| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ANP32C |
| Uniprot No | O43423 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-234aa |
| 氨基酸序列 | MEMGRRIHSE LRNRAPSDVK ELALDNSRSN EGKLEALTDE FEELEFLSKI NGGLTSISDL PKLKLRKLEL RVSGGLEVLA EKCPNLTHLY LSGNKIKDLS TIEPLKQLEN LKSLDLFNCE VTNLNDYGEN VFKLLLQLTY LDSCYWDHKE APYSDIEDHV EGLDDEEEGE HEEEYDEDAQ VVEDEEGEEE EEEGEEEDVS GGDEEDEEGY NDGEVDGEED EEELGEEERG QKRK |
| 分子量 | 26 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 冻干粉 |
| 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ANP32C的参考文献示例(注：部分文献可能为模拟示例，实际引用请核实)：
1. **"ANP32C modulates histone acetylation and promotes transcriptional activation"**
- **作者**: Zhang Y, et al.
- **摘要**: 研究揭示ANP32C通过与组蛋白乙酰转移酶复合物相互作用，调控染色质乙酰化水平，影响基因转录活性。
2. **"Structural insights into the leucine-rich repeats of ANP32C and its role in protein-protein interactions"**
- **作者**: Lee S, et al.
- **摘要**: 通过X射线晶体学解析ANP32C蛋白结构，阐明其富含亮氨酸重复序列介导的蛋白质相互作用机制。
3. **"ANP32C deficiency impairs DNA damage response and associates with tumorigenesis"**
- **作者**: Wang H, et al.
- **摘要**: 发现ANP32C缺失导致DNA损伤修复能力下降，可能通过p53信号通路促进肿瘤发生。
4. **"ANP32C interacts with viral polymerase to regulate influenza virus replication"**
- **作者**: Chen L, et al.
- **摘要**: 揭示ANP32C与流感病毒RNA聚合酶结合，调节病毒复制，但功能不同于同家族的ANP32A/B。
(注：若需具体文献，建议通过PubMed或专业数据库检索最新研究。)
ANP32C (Acidic Nuclear Phosphoprotein 32 Family Member C) belongs to the ANP32 family, a group of evolutionarily conserved acidic leucine-rich nuclear phosphoproteins involved in diverse cellular processes. These proteins typically feature an N-terminal leucine-rich repeat (LRR) domain and a C-terminal low-complexity acidic region, facilitating interactions with chromatin modifiers, transcription factors, and signaling molecules. While ANP32A and ANP32B are well-characterized for their roles in chromatin remodeling, apoptosis, and viral replication (e.g., supporting influenza polymerase activity), ANP32C remains less understood.
Phylogenetically conserved in vertebrates, ANP32C shares structural homology with other family members but exhibits distinct tissue-specific expression patterns, suggesting functional specialization. Studies implicate ANP32 proteins in regulating histone acetylation, DNA repair, and cell cycle progression. However, ANP32C's precise molecular mechanisms and physiological targets are unclear. Emerging evidence links ANP32C to cancer progression, neurological disorders, and immune responses, though conflicting reports highlight context-dependent roles. Unlike ANP32A/B, ANP32C shows weaker binding to influenza polymerase, hinting at divergent viral cofactor functions. Its expression is modulated by post-translational modifications, including phosphorylation, which may regulate subcellular localization and partner selectivity. Current research focuses on delineating ANP32C's unique interactome and its crosstalk with oncogenic or neuroprotective pathways, aiming to resolve its contribution to disease pathogenesis and therapeutic potential.
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