| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NFIX |
| Uniprot No | Q14938-3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-441aa |
| 氨基酸序列 | MYSPYCLTQDEFHPFIEALLPHVRAFSYTWFNLQARKRKYFKKHEKRMSK DEERAVKDELLGEKPEIKQKWASRLLAKLRKDIRPEFREDYVLTITGKKP PCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERL YKSPQCSNPGLCVQPHHIGVTIKELDLYLAYFVHTPESGQSDSSNQQGDA DIKPLPNGHLSFQDCFVTSGVWNVTELVRVSQTPVATASGPNFSLADLES PSYYNINQVTLGRRSITSPPSTSTTKRPKSIDDSEMESPVDDVFYPGTGR SPAAGSSQSSGWPNDVDAGPASLKKSGKLDFCSALSSQGSSPRMAFTHHP LPVLAGVRPGSPRATASALHFPSTSIIQQSSPYFTHPTIRYHHHHGQDSL KEFVQFVCSDGSGQATGQHSQRQAPPLPTGLSASDPGTATF |
| 预测分子量 | 74 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NFIX重组蛋白的3篇代表性文献摘要(信息基于公开研究内容整合，非真实文献，仅供示例参考)：
1. **《NFIX重组蛋白调控神经干细胞分化的分子机制》**
*作者：Smith A, et al. (2015)*
摘要：研究发现NFIX重组蛋白通过抑制Notch信号通路，促进小鼠胚胎神经干细胞向神经元分化，揭示了其在神经发育中的关键调控作用。
2. **《NFIX缺失导致骨骼发育异常的基因治疗研究》**
*作者：Zhang L, et al. (2019)*
摘要：通过构建NFIX基因敲除小鼠模型，发现NFIX重组蛋白递送可部分恢复颅骨闭合缺陷，为骨骼发育疾病提供了潜在治疗策略。
3. **《NFIX重组蛋白抑制胶质母细胞瘤侵袭的机制》**
*作者：Chen Y, et al. (2021)*
摘要：NFIX过表达显著降低胶质母细胞瘤细胞的迁移能力，其机制与调控MMP9和上皮-间质转化(EMT)通路相关，提示其作为肿瘤抑制因子的潜力。
4. **《高效表达NFIX重组蛋白的哺乳动物系统优化》**
*作者：Wang H, et al. (2020)*
摘要：开发了一种基于HEK293细胞的新型NFIX重组蛋白表达纯化方案，获得高纯度活性蛋白，为后续功能研究提供可靠工具。
注：以上文献名为虚拟示例，实际研究需通过PubMed等数据库检索真实文献。
**Background of NFIX Recombinant Protein**
The NFIX (Nuclear Factor I X) recombinant protein is a engineered version of the NFIX transcription factor, which belongs to the Nuclear Factor I (NFI) family. NFI proteins are evolutionarily conserved DNA-binding proteins that regulate gene expression by binding to specific promoter or enhancer regions. NFIX, encoded by the *NFIX* gene, plays critical roles in cellular differentiation, organ development, and tissue homeostasis. It is particularly implicated in neurodevelopment, skeletal formation, and hematopoiesis. Dysregulation or mutations in NFIX are associated with developmental disorders such as Sotos syndrome and Malan syndrome, highlighting its biological significance.
Recombinant NFIX proteins are typically produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) to ensure high purity and functionality. These proteins retain key structural domains, including the N-terminal DNA-binding/dimerization domain (NAC domain) and C-terminal regulatory regions, enabling them to interact with DNA and other proteins. Researchers utilize NFIX recombinant proteins to study its molecular mechanisms, including its role in chromatin remodeling, transcriptional activation/repression, and crosstalk with signaling pathways like TGF-β or Wnt.
In biomedical research, NFIX recombinant proteins serve as tools for *in vitro* assays, protein-protein/DNA interaction studies, and functional genomics. They also hold potential in therapeutic exploration, such as targeting NFIX-related pathways in cancers or regenerative medicine. The development of NFIX recombinant variants (e.g., tagged or truncated forms) further expands their utility in structural biology and high-throughput screening. Overall, NFIX recombinant proteins are vital for dissecting its physiological roles and developing interventions for NFIX-associated pathologies.
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