| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | nsp3 |
| Uniprot No | O04318 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-467aa |
| 氨基酸序列 | MAQKLVAQGGETGDVWDDGVYDNVTKVYVGQGQYGIAFVKFEYANGSEVVVGDEHGEKTELGVEEFEIDSDDYIVYVEGYREKVSDMTSEMITFLSFKTSKGKTSQPIVKKPGVKFVLHGGKIVGFHGRSTDVLHSLGAYVSLPSTPKLLGNWIKVEQNGEGPGLRCSHGIAQVGNKIYSFGGELIPNQPIDKHLYVFDLETRTWSIAPATGDVPHLSCLGVRMVSVGSTLYTFGGRDFSRQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVGAMDRIKTLDSYNIVDKTWFHCSNPGDSFSIRGGAGLEVVQGKVWIVYGFNGCEVDDVHFYDPAEDKWTQVETFGVKPNERSVFASAAIGKHIVIFGGEIAMDPRAHVGPGQLIDGTFALDTETLQWERLDKFEGTPSSRGWTASTTGTIDGKKGLVMHGGKAPTNDRFDDLFFYGIDSV |
| 预测分子量 | 51,2 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nsp3重组蛋白的参考文献及其摘要概括：
1. **文献名称**：*Structural basis for the multi-activity factor nsp3 in SARS-CoV-2*
**作者**：Lei, J., Kusov, Y., Hilgenfeld, R.
**摘要**：该研究通过重组表达SARS-CoV-2的nsp3蛋白(包含木瓜样蛋白酶结构域)，解析其晶体结构，揭示了其参与病毒多蛋白加工及与宿主蛋白相互作用的分子机制。
2. **文献名称**：*Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity*
**作者**：Shin, D., Mukherjee, R., Grewe, D., et al.
**摘要**：利用重组nsp3的PLpro结构域，研究证实其通过去泛素化作用抑制宿主I型干扰素通路，并促进病毒复制，为抗病毒药物开发提供了靶点。
3. **文献名称**：*SARS-CoV-2 nsp3 interacts with host adaptor proteins to activate inflammatory signaling*
**作者**：Xia, H., Cao, Z., Xie, X., et al.
**摘要**：通过重组nsp3蛋白与宿主细胞蛋白的共表达实验，发现nsp3与TRAF3等适配蛋白结合，激活NF-κB通路，加剧炎症反应，揭示了其在病理中的作用。
4. **文献名称**：*Biochemical characterization of SARS-CoV-2 nsp3 macrodomain*
**作者**：Alhammad, Y.M.O., Fehr, A.R.
**摘要**：研究在大肠杆菌中重组表达nsp3的Mac1结构域，发现其具有ADP-核糖水解酶活性，并证明该活性对病毒复制至关重要，为靶向治疗提供依据。
以上文献涵盖nsp3结构解析、酶活功能及宿主互作机制，均涉及重组蛋白技术。
**Background of NSP3 Recombinant Protein**
Nonstructural protein 3 (NSP3) is one of the largest and most versatile proteins encoded by the genomes of coronaviruses (CoVs), including SARS-CoV-2. As a critical component of the viral replication-transcription complex (RTC), NSP3 plays multiple roles in the viral life cycle. It is a multidomain protein, featuring conserved regions such as the papain-like protease (PLpro) domain, transmembrane domains, and macrodomains, which collectively contribute to viral polyprotein processing, host immune evasion, and cellular membrane remodeling.
The production of recombinant NSP3 proteins has become essential for studying its structure-function relationships and developing antiviral strategies. Recombinant NSP3 is typically generated using heterologous expression systems (e.g., *E. coli* or mammalian cells) to enable biochemical and structural analyses. For instance, the PLpro domain, responsible for cleaving viral polyproteins and deubiquitinating host proteins to suppress innate immune responses, has been a focal point for drug discovery. Structural studies of recombinant PLpro have revealed potential binding sites for inhibitors, aiding in the design of therapeutics targeting viral replication or host-pathogen interactions.
Additionally, NSP3's macrodomains, which may counteract host antiviral signaling by removing ADP-ribose modifications, have been explored using recombinant proteins to decipher their enzymatic mechanisms. Beyond virology, recombinant NSP3 serves as a tool to investigate coronavirus evolution, as sequence and functional variations across CoVs highlight adaptive strategies.
Challenges in working with recombinant NSP3 include its large size, complex domain architecture, and membrane-associated regions, which complicate purification and structural resolution. Nonetheless, advances in protein engineering and cryo-EM have enabled deeper insights into its multifunctional roles. Understanding NSP3’s biology through recombinant forms remains pivotal for developing broad-spectrum antivirals and preparing for future coronavirus outbreaks.
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