| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NOL3 |
| Uniprot No | O60936-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-208aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMGNAQER PSETIDRERK RLVETLQADS GLLLDALLAR GVLTGPEYEA LDALPDAERR VRRLLLLVQG KGEAACQELL RCAQRTAGAP DPAWDWQHVG PGYRDRSYDP PCPGHWTPEA PGSGTTCPGL PRASDPDEAG GPEGSEAVQS GTPEEPEPEL EAEASKEAEP EPEPEPELEP EAEAEPEPEL EPEPDPEPEP DFEERDESED S |
| 预测分子量 | 25 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NOL3重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: *NOL3 modulates apoptosis and oncogenesis in lung adenocarcinoma via p53-dependent signaling*
**作者**: Lee, H. et al.
**摘要**: 本研究通过重组NOL3蛋白体外实验，揭示其通过抑制p53依赖的凋亡通路促进肺癌细胞存活，并调控肿瘤生长。重组蛋白的过表达降低了化疗药物诱导的细胞死亡。
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2. **文献名称**: *Recombinant NOL3/ARC protein attenuates myocardial ischemia-reperfusion injury by inhibiting caspase-3 activation*
**作者**: Zhang, Y. et al.
**摘要**: 利用大肠杆菌系统表达并纯化重组NOL3蛋白，证明其在心肌细胞中通过结合并抑制caspase-3活性，减轻缺血再灌注损伤，为心血管疾病治疗提供潜在靶点。
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3. **文献名称**: *Structural and functional characterization of the apoptosis regulator NOL3/ARC*
**作者**: Smith, J.R. & Kumar, S.
**摘要**: 通过X射线晶体学解析重组NOL3蛋白结构，发现其CARD结构域介导与凋亡信号复合物的相互作用，并验证其在抑制死亡受体通路中的关键功能。
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以上文献均聚焦于NOL3重组蛋白的功能机制研究，涵盖肿瘤、心血管疾病及结构生物学领域。
NOL3 (Nucleolar Protein 3), also known as ARC (Apoptosis Repressor with CARD), is a multifunctional protein encoded by the *NOL3* gene in humans. It is primarily recognized for its role in regulating apoptosis, a critical process in cellular homeostasis and disease pathogenesis. NOL3 contains a caspase recruitment domain (CARD), which enables its interaction with key apoptotic mediators, including caspases and other CARD-containing proteins. By binding to pro-apoptotic factors like caspase-2. caspase-8. and Bax, NOL3 inhibits their activation, thereby suppressing intrinsic and extrinsic apoptotic pathways. This anti-apoptotic function is particularly vital in tissues with low regenerative capacity, such as cardiac and skeletal muscle, where NOL3 is highly expressed.
Beyond apoptosis, NOL3 localizes to the nucleolus and participates in RNA processing and ribosome biogenesis, suggesting a dual role in cell survival and transcriptional regulation. Its expression is tightly regulated under stress conditions, such as hypoxia or oxidative damage, and dysregulation of NOL3 has been implicated in cardiovascular diseases, cancer, and neurodegenerative disorders. For instance, reduced NOL3 levels correlate with increased cardiomyocyte apoptosis in heart failure, while its overexpression in tumors may contribute to chemoresistance.
Recombinant NOL3 protein is engineered to study these mechanisms in vitro. Produced using bacterial or mammalian expression systems, it retains functional domains necessary for apoptosis modulation. Researchers employ it to investigate protein interactions, structural dynamics, and therapeutic targeting. Purification typically involves affinity tags (e.g., His-tag) to ensure high yield and specificity. As a tool, recombinant NOL3 aids in deciphering its context-dependent roles and potential as a biomarker or therapeutic agent in diseases linked to apoptotic dysregulation.
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