| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VNN3 |
| Uniprot No | Q9NY84-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 175-274aa |
| 氨基酸序列 | ARYHKYNLFAPEIQFDFPKDSELVTFDTPFGKFGIFTCFDIFSHDPAVVV VDEFQLTAFSTPQHGTTRCPSSRLFPSIQHGPRPWESIYLLQIPTTPACT |
| 预测分子量 | 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VNN3(Vanin-3)重组蛋白的3篇示例参考文献(内容为虚构示例，仅供参考)：
1. **《重组人Vanin-3蛋白的表达及其在氧化应激中的功能研究》**
作者：Li, X.; Wang, Y.; Chen, J.
摘要：本研究成功在大肠杆菌中表达并纯化了具有生物活性的重组人VNN3蛋白，证实其具有磷酸酶活性，并发现其可通过调节谷胱甘肽代谢缓解细胞氧化应激损伤。
2. **《Vanin-3重组蛋白抑制炎症反应的机制探索》**
作者：Martinez, R.; Kim, H.; Tanaka, S.
摘要：通过哺乳动物细胞系统表达VNN3重组蛋白，发现其能显著降低脂多糖(LPS)诱导的巨噬细胞炎症因子释放，提示VNN3可能通过NF-κB通路调控先天免疫反应。
3. **《重组VNN3蛋白促进肿瘤细胞迁移的体外实验证据》**
作者：Zhang, L.; Gupta, P.; Liu, F.
摘要：利用HEK293细胞表达的重组VNN3蛋白处理结肠癌细胞，发现其通过上调基质金属蛋白酶(MMP-9)增强肿瘤细胞迁移能力，为VNN3的促癌机制提供了新依据。
注：以上文献信息为模拟生成，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实文献。
**Background of VNN3 Recombinant Protein**
VNN3 (Vanin-3), a member of the vanin protein family, is a glycosylphosphatidylinositol (GPI)-anchored ectoenzyme encoded by the *VNN3* gene in humans. The vanin family, including VNN1. VNN2. and VNN3. is evolutionarily conserved and characterized by pantetheinase activity, which hydrolyzes pantetheine to produce cysteamine and pantothenic acid (vitamin B5). These metabolites play critical roles in oxidative stress response, inflammation, and metabolic regulation. While VNN1 and VNN2 have been extensively studied in immune modulation and tissue repair, VNN3 remains less characterized, though it shares structural homology with other vanins, including a conserved catalytic domain.
VNN3 is predominantly expressed in specific tissues, such as the liver, kidneys, and gastrointestinal tract, suggesting organ-specific functions. Its GPI anchor enables membrane localization, potentially influencing cell-matrix interactions or signaling pathways. Studies implicate VNN3 in modulating cellular redox balance by regulating cysteamine levels, which affect glutathione synthesis and detoxification processes. Dysregulation of VNN3 has been loosely associated with metabolic disorders, inflammatory conditions, and cancer progression, though mechanistic insights are limited.
Recombinant VNN3 protein is produced via heterologous expression systems (e.g., mammalian or insect cells) to ensure proper post-translational modifications, such as glycosylation and GPI anchoring. This engineered protein serves as a tool to study VNN3’s enzymatic activity, substrate specificity, and interactions in vitro or in cellular models. It also aids in exploring therapeutic potential, such as targeting oxidative stress-related diseases or developing biomarkers. Despite its emerging relevance, further research is needed to fully elucidate VNN3’s physiological and pathological roles, distinguishing it from other vanin family members.
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