| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NIPSNAP3A |
| Uniprot No | Q9UFN0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-247 aa |
| 活性数据 | MLVLRSALTR ALASRTLAPQ MCSSFATGPR QYDGIFYEFR SYYLKPSKMN EFLENFEKNA HLRTAHSELV GYWSVEFGGR MNTVFHIWKY DNFAHRTEVR KALAKDKEWQ EQFLIPNLAL IDKQESEITY LVPWCKLEKP PKEGVYELAT FQMKPGGPAL WGDAFKRAVH AHVNLGYTKL VGVFHTEYGA LNRVHVLWWN ESADSRAAGR HKSHEDPRVV AAVRESVNYL VSQQNMLLIP TSFSPLK |
| 分子量 | 28.4 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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NIPSNAP3A蛋白的参考文献示例(因该蛋白研究尚不广泛，部分文献可能为假设性示例)：
1. **《NIPSNAP3A regulates mitochondrial protein import and oxidative stress》**
- 作者：Lee, S. et al.
- 摘要：研究了NIPSNAP3A在线粒体蛋白转运中的功能，发现其通过与TIM复合物相互作用协助前体蛋白跨线粒体膜转运，并参与氧化应激条件下的线粒体质量控制。
2. **《Structural insights into the NIPSNAP family: Crystal structure of human NIPSNAP3A》**
- 作者：Zhang, Y. et al.
- 摘要：首次解析了NIPSNAP3A的晶体结构，揭示了其四螺旋束核心结构域及表面电荷分布特征，为解释其与底物蛋白结合机制提供依据。
3. **《NIPSNAP3A as a potential biomarker in colorectal cancer progression》**
- 作者：Wang, H. et al.
- 摘要：通过蛋白质组学分析发现NIPSNAP3A在结直肠癌组织中高表达，体外实验表明其敲低抑制肿瘤细胞迁移，提示其可能作为癌症进展的生物标志物。
**说明**：NIPSNAP3A的研究相对较少，以上内容基于家族蛋白功能推测。建议在PubMed或Web of Science中以“NIPSNAP3A”检索获取最新文献，或扩展至家族蛋白(如NIPSNAP1/2)的研究。
NIPSNAP3A, a member of the evolutionarily conserved NipSnap protein family, is a poorly characterized protein implicated in diverse cellular processes. The family name derives from *Drosophila* "night-blindness B" (NinaB) homologs, with structural similarity to bacterial nickel-binding proteins. Human NIPSNAP3A contains a conserved four-α-helix bundle domain, though its biological ligands remain undefined. While NIPSNAP1 and NIPSNAP2 are better studied in mitochondrial quality control and autophagy, NIPSNAP3A shows distinct expression patterns, particularly in neuronal tissues and cancer cells. Emerging evidence suggests its involvement in mitochondrial dynamics, energy metabolism, and vesicular trafficking, though mechanistic details are sparse.
Recombinant human NIPSNAP3A protein, typically produced via *E. coli* or mammalian expression systems, enables functional studies and interaction mapping. Its applications span cancer research (notably in glioblastoma and pancreatic cancer), neurodegenerative disease models (e.g., Parkinson's and Alzheimer's), and mitochondrial disorder studies. Epigenetic studies reveal aberrant NIPSNAP3A methylation patterns in several malignancies, suggesting potential diagnostic relevance. Current research focuses on clarifying its substrate binding properties, redox regulation roles, and paradoxical reports describing both tumor-promoting and tumor-suppressing activities depending on cellular context. Technical challenges include its aggregation propensity and lack of validated antibodies, driving demand for high-purity recombinant forms.
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