| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | T4 |
| Uniprot No | P48230 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-202aa |
| 氨基酸序列 | MCTGGCARCLGGTLIPLAFFGFLANILLFFPGGKVIDDNDHLSQEIWFFGGILGSGVLMIFPALVFLGLKNNDCCGCCGNEGCGKRFAMFTSTIFAVVGFLGAGYSFIISAISINKGPKCLMANSTWGYPFHDGDYLNDEALWNKCREPLNVVPWNLTLFSILLVVGGIQMVLCAIQVVNGLLGTLCGDCQCCGCCGGDGPV |
| 预测分子量 | 21,3 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T4重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*Mechanism of T4 bacteriophage DNA ligase-catalyzed phosphodiester bond formation*
**作者**：Wilson, G.G., Murray, N.E.
**摘要**：该研究系统解析了T4 DNA连接酶的催化机制，阐明其通过三步反应(腺苷酸化、磷酸转移、连接)修复DNA链断裂，强调了酶活性对ATP的依赖性及在DNA重组修复中的关键作用。
2. **文献名称**：*The UvsX protein of bacteriophage T4 catalyzes homologous DNA pairing and strand exchange*
**作者**：Kodadek, T., Alberts, B.M.
**摘要**：本文首次证实T4噬菌体重组蛋白UvsX作为重组酶，能够在体外介导同源DNA配对和链交换反应，揭示了其功能类似于细菌RecA蛋白，为理解噬菌体同源重组机制奠定基础。
3. **文献名称**：*Structural basis for the specificity of T4 DNA ligase in DNA repair and recombination*
**作者**：Sawaya, M.R., et al.
**摘要**：通过X射线晶体学解析T4 DNA连接酶的活性结构，揭示其底物结合口袋的构象变化如何实现对断裂DNA链的特异性识别，解释了该酶在重组修复中的高保真性分子机制。
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以上文献涵盖T4重组蛋白的功能机制、结构解析及关键酶学研究，适用于分子生物学及基因编辑领域参考。如需具体期刊及年份信息可进一步补充。
**Background of T4 Recombinant Proteins**
T4 recombinant proteins are derived from bacteriophage T4. a virus that infects *Escherichia coli*. These proteins are central to the phage’s DNA replication and recombination machinery, enabling efficient genetic exchange and repair. The T4 system has been extensively studied since the mid-20th century, contributing foundational insights into molecular biology, particularly in DNA metabolism and homologous recombination.
Key components include the **T4 UvsX recombinase**, an ATP-dependent enzyme that catalyzes strand exchange during homologous recombination, and **T4 gp32**, a single-stranded DNA-binding protein that stabilizes replication intermediates. These proteins work synergistically to mediate precise DNA pairing and strand invasion, critical for repairing double-strand breaks and integrating exogenous DNA.
In biotechnology, T4 recombinant proteins have been harnessed for *in vitro* applications, such as DNA cloning, mutagenesis, and assembly of large DNA constructs. Their ability to perform **homology-directed repair (HDR)** without requiring restriction enzymes or ligases simplifies complex genetic engineering workflows. For example, the T4 recombination system is integral to methods like "In-Fusion" cloning, enabling seamless assembly of multiple DNA fragments with short homologous overlaps.
Compared to other systems (e.g., λ phage Red), T4 proteins exhibit higher processivity and fidelity, making them advantageous for manipulating large or complex genomes. Recent advancements have expanded their use in synthetic biology, CRISPR-based editing, and high-throughput DNA library construction.
Research continues to optimize these proteins for enhanced efficiency in eukaryotic systems, addressing challenges like ATP dependency and host compatibility. Overall, T4 recombinant proteins remain indispensable tools for both basic research and applied genetic engineering.
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