| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NAGK |
| Uniprot No | Q9UJ70 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-344aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAAIYGG VEGGGTRSEV LLVSEDGKIL AEADGLSTNH WLIGTDKCVE RINEMVNRAK RKAGVDPLVP LRSLGLSLSG GDQEDAGRIL IEELRDRFPY LSESYLITTD AAGSIATATP DGGVVLISGT GSNCRLINPD GSESGCGGWG HMMGDEGSAY WIAHQAVKIV FDSIDNLEAA PHDIGYVKQA MFHYFQVPDR LGILTHLYRD FDKCRFAGFC RKIAEGAQQG DPLSRYIFRK AGEMLGRHIV AVLPEIDPVL FQGKIGLPIL CVGSVWKSWE LLKEGFLLAL TQGREIQAQN FFSSFTLMKL RHSSALGGAS LGARHIGHLL PMDYSANAIA FYSYTFS |
| 预测分子量 | 40 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NAGK重组蛋白的代表性文献(注：文献信息为模拟生成，仅用于示例)：
1. **"Expression and Characterization of Recombinant N-Acetylglutamate Kinase from Arabidopsis thaliana"**
- 作者：Chen L. et al.
- 摘要：报道了拟南芥NAGK在大肠杆菌中的重组表达与纯化，分析了其酶动力学特性及精氨酸反馈抑制机制。
2. **"Crystal Structure of NAGK from Thermus thermophilus: Insights into Catalytic Mechanism"**
- 作者：Yamaguchi H. et al.
- 摘要：通过重组表达嗜热菌NAGK蛋白，解析了其晶体结构，揭示了ATP结合域和底物识别位点的关键氨基酸残基。
3. **"Functional Analysis of Human NAGK in Urea Cycle Disorders"**
- 作者：Wang Q. et al.
- 摘要：利用HEK293细胞表达人源重组NAGK，研究其突变体与尿素循环代谢疾病的关联，为临床诊断提供分子基础。
4. **"Optimized Production of NAGK in Pichia pastoris for Industrial Applications"**
- 作者：Rodríguez E. et al.
- 摘要：开发了毕赤酵母高效表达重组NAGK的工艺，验证其在酶法合成精氨酸前体化合物中的规模化应用潜力。
**提示**：实际文献需通过PubMed/SciHub等平台检索(关键词：NAGK + recombinant/prokaryotic expression/purification)，推荐结合UniProt数据库(ID: Q8T6A3)查找引用文献。
**Background of N-Acetylglutamate Kinase (NAGK) Recombinant Protein**
N-Acetylglutamate kinase (NAGK) is a critical enzyme in the arginine biosynthesis pathway, primarily found in microorganisms, plants, and some eukaryotes. It catalyzes the ATP-dependent phosphorylation of N-acetylglutamate (NAG) to form N-acetylglutamyl phosphate, a rate-limiting step in the production of arginine, an essential amino acid involved in protein synthesis, nitrogen metabolism, and nitric oxide signaling. NAGK’s activity is tightly regulated, often through feedback inhibition by arginine, highlighting its role in maintaining metabolic balance.
Recombinant NAGK proteins are engineered using genetic engineering techniques, where the *NAGK* gene is cloned into expression vectors (e.g., *E. coli*, yeast, or mammalian systems) to produce purified, functional enzyme variants. This approach enables large-scale production of NAGK with high purity and consistency, bypassing challenges associated with isolating the enzyme from native sources. Recombinant NAGK is widely utilized in biochemical and structural studies to investigate its catalytic mechanism, allosteric regulation, and interactions with substrates or inhibitors.
Structurally, NAGK belongs to the amino acid kinase family, characterized by a conserved ATP-binding domain and a substrate-specific catalytic site. Recent crystallographic and cryo-EM studies have resolved its 3D architecture, revealing dynamic conformational changes during catalysis and regulation. These insights have spurred applications in drug discovery (e.g., targeting microbial NAGK for antibiotic development) and agricultural biotechnology (e.g., enhancing nitrogen use efficiency in crops). Additionally, recombinant NAGK serves as a tool enzyme in metabolic engineering and synthetic biology to optimize arginine pathways for industrial or therapeutic purposes.
Overall, recombinant NAGK represents a pivotal resource for advancing research in enzymology, metabolic diseases, and biotechnological innovations.
在生物科技领域，蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者，凭借自身卓越的研发实力，每年能成功研发 1000 多种全新蛋白，在重组蛋白领域不断突破。 在重组蛋白生产过程中，艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白，到具有特定催化功能的酶、参与信号传导的激酶，再到用于免疫研究的病毒抗原，艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统，昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势，能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求，从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品，更是从源头到终端的一站式解决方案。从最初的基因合成，精准地构建出符合要求的基因序列，到载体构建，为蛋白表达创造适宜的环境，再到蛋白质表达和纯化，每一个环节都严格把控。我们充分尊重客户的个性化需求，在表达 / 纯化标签的选择、表达宿主的确定等方面，为客户量身定制专属方案。 同时，艾普蒂还配备了多种纯化体系，能够应对不同特性蛋白的纯化需求。这种灵活性和专业性，极大地提高了蛋白表达和纯化的成功率，让客户的研究项目得以顺利推进，在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台，包括： 哺乳动物细胞表达平台：利用哺乳动物细胞精准修饰蛋白，产出与天然蛋白相似的重组蛋白，用于药物研发、细胞治疗等。 杂交瘤开发平台：通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株，优化后的技术让抗体亲和力与特异性更高，应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台：FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞；Beacon® 基于微流控技术，单细胞水平捕获、分析 B 细胞，挖掘抗体多样性，缩短开发周期。 凭借这些平台，艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务，推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
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