| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FIGN |
| Uniprot No | Q5HY92 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 479-759aa |
| 氨基酸序列 | QGPPVDWNDIAGLDLVKAVIKEEVLWPVLRSDAFSGLTALPRSILLFGPRGTGKTLLGRCIASQLGATFFKIAGSGLVAKWLGEAEKIIHASFLVARCRQPSVIFVSDIDMLLSSQVNEEHSPVSRMRTEFLMQLDTVLTSAEDQIVVICATSKPEEIDESLRRYFMKRLLIPLPDSTARHQIIVQLLSQHNYCLNDKEFALLVQRTEGFSGLDVAHLCQEAVVGPLHAMPATDLSAIMPSQLRPVTYQDFENAFCKIQPSISQKELDMYVEWNKMFGCSQ |
| 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. |
以下是关于FIGN重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：FIGN regulates recombination in meiosis through its evolutionarily conserved interaction with the RAD51/WAS complex
**作者**：Zhang Y, et al.
**摘要**：该研究揭示了FIGN蛋白通过与RAD51/WAS复合物相互作用，调控减数分裂过程中同源重组的关键功能。实验表明，FIGN缺失会导致染色体联会异常和基因组不稳定。
2. **文献名称**：Structural and functional analysis of FIGN reveals its role in maintaining genome integrity
**作者**：Li X, et al.
**摘要**：通过晶体结构解析和功能实验，研究发现FIGN重组蛋白通过结合单链DNA并促进修复因子的招募，在DNA损伤修复中发挥重要作用，尤其在维持体细胞基因组稳定性中至关重要。
3. **文献名称**：FIGN knockdown enhances chemosensitivity in ovarian cancer by impairing homologous recombination repair
**作者**：Wang H, et al.
**摘要**：该文献报道FIGN在卵巢癌细胞中高表达，并通过调控同源重组修复途径影响化疗耐药性。抑制FIGN可增强顺铂等药物的敏感性，提示其作为癌症治疗靶点的潜力。
(注：以上文献信息为示例性内容，实际文献需通过学术数据库检索确认。)
FIGN (fidgetin) is a member of the ATP-dependent metalloprotease family, primarily known for its microtubule-severing activity. This protein plays a critical role in regulating microtubule dynamics, which is essential for cellular processes such as mitosis, intracellular transport, and cytoskeleton remodeling. The FIGN gene encodes a conserved AAA-ATPase domain, enabling it to bind and hydrolyze ATP to disassemble microtubule filaments. Studies have linked FIGN to developmental processes, including neurogenesis and cilia formation, with mutations or dysregulation implicated in congenital disorders like hydrocephalus and microcephaly.
Recombinant FIGN protein is produced using genetic engineering techniques, typically through expression in bacterial or eukaryotic systems like *E. coli* or insect cells. This allows large-scale production of purified, bioactive FIGN for functional studies. Researchers utilize recombinant FIGN to investigate its enzymatic mechanisms, interaction partners, and role in diseases. For example, its microtubule-cutting activity is studied in cancer biology, where abnormal microtubule dynamics contribute to uncontrolled cell division. Additionally, FIGN's involvement in DNA repair pathways and genome stability has sparked interest in its potential as a therapeutic target.
Recent advances in structural biology, such as cryo-EM, have enabled detailed analysis of FIGN's conformational changes during ATP hydrolysis. However, its precise regulatory mechanisms and tissue-specific functions remain under exploration. Recombinant FIGN tools are pivotal in bridging these knowledge gaps, offering insights into fundamental cell biology and translational applications in regenerative medicine or oncology.
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