| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRYGB |
| Uniprot No | P07316 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-175aa |
| 氨基酸序列 | MGKITFYEDRAFQGRSYECTTDCPNLQPYFSRCNSIRVESGCWMIYERPNYQGHQYFLRRGEYPDYQQWMGLSDSIRSCCLIPPHSGAYRMKIYDRDELRGQMSELTDDCISVQDRFHLTEIHSLNVLEGSWILYEMPNYRGRQYLLRPGEYRRFLDWGAPNAKVGSLRRVMDLY |
| 预测分子量 | 24.9 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CRYGB重组蛋白的3篇参考文献示例(注：以下内容为虚构示例，实际文献需通过学术数据库检索确认)：
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1. **文献名称**：*"Recombinant Expression and Biophysical Characterization of Human Crystallin Gamma-B (CRYGB) in a Bacterial System"*
**作者**：Zhang L, et al.
**摘要**：本研究成功在大肠杆菌中表达了重组人源CRYGB蛋白，优化了表达和纯化条件，并通过圆二色谱和动态光散射分析了其二级结构和溶液中的聚集特性，为研究CRYGB的病理机制提供了工具。
2. **文献名称**：*"CRYGB Mutations Disrupt Protein Solubility: Insights from Recombinant Mutant Models"*
**作者**：Kumar S, et al.
**摘要**：通过构建CRYGB致病突变体的重组蛋白，发现某些突变(如R14C)显著降低蛋白溶解度并促进异常聚集，提示其与先天性白内障发病的分子关联。
3. **文献名称**：*"Interactome Profiling of Recombinant CRYGB Reveals Novel Binding Partners in Lens Epithelial Cells"*
**作者**：Wang Y, et al.
**摘要**：利用重组CRYGB蛋白进行免疫共沉淀联合质谱分析，鉴定出多个与CRYGB相互作用的晶状体上皮细胞蛋白，揭示了其在细胞骨架调控中的潜在新功能。
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建议通过**PubMed**或**Web of Science**以关键词“CRYGB recombinant”检索真实文献。如需具体文献协助，请提供更多上下文。
CRYGB (β-crystallin B2) is a member of the βγ-crystallin superfamily, primarily expressed in the vertebrate eye lens. These crystallins are essential structural proteins that maintain lens transparency and refractive properties by forming tightly packed, soluble oligomers. CRYGB, encoded by the *CRYGB* gene on chromosome 2 in humans, contributes to short-range ordered lattice arrangements critical for optical clarity. Mutations in CRYGB are linked to congenital cataracts, highlighting its role in lens homeostasis.
Recombinant CRYGB protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional protein for research. Its recombinant form enables studies on structural dynamics, aggregation mechanisms, and disease-related variants. Researchers utilize it to probe cataractogenesis—particularly how missense mutations disrupt protein folding, solubility, or interactions with other crystallins (e.g., αA-crystallin). Such insights aid in modeling cataract pathology and screening potential therapeutic compounds.
Beyond ophthalmology, CRYGB’s βγ-crystallin domain shares evolutionary ties with microbial stress-response proteins, making it a model for studying protein stability and misfolding diseases. Recombinant CRYGB also serves in biophysical assays (e.g., X-ray crystallography, NMR) to resolve its tertiary structure and calcium-binding motifs, which may influence lens elasticity and aging. Recent work explores its potential in bioengineering, such as designing thermo-stable scaffolds for drug delivery. However, challenges persist in mimicking its native post-translational modifications *in vitro*, necessitating advanced expression systems. Overall, recombinant CRYGB bridges basic lens biology and translational applications in vision disorders.
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