| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NHEJ1 |
| Uniprot No | Q9H9Q4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-224aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMEELEQG LLMQPWAWLQ LAENSLLAKV FITKQGYALL VSDLQQVWHE QVDTSVVSQR AKELNKRLTA PPAAFLCHLD NLLRPLLKDA AHPSEATFSC DCVADALILR VRSELSGLPF YWNFHCMLAS PSLVSQHLIR PLMGMSLALQ CQVRELATLL HMKDLEIQDY QESGATLIRD RLKTEPFEEN SFLEQFMIEK LPEACSIGDG KPFVMNLQDL YMAVTTQ |
| 预测分子量 | 28 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NHEJ1(即XLF/Cernunnos)重组蛋白的3篇经典参考文献，简要整理如下：
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1. **文献名称**：*Cernunnos, a Novel Nonhomologous End-Joining Factor, Is Mutated in Human Immunodeficiency with Microcephaly*
**作者**：Buck, D. 等
**摘要**：本研究首次将NHEJ1(命名为Cernunnos)基因突变与人类严重免疫缺陷及小头症联系起来，证明其参与V(D)J重组和DNA双链断裂修复，是NHEJ通路的关键因子。
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2. **文献名称**：*XLF Interacts with the XRCC4-DNA Ligase IV Complex to Promote DNA Nonhomologous End-Joining*
**作者**：Ahnesorg, P. 等
**摘要**：该研究发现XLF(即NHEJ1)与XRCC4-连接酶IV复合物直接相互作用，增强DNA末端连接活性，尤其在修复辐射诱导的DNA损伤中起核心作用，并解释了其缺陷导致的免疫系统异常。
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3. **文献名称**：*XRCC4 and XLF Form an Extended Grooved Scaffold for DNA Ligation and V(D)J Recombination*
**作者**：Mahaney, B.L. 等
**摘要**：通过结构生物学分析，揭示了XRCC4与XLF(NHEJ1)形成螺旋复合物，为DNA连接酶IV提供结合平台，促进DNA末端对齐和连接，阐明了其在V(D)J重组中的分子机制。
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这些研究共同阐明了NHEJ1在DNA修复和免疫系统中的功能，为理解相关疾病提供了分子基础。
Non-homologous end joining 1 (NHEJ1), also known as XLF (XRCC4-like factor) or Cernunnos, is a critical protein involved in the non-homologous end joining (NHEJ) pathway, the primary DNA repair mechanism for double-strand breaks (DSBs) in higher eukaryotes. Discovered in 2006. NHEJ1 plays a central role in maintaining genomic stability by facilitating the ligation of DNA ends when homologous recombination is unavailable, particularly during the G1 phase of the cell cycle. Structurally, it shares homology with XRCC4. another key NHEJ factor, featuring an N-terminal globular domain that mediates interactions with XRCC4 and a flexible C-terminal region. This interaction stabilizes the XRCC4-DNA ligase IV complex, enhancing its enzymatic activity and bridging distant DNA ends during repair.
NHEJ1 is indispensable for V(D)J recombination, a process essential for generating diverse antigen receptors in developing lymphocytes. Mutations in the *NHEJ1* gene are linked to severe combined immunodeficiency (SCID), characterized by radiosensitivity, growth defects, and impaired immune function. Additionally, NHEJ1’s role extends beyond immune system development; it influences cellular responses to ionizing radiation and chemotherapeutic agents. Recent studies highlight its involvement in regulating replication stress and telomere maintenance, suggesting broader implications in cancer biology and aging. Despite its error-prone nature, NHEJ1-mediated repair is evolutionarily conserved, underscoring its biological necessity. Ongoing research aims to elucidate its structural dynamics and therapeutic potential, particularly in improving CRISPR-based genome editing efficiency and precision. Understanding NHEJ1’s mechanisms may advance strategies for treating genetic disorders, cancers, and radiation-induced damage.
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