| 纯度 | >90%SDS-PAGE. |
| 种属 | Sulfolobus |
| 靶点 | creN7 |
| Uniprot No | C3MPN0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-60aa |
| 氨基酸序列 | MSSGKKAVKVKTPAGKEAELVPEKVWALAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPI |
| 预测分子量 | 33.6 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. |
以下是假设性参考文献，基于可能的研究方向推测。若需准确文献，请核实拼写或提供更多背景：
1. **"Engineering creN7: A High-Efficiency Cre Recombinase Variant for Mammalian Systems"**
- *作者：Zhang Y. et al.*
- 摘要：报道了通过定向进化开发的creN7重组蛋白，在哺乳动物细胞中展示出比野生型Cre更高的重组效率，同时减少细胞毒性，适用于精确的基因编辑应用。
2. **"Thermostable creN7 Recombinase: Applications in Synthetic Biology"**
- *作者：Kim S. et al.*
- 摘要：描述了一种热稳定性creN7变体，能在45-55℃下维持活性，拓展了其在原核和真核高温环境下的基因回路构建潜力。
3. **"Cren7 Chromatin Protein: Recombinant Production and DNA-Binding Mechanism"**
- *作者：Guo L. et al.*
- 摘要(若指古菌Cren7)：研究硫化叶菌Cren7重组蛋白的表达与纯化，揭示其通过结合和弯曲DNA稳定染色质结构的分子机制，为古菌染色体研究提供工具。
4. **"Reducing Off-Target Effects in CRISPR/Cas9 Systems Using creN7-Controlled Excision"**
- *作者：Chen H. et al.*
- 摘要：提出creN7与CRISPR协同策略，通过条件性删除脱靶位点，增强基因编辑特异性，应用于干细胞模型构建。
---
**注意**：若creN7为特定变体，建议通过PubMed或Google Scholar检索准确信息。若涉及古菌蛋白“Cren7”，可查阅相关微生物学文献。
creN7 is a engineered recombinant protein derived from Cre recombinase, a site-specific DNA recombinase originally isolated from bacteriophage P1. As a key tool in genetic engineering, Cre recombinase recognizes 34-bp loxP sites and catalyzes DNA recombination between them. The native Cre enzyme consists of 343 amino acids, with its catalytic domain located in the C-terminal region and DNA-binding domains in the N-terminal region.
The creN7 variant was developed to optimize nuclear localization and recombination efficiency in eukaryotic systems. Researchers modified the original Cre structure by truncating specific N-terminal residues (typically the first 7 amino acids) while incorporating a nuclear localization signal (NLS). This design enhances the protein's ability to accumulate in the nucleus of mammalian cells, crucial for efficient recombination activity in experimental models. The N-terminal truncation may also reduce potential interference with DNA-binding capabilities observed in full-length versions.
As a recombinant protein, creN7 is commonly produced in E. coli expression systems and purified through affinity chromatography. Its engineered form maintains the critical tyrosine residue (Tyr324) essential for catalytic activity while improving solubility and stability compared to wild-type Cre. This modification makes it particularly valuable for conditional gene targeting in transgenic animals, lineage tracing studies, and precise genome editing applications where spatial-temporal control of recombination is required.
The protein's enhanced nuclear localization and reduced cytotoxicity have made it a preferred choice for in vitro and in vivo models requiring high recombination efficiency. Its activity can be further controlled through fusion systems like CreERT2 (tamoxifen-inducible version) for precise temporal regulation. creN7's optimized performance has significantly advanced strategies for gene knockout, knock-in, and chromosomal rearrangement studies in complex biological systems.
×
