| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IRF4 |
| Uniprot No | Q15306 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-451aa |
| 氨基酸序列 | MNLEGGGRGGEFGMSAVSCGNGKLRQWLIDQIDSGKYPGLVWENEEKSIF RIPWKHAGKQDYNREEDAALFKAWALFKGKFREGIDKPDPPTWKTRLRCA LNKSNDFEELVERSQLDISDPYKVYRIVPEGAKKGAKQLTLEDPQMSMSH PYTMTTPYPSLPAQQVHNYMMPPLDRSWRDYVPDQPHPEIPYQCPMTFGP RGHHWQGPACENGCQVTGTFYACAPPESQAPGVPTEPSIRSAEALAFSDC RLHICLYYREILVKELTTSSPEGCRISHGHTYDASNLDQVLLPYPEDNGQ RKNIEKLLSHLERGVVPWMAPDGLYAKRLCQSRIYWDGPLALCNDRPNKL ERDQTCKLFDTQQFLSELQAFAHHGRSLPRFQVTLCFGEEFPDPQRQRKL ITAHVEPLLARQLYYFAQQNSGHFLRGYDLPEHISNPEDYHRSIRHSSIQ E |
| 预测分子量 | 75 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IRF4重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**：*Structural basis of dimerization and nucleic acid binding in human IRF4*
**作者**：Escalante CR et al.
**摘要**：该研究解析了IRF4重组蛋白的晶体结构，揭示了其二聚化机制及与DNA结合的分子基础，为解释其在淋巴细胞分化中的调控功能提供结构依据。
2. **文献名称**：*IRF4 regulates B cell signaling and plasma cell differentiation via direct binding to multiple target genes*
**作者**：Sciammas R et al.
**摘要**：通过重组IRF4蛋白的体外实验，证明其直接结合多个B细胞相关基因启动子，调控抗体分泌和浆细胞分化，揭示其在体液免疫中的核心作用。
3. **文献名称**：*Recombinant IRF4 protein rescues Th17 differentiation in IRF4-deficient T cells*
**作者**：Brüstle A et al.
**摘要**：研究利用重组IRF4蛋白回补实验，证实IRF4通过调控IL-17等细胞因子表达驱动Th17细胞分化，为自身免疫疾病机制研究提供实验模型。
(注：以上文献信息为示例性内容，实际引用时需核对原文准确性。)
Interferon Regulatory Factor 4 (IRF4) is a transcription factor belonging to the IRF family, primarily expressed in immune cells such as lymphocytes, macrophages, and dendritic cells. It plays a pivotal role in regulating immune responses, including lymphocyte development, plasma cell differentiation, and cytokine signaling. Structurally, IRF4 contains a conserved N-terminal DNA-binding domain, a central regulatory region, and a C-terminal transactivation domain. Its activity is tightly regulated through post-translational modifications and interactions with partner proteins like PU.1 or SPIB.
Recombinant IRF4 protein is engineered in vitro using expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional IRF4 for research or therapeutic applications. This protein retains the ability to bind DNA and regulate target genes, enabling studies on its molecular mechanisms in immune regulation and disease. Researchers utilize recombinant IRF4 to investigate its dual role in both promoting and suppressing immune-related pathways, depending on cellular context. For example, IRF4 is essential for T helper cell differentiation but is also implicated in oncogenesis, particularly in hematologic malignancies like multiple myeloma.
Interest in recombinant IRF4 has grown due to its therapeutic potential. Inhibitors targeting IRF4 are being explored for cancer treatment, while its immunomodulatory functions are relevant for autoimmune disease management. Additionally, structural studies using recombinant IRF4 help identify binding interfaces for drug design. Despite its complexity, recombinant IRF4 remains a critical tool for dissecting immune signaling networks and developing precision therapies.
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