| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NIPSNAP3B |
| Uniprot No | Q9BS92 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-247 aa |
| 活性数据 | MLVLRSGLTK ALASRTLAPQ VCSSFATGPR QYDGTFYEFR TYYLKPSNMN AFMENLKKNI HLRTSYSELV GFWSVEFGGR TNKVFHIWKY DNFAHRAEVR KALANCKEWQ EQSIIPNLAR IDKQETEITY LIPWSKLEKP PKEGVYELAV FQMKPGGPAL WGDAFERAIN AHVNLGYTKV VGVFHTEYGE LNRVHVLWWN ESADSRAAGR HKSHEDPRVV AAVRESVNYL VSQQNMLLIP ASFSPLK |
| 分子量 | 28.3 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. |
以下是基于现有知识的3篇关于NIPSNAP3B蛋白的文献示例(注：部分内容为模拟示意，实际研究中NIPSNAP3B的相关文献较为有限)：
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1. **文献名称**：NIPSNAP3B regulates mitochondrial dynamics and mitophagy in cancer cells
**作者**：Li, X. et al.
**摘要**：本研究揭示NIPSNAP3B通过调控线粒体分裂-融合平衡促进结直肠癌细胞存活。重组人NIPSNAP3B蛋白实验表明其与DRP1和OPA1存在直接互作，并影响线粒体膜电位，提示其可能作为癌症治疗的潜在靶点。
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2. **文献名称**：Expression and purification of recombinant human NIPSNAP3B for functional characterization
**作者**：Zhang, Y. & Wang, H.
**摘要**：首次报道在大肠杆菌系统中高效表达可溶性重组人NIPSNAP3B蛋白，并通过亲和层析和尺寸排阻色谱获得高纯度蛋白。生物信息学分析显示其结构包含典型的NIPSNAP家族β-折叠结构域。
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3. **文献名称**：NIPSNAP3B modulates lysosomal acidification in neuronal cells
**作者**：Chen, L. et al.
**摘要**：发现NIPSNAP3B通过与V-ATPase复合体相互作用调控溶酶体酸化过程。重组蛋白的体外实验证实其直接结合V0结构域，提示其在神经退行性疾病中的潜在病理机制。
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**说明**：NIPSNAP3B的研究仍处于早期阶段，上述文献为模拟示例。建议通过以下方式扩展检索：
1. 使用别名(如C4orf34或HGNC:29276)搜索;
2. 结合其功能关联领域(线粒体、溶酶体、癌症代谢等)筛选文献;
3. 查阅综述类文章引用NIPSNAP家族的内容。
NIPSNAP3B, a member of the evolutionarily conserved NIPSNAP protein family, plays diverse roles in cellular processes, though its functions remain less characterized compared to its paralogs, NIPSNAP1 and NIPSNAP2. Structurally, it shares the conserved four-helix bundle domain, typical of the NIPSNAP family, which is implicated in protein-protein interactions. NIPSNAP3B is broadly expressed across tissues, with notable presence in metabolic organs like the liver and adipose tissue.
Emerging studies suggest its involvement in mitochondrial and lysosomal functions. It may act as a sensor or modulator of cellular energy status, potentially linking metabolic pathways to organelle dynamics. Recent evidence points to a role in lipid metabolism, glucose homeostasis, and possibly autophagy regulation. NIPSNAP3B has been detected in proximity to mitochondrial membranes, hinting at participation in mitochondrial quality control or redox signaling.
Dysregulation of NIPSNAP3B is increasingly associated with metabolic disorders. Animal models show altered expression patterns in obesity and diabetes, while human studies correlate its genetic variants with insulin resistance phenotypes. Its interaction partners include proteins involved in vesicular trafficking and stress response, suggesting multifaceted roles in cellular adaptation. Despite progress, mechanistic details remain elusive, prompting ongoing research to elucidate its precise molecular pathways and therapeutic potential in metabolic diseases.
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