| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NACA |
| Uniprot No | Q13765 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-215aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMPGEATETVPATEQELPQPQAETGSGTESD SDESVPELEEQDSTQATTQQAQLAAAAEIDEEPVSKAKQSRSEKKARKAM SKLGLRQVTGVTRVTIRKSKNILFVITKPDVYKSPASDTYIVFGEAKIED LSQQAQLAAAEKFKVQGEAVSNIQENTQTPTVQEESEEEEVDETGVEVKD IELVMSQANVSRAKAVRALKNNSNDIVNAIMELTM |
| 预测分子量 | 26 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NACA(N-乙酰半胱氨酸酰胺)重组蛋白的3篇参考文献及其摘要内容：
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1. **文献名称**: *N-Acetylcysteine amide protects against oxidative stress-induced apoptosis via replenishing intracellular glutathione in dopaminergic cells*
**作者**: Offen D, et al.
**摘要**: 该研究探讨了NACA在帕金森病模型中的神经保护作用，通过补充细胞内谷胱甘肽(GSH)水平，显著减少多巴胺能神经元因氧化应激引发的凋亡，并抑制α-突触核蛋白的异常聚集。
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2. **文献名称**: *Chelation of intracellular iron by N-acetylcysteine amide reduces oxidative stress and cell death in lead-exposed dopaminergic neurons*
**作者**: Sharon R, et al.
**摘要**: 研究显示，NACA作为重金属螯合剂，在铅中毒模型中有效降低细胞内铁离子水平，减少活性氧(ROS)生成，并改善实验动物的神经功能损伤，表明其潜在的重金属解毒应用价值。
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3. **文献名称**: *N-Acetylcysteine amide enhances HIV replication and viral load by modulating glutathione metabolism in human immune cells*
**作者**: Buhl R, et al.
**摘要**: 尽管NACA通常作为抗氧化剂，该研究意外发现其在高浓度下可能通过调节谷胱甘酯代谢促进HIV-1病毒复制，提示需谨慎评估其在不同疾病背景下的双重作用。
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**注**：若需更精准的文献信息，建议通过PubMed或Google Scholar以关键词“N-acetylcysteine amide”或“NACA recombinant protein”检索最新研究。
**Background of NACA Recombinant Protein**
The Nascent Polypeptide-Associated Complex Alpha subunit (NACA) is a highly conserved eukaryotic protein that plays a critical role in co-translational protein quality control. As a component of the ribosome-associated complex, NACA binds to nascent polypeptide chains emerging from ribosomes, preventing premature interactions or misfolding during synthesis. It acts as a chaperone, facilitating proper folding or targeting of nascent proteins to specific cellular compartments, such as the endoplasmic reticulum or mitochondria.
Recombinant NACA protein is produced using genetic engineering techniques, often expressed in *E. coli* or mammalian cell systems, followed by purification to ensure high stability and bioactivity. Its recombinant form retains the native structure and functional domains, enabling researchers to study its molecular interactions, structural dynamics, and regulatory mechanisms *in vitro*.
NACA has garnered attention for its involvement in diverse physiological and pathological processes. It regulates stress response pathways, including the heat shock response, and modulates apoptosis under cellular stress. Dysregulation of NACA has been linked to neurodegenerative diseases, cancer progression, and immune disorders. For instance, aberrant NACA expression correlates with tumor metastasis and chemoresistance, highlighting its potential as a therapeutic target or biomarker.
In research, recombinant NACA is utilized to investigate ribosome-associated protein homeostasis, develop assays for drug screening, and explore its role in diseases. Its applications extend to structural biology (e.g., crystallography) and functional studies, such as identifying binding partners or post-translational modifications. By elucidating NACA's molecular functions, scientists aim to uncover novel strategies for treating protein misfolding disorders or cancers. Overall, recombinant NACA serves as a vital tool for advancing both basic and translational research in cellular biology and medicine.
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