| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IER2 |
| Uniprot No | Q9BTL4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-223aa |
| 氨基酸序列 | MEVQKEAQRIMTLSVWKMYHSRMQRGGLRLHRSLQLSLVMRSARELYLSAKVEALEPEVSLPAALPSDPRLHPPREAESTAETATPDGEHPFPEPMDTQEAPTAEETSACCAPRPAKVSRKRRSSSLSDGGDAGLVPSKKARLEEKEEEEGASSEVADRLQPPPAQAEGAFPNLARVLQRRFSGLLNCSPAAPPTAPPACEAKPACRPADSMLNVLVRAVVAF |
| 预测分子量 | 24,1 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IER2重组蛋白的假设性参考文献示例(请注意，这些文献为模拟示例，实际研究需查阅学术数据库)：
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1. **文献名称**: *IER2 Recombinant Protein Induces Apoptosis in Cancer Cells via p53 Activation*
**作者**: Zhang L, et al.
**摘要**: 本研究通过重组表达IER2蛋白，发现其在多种癌细胞系中通过激活p53通路诱导细胞凋亡，提示IER2可能作为肿瘤治疗的潜在靶点。
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2. **文献名称**: *Characterization of IER2 Recombinant Protein in Oxidative Stress Response*
**作者**: Gupta S, Patel RK.
**摘要**: 作者利用大肠杆菌系统表达并纯化IER2重组蛋白，证实其在细胞氧化应激模型中通过调控Nrf2通路增强抗氧化反应，降低ROS水平。
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3. **文献名称**: *Recombinant IER2 Modulates Inflammatory Cytokines in Macrophages*
**作者**: Kim J, et al.
**摘要**: 研究发现重组IER2蛋白可抑制LPS诱导的巨噬细胞中TNF-α和IL-6的表达，表明其在炎症性疾病中的潜在调控作用。
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4. **文献名称**: *Structural and Functional Analysis of IER2 Recombinant Protein*
**作者**: Müller T, et al.
**摘要**: 通过X射线晶体学解析IER2重组蛋白结构，结合体外实验揭示其DNA结合域的关键氨基酸残基，为功能机制研究提供结构基础。
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**建议**：实际文献可通过PubMed、Google Scholar等平台以关键词“IER2 recombinant protein”或“IER2 overexpression”检索。部分真实研究可能涉及IER2在细胞周期、癌症或代谢疾病中的功能。
The IER2 (Immediate Early Response 2) protein, encoded by the IER2 gene, is a member of the immediate-early gene (IEG) family, which is rapidly induced in response to extracellular stimuli such as growth factors, stress signals, or mitogenic agents. It functions as a transcriptional regulator involved in cellular processes including proliferation, differentiation, and apoptosis. Structurally, IER2 contains a conserved N-terminal domain that facilitates protein-protein interactions and a basic helix-loop-helix (bHLH) domain critical for DNA binding and transcriptional modulation.
Recombinant IER2 protein is engineered using expression systems like *E. coli* or mammalian cells to produce purified, biologically active forms for experimental studies. Its recombinant version often includes affinity tags (e.g., His-tag) for efficient purification. Researchers utilize this protein to investigate its role in signaling pathways, particularly in stress responses and cell cycle regulation. For example, IER2 has been implicated in modulating the MAPK/ERK pathway and influencing cellular responses to DNA damage or oxidative stress. Dysregulation of IER2 expression has been associated with cancer progression, making it a potential target for therapeutic exploration.
Studies involving recombinant IER2 also focus on its interaction with other regulatory proteins, such as transcription factors or chromatin modifiers, to elucidate its mechanistic contributions to gene expression networks. Its transient expression pattern post-stimulation suggests a role as a "molecular switch" in transitioning cells from quiescence to active states. Ongoing research aims to clarify its context-dependent functions, which may vary across tissue types or disease conditions, underscoring its importance in both basic biology and translational applications.
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