| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRYBB1 |
| Uniprot No | P53674 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-252aa |
| 氨基酸序列 | SQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE GSFPVLATEP PK |
| 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3篇关于CRYBB1重组蛋白的文献信息概要：
1. **文献名称**：Expression and Purification of Recombinant Human CRYBB1 in Escherichia coli
**作者**：Smith J, et al.
**摘要**：研究报道了利用大肠杆菌表达系统成功克隆和纯化人源CRYBB1重组蛋白，通过His标签亲和层析获得高纯度蛋白，并验证其结构完整性，为后续功能研究奠定基础。
2. **文献名称**：Crystallin Beta B1 Mutation Alters Protein Stability in Congenital Cataracts
**作者**：Chen L, et al.
**摘要**：通过构建CRYBB1突变体重组蛋白(如R58H)，发现突变导致蛋白热稳定性下降和聚集倾向增加，揭示了特定氨基酸替换在先天性白内障发病中的分子机制。
3. **文献名称**：Biophysical Characterization of Recombinant CRYBB1 and Its Interaction with Lens Membrane Lipids
**作者**：Wang Y, et al.
**摘要**：利用圆二色谱和表面等离子共振技术分析重组CRYBB1的二级结构及与晶状体膜脂质的相互作用，发现其β-折叠构象在维持晶状体透明度中的关键作用。
注：以上文献信息为基于研究领域常见主题的模拟概括，实际文献需通过PubMed/Google Scholar等平台检索确认。建议补充关键词"recombinant CRYBB1 protein"+"cataract"+"mutant"进行精准查找。
CRYBB1 (beta-crystallin B1) is a member of the βγ-crystallin superfamily, predominantly expressed in the eye lens, where it contributes to lens transparency and refractive properties. As a structural protein, CRYBB1 plays a critical role in maintaining lens integrity by forming soluble oligomers with other crystallins. Mutations in the CRYBB1 gene are associated with congenital cataracts, highlighting its importance in lens development and homeostasis.
Recombinant CRYBB1 protein is engineered using expression systems (e.g., E. coli or mammalian cells) to produce the protein in vitro for functional studies. The recombinant form typically retains key structural features, including two conserved β-sheet "Greek key" motifs that mediate protein-protein interactions and stability. Researchers utilize CRYBB1 recombinant proteins to investigate cataract pathogenesis, particularly how mutations disrupt protein folding, solubility, or interactions. These studies often involve biophysical analyses (e.g., spectroscopy, X-ray crystallography) to assess aggregation propensity or thermal stability.
Beyond disease modeling, recombinant CRYBB1 serves as a tool for exploring lens regeneration mechanisms and age-related crystallin modifications. Its biochemical properties also make it relevant in biomaterials research for designing synthetic polymers mimicking lens transparency. Current therapeutic strategies aim to stabilize mutant CRYBB1 or prevent aggregation using chaperone molecules, with recombinant proteins enabling high-throughput drug screening. Despite progress, challenges remain in replicating native post-translational modifications and oligomerization states in vitro, underscoring the need for advanced expression systems to bridge structural and functional insights.
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