纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | NAPRT |
Uniprot No | Q6XQN6 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 229-538aa |
氨基酸序列 | MLAPAAGEGPGVDLAAKAQVWLEQVCAHLGLGVQEPHPGERAAFVAYALAFPRAFQGLLDTYSVWRSGLPNFLAVALALGELGYRAVGVRLDSGDLLQQAQEIRKVFRAAAAQFQVPWLESVLIVVSNNIDEEALARLAQEGSEVNVIGIGTSVVTCPQQPSLGGVYKLVAVGGQPRMKLTEDPEKQTLPGSKAAFRLLGSDGSPLMDMLQLAEEPVPQAGQELRVWPPGAQEPCTVRPAQVEPLLRLCLQQGQLCEPLPSLAESRALAQLSLSRLSPEHRRLRSPAQYQVVLSERLQALVNSLCAGQSP |
预测分子量 | 35.2 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篇与NAPRT(Nicotinate Phosphoribosyltransferase)重组蛋白相关的文献摘要概括:
1. **文献名称**: *"Cloning, expression, and characterization of recombinant human nicotinate phosphoribosyltransferase"*
**作者**: Hara N. et al.
**摘要**: 研究报道了人源NAPRT基因在大肠杆菌中的重组表达及纯化,分析了其酶活性与NAD+生物合成的关系,并探讨其结构功能特征。
2. **文献名称**: *"Structural insights into the mechanism of NAD+ biosynthesis by human NAPRT"*
**作者**: Khan J.A. et al.
**摘要**: 通过X射线晶体学解析重组NAPRT蛋白的三维结构,揭示了其底物结合位点及催化机制,为靶向药物设计提供依据。
3. **文献名称**: *"Recombinant NAPRT as a potential biomarker in cancer therapy resistance"*
**作者**: Piacente F. et al.
**摘要**: 研究发现重组NAPRT在肿瘤细胞中的过表达可增强NAD+补救途径活性,导致化疗药物(如烟酰胺类似物)耐药性,提出其作为治疗靶点的潜力。
注:上述文献为示例性概括,实际文献需通过PubMed/Google Scholar等平台检索确认。
**Background of NAPRT Recombinant Protein**
Nicotinate phosphoribosyltransferase (NAPRT) is a key enzyme in the cellular NAD+ salvage pathway, catalyzing the conversion of nicotinic acid (NA) to nicotinic acid mononucleotide (NAMN), a precursor for NAD+ biosynthesis. NAD+ is an essential coenzyme involved in redox reactions, energy metabolism, DNA repair, and signaling processes. Unlike the de novo NAD+ synthesis pathway, which relies on tryptophan, the salvage pathway mediated by NAPRT provides a critical alternative route for maintaining NAD+ homeostasis, particularly under stress conditions or in tissues with high metabolic demands.
NAPRT is expressed in various human tissues, including the liver, kidney, and intestines. Its activity is tightly regulated, and dysregulation has been linked to metabolic disorders, cancer, and neurodegenerative diseases. For instance, certain cancers exhibit NAPRT downregulation, making them susceptible to NAD+-depleting therapies like nicotinamide phosphoribosyltransferase (NAMPT) inhibitors. Conversely, NAPRT overexpression in tumors may confer resistance to such treatments, highlighting its therapeutic relevance.
Recombinant NAPRT protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), enables detailed biochemical and structural studies. Purification techniques such as affinity chromatography yield high-purity protein for functional assays, crystallography, or drug screening. Structural insights into NAPRT’s active site and regulatory mechanisms have spurred interest in developing small-molecule modulators to target NAD+ metabolism in diseases.
Additionally, recombinant NAPRT serves as a tool to explore cellular NAD+ dynamics, gene expression regulation, and interactions with partner proteins. Its role in inflammation and aging further underscores its potential as a biomarker or therapeutic target. Ongoing research aims to harness NAPRT’s enzymatic properties for innovative treatments, including enzyme replacement therapies or combinatorial approaches with NAD+-targeting drugs. Overall, NAPRT recombinant protein is pivotal in advancing our understanding of NAD+ biology and its translational applications.
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