study of molecular mechanisms underlying cataractogenesis, including misfolding, solubility loss, and intracellular aggregation. Researchers employ it to investigate structural dynamics, thermal stability, and interactions with other crystallins or chaperones. Beyond cataract research, CRYBA2 has potential applications in developing therapeutic strategies (e.g., protein stabilization agents or gene therapies) and in vitro models for drug screening.
Studies also explore its non-lens roles, such as in retinal development and neurological tissues, though these remain less characterized. Recombinant CRYBA2 serves as a vital tool for unraveling both physiological and pathological pathways linked to crystallin dysfunction.
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