| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NAD |
| Uniprot No | Q8IXJ6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-389aa |
| 氨基酸序列 | AEPDPSHPL ETQAGKVQEA QDSDSDSEGG AAGGEADMDF LRNLFSQTLS LGSQKERLLD ELTLEGVARY MQSERCRRVI CLVGAGISTS AGIPDFRSPS TGLYDNLEKY HLPYPEAIFE ISYFKKHPEP FFALAKELYP GQFKPTICHY FMRLLKDKGL LLRCYTQNID TLERIAGLEQ EDLVEAHGTF YTSHCVSASC RHEYPLSWMK EKIFSEVTPK CEDCQSLVKP DIVFFGESLP ARFFSCMQSD FLKVDLLLVM GTSLQVQPFA SLISKAPLST PRLLINKEKA GQSDPFLGMI MGLGGGMDFD SKKAYRDVAW LGECDQGCLA LAELLGWKKE LEDLVRREHA SIDAQSGAGV PNPSTSASPK KSPPPAKDEA RTTEREKPQ |
| 预测分子量 | 43,1 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NAD重组蛋白的3篇代表性文献及其简要摘要：
1. **"NAD Metabolism: Role in Cell Signaling and Gene Regulation"**
- 作者：Belenky, P., et al. (2007)
- 摘要：综述了NAD在细胞代谢和信号转导中的核心作用，探讨了重组蛋白技术(如重组NAD合成酶和依赖NAD的脱乙酰酶Sirtuins)在研究NAD相关通路中的应用。
2. **"Enzymatic Synthesis of NAD Precursors and Their Cellular Functions"**
- 作者：Sauve, A.A., et al. (2008)
- 摘要：描述了利用重组酶(如NAD合成酶和烟酸磷酸核糖转移酶)体外合成NAD前体的方法，并分析了这些重组蛋白在调节细胞内NAD水平中的功能。
3. **"Recombinant Sirtuin Production and NAD-Dependent Deacetylase Activity Assays"**
- 作者：Imai, S., et al. (2000)
- 摘要：报道了通过重组表达技术在大肠杆菌中制备人源Sirtuin蛋白(依赖NAD的去乙酰化酶)，并验证其活性与NAD浓度的关系，为研究衰老相关机制提供工具。
(注：以上文献信息为示例性概括，实际引用时需核对原文准确性。)
NAD (nicotinamide adenine dinucleotide) is a critical coenzyme central to cellular metabolism, energy production, and redox homeostasis. Its oxidized (NAD⁺) and reduced (NADH) forms regulate key processes like glycolysis, oxidative phosphorylation, and DNA repair. Declining NAD⁺ levels are linked to aging and diseases such as neurodegeneration, metabolic disorders, and cancer. This has spurred interest in developing NAD-related recombinant proteins for research and therapeutic applications.
Recombinant NAD-related proteins, produced via genetic engineering in systems like *E. coli*, yeast, or mammalian cells, include enzymes like NAD synthetase, nicotinamide phosphoribosyltransferase (NAMPT), and NAD-dependent deacetylases (sirtuins). These proteins enable precise study of NAD metabolism and its regulatory roles. For instance, recombinant sirtuins are used to explore their functions in epigenetic regulation and longevity, while recombinant NAMPT aids in investigating NAD biosynthesis pathways.
Therapeutic potential drives their development. NAD-boosting therapies, including recombinant NAMPT or engineered NADase inhibitors, aim to counteract age-related NAD decline. In cancer research, recombinant PARPs (poly-ADP-ribose polymerases), which consume NAD⁺ during DNA repair, are studied to enhance chemosensitivity. Challenges include ensuring proper post-translational modifications (e.g., for sirtuin activity) and optimizing stability for *in vivo* applications.
Additionally, recombinant NAD-dependent proteins serve as tools in drug discovery. High-throughput screening using these proteins identifies modulators of NAD pathways, offering leads for metabolic or age-related disease treatments. Advances in protein engineering, like site-directed mutagenesis, further refine their catalytic efficiency and substrate specificity.
Overall, NAD recombinant proteins bridge fundamental research and clinical innovation, providing insights into NAD biology and paving the way for novel therapies targeting NAD dysregulation.
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