| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EGR1 |
| Uniprot No | P18146 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 282-433aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMQQPSLTPLSTIKAFATQSGSQDLKALNTS YQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDRRFSRSDELTRHIR IHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDE RKRHTKIHLRQKDKKADKSVVAS |
| 预测分子量 | 20 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3篇关于EGR1重组蛋白的文献示例，内容基于真实研究领域方向概括(部分信息为模拟简化)：
1. **文献名称**：*"Recombinant EGR1 Protein Regulates Neuronal Apoptosis via p53 Signaling in Alzheimer's Disease Models"*
**作者**：Chen L. et al.
**摘要**：研究利用大肠杆菌表达系统纯化的重组人EGR1蛋白，揭示了其在阿尔茨海默病细胞模型中通过激活p53通路促进神经元凋亡的机制。
2. **文献名称**：*"Structural and Functional Characterization of EGR1 Zinc Finger Domain Expressed in HEK293 Cells"*
**作者**：Kim S. et al.
**摘要**：报道了在哺乳动物细胞(HEK293)中表达并纯化的EGR1重组蛋白，通过X射线晶体学解析其锌指结构域的三维结构，并验证其与靶DNA序列的结合能力。
3. **文献名称**：*"EGR1 Recombinant Protein Inhibits Tumor Growth by Suppressing VEGF in Hepatocellular Carcinoma"*
**作者**：Wang Y. et al.
**摘要**：实验证明通过昆虫杆状病毒系统生产的EGR1重组蛋白能够下调肝癌细胞中VEGF的表达，抑制血管生成和肿瘤生长，提示其潜在治疗价值。
(注：以上为领域知识整合的模拟文献，实际文献需通过PubMed/Google Scholar检索确认。建议用关键词“EGR1 recombinant protein expression”或“EGR1 purification function”查找最新研究。)
**Background of EGR1 Recombinant Protein**
Early Growth Response Protein 1 (EGR1), also known as ZNF268 or NGFI-A, is a transcription factor belonging to the EGR family of zinc-finger proteins. It plays a critical role in regulating gene expression in response to various stimuli, including growth factors, stress signals, and hormonal changes. EGR1 binds to GC-rich promoter regions of target genes, modulating processes such as cell proliferation, differentiation, apoptosis, and tissue repair. Its expression is rapidly induced during early stages of cellular activation, making it a key player in both physiological and pathological conditions, such as cancer, neurodegeneration, and cardiovascular diseases.
Recombinant EGR1 protein is engineered to enable detailed study of its structure, function, and interactions. Typically produced in *E. coli* or mammalian expression systems, the recombinant form retains the DNA-binding domain and transcriptional regulatory activity of native EGR1. Purification tags (e.g., GST, His-tag) are often added to facilitate isolation and detection. Researchers use this tool to investigate EGR1’s role in signaling pathways, its interaction with co-regulators (e.g., p300. NF-κB), and its involvement in diseases. For example, EGR1 is implicated in tumor suppression or promotion, depending on context, and influences neuronal plasticity and inflammation.
Applications of recombinant EGR1 include *in vitro* DNA-binding assays, chromatin immunoprecipitation (ChIP), and studies exploring its post-translational modifications (e.g., phosphorylation). Mutant variants are also generated to dissect functional domains or mimic disease-associated dysregulation. Additionally, it serves as a potential therapeutic target or biomarker in conditions like fibrosis, atherosclerosis, and Alzheimer’s disease. By enabling precise manipulation and analysis, recombinant EGR1 protein remains indispensable for unraveling its multifaceted roles in health and disease.
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