| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ANKRD27 |
| Uniprot No | Q96NW4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1050aa |
| 氨基酸序列 | MALYDEDLLKNPFYLALQKCRPDLCSKVAQIHGIVLVPCKGSLSSSIQSTCQFESYILIPVEEHFQTLNGKDVFIQGNRIKLGAGFACLLSVPILFEETFYNEKEESFSILCIAHPLEKRESSEEPLAPSDPFSLKTIEDVREFLGRHSERFDRNIASFHRTFRECERKSLRHHIDSANALYTKCLQQLLRDSHLKMLAKQEAQMNLMKQAVEIYVHHEIYNLIFKYVGTMEASEDAAFNKITRSLQDLQQKDIGVKPEFSFNIPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSLAKDELGYCLTSFEAAIEYIRQGSLSAKPPESEGFGDRLFLKQRMSLLSQMTSSPTDCLFKHIASGNQKEVERLLSQEDHDKDTVQKMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYDVESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSVMEAYHLSFERRQKSSEAPVQSPQRSVDSISQESSTSSFSSMSASSRQEETKKDYREVEKLLRAVADGDLEMVRYLLEWTEEDLEDAEDTVSAADPEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCAEQNSKIMELLQVVPSCVASLDDVAETDRKEYVTVKIRKKWNSKLYDLPDEPFTRQFYFVHSAGQFKGKTSREIMARDRSVPNLTEGSLHEPGRQSVTLRQNNLPAQSGSHAAEKGNSDWPERPGLTQTGPGHRRMLRRHTVEDAVVSQGPEAAGPLSTPQEVSASRS |
| 分子量 | 143.4 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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ANKRD27的3条参考文献示例(基于知识库总结，非真实文献)：
1. **文献名称**: *ANKRD27 regulates EGFR trafficking through its VPS9 domain*
**作者**: Saito K, et al.
**摘要**: 本研究揭示了ANKRD27通过其VPS9结构域与早期内体中的Rab7 GTP酶相互作用，调控表皮生长因子受体(EGFR)的胞内运输过程，从而影响EGFR的溶酶体降解和信号传导活性。
2. **文献名称**: *ANKRD27 interacts with the retromer complex in endosomal protein sorting*
**作者**: Chen L, et al.
**摘要**: 该研究通过蛋白质组学分析发现ANKRD27与逆向转运复合体(retromer)亚基VPS35特异性结合，参与内体-高尔基体逆向运输途径，并证明其功能缺失导致细胞中脂质稳态异常。
3. **文献名称**: *Downregulation of ANKRD27 correlates with poor prognosis in colorectal cancer*
**作者**: Wang Y, et al.
**摘要**: 该临床研究显示，ANKRD27在结直肠癌组织中表达显著降低，其低表达与患者总生存期缩短相关。机制研究表明ANKRD27可能通过调控Wnt/β-catenin通路抑制肿瘤转移。
注：以上文献为基于ANKRD27已知功能(如VPS9结构域、内体运输、癌症关联)构建的模拟摘要，实际研究请通过PubMed或Google Scholar检索具体文献。
Ankyrin Repeat Domain-containing Protein 27 (ANKRD27) is a member of the ankyrin repeat family, characterized by conserved 33-amino acid motifs that mediate protein-protein interactions. It is primarily localized to the trans-Golgi network (TGN) and endosomal compartments, where it functions as a regulatory scaffold. ANKRD27 is known to interact with the retromer complex component VPS26A and the sorting receptor SorLA (SORL1), suggesting roles in intracellular trafficking, cargo sorting, and vesicular transport. These processes are critical for maintaining cellular homeostasis, receptor recycling, and synaptic function in neurons.
Studies link ANKRD27 to neurological disorders, particularly Alzheimer’s disease, through its association with SorLA, which regulates amyloid precursor protein (APP) processing. Dysregulation of ANKRD27 may contribute to aberrant APP trafficking and amyloid-β accumulation. Additionally, ANKRD27 has been implicated in cancer, with elevated expression observed in glioblastoma and colorectal tumors, though its mechanistic role remains unclear. Post-translational modifications, such as phosphorylation and SUMOylation, further modulate its activity and subcellular localization.
Despite progress, ANKRD27's full functional scope is not well-defined. Current research focuses on its interplay with trafficking pathways, disease-related mutations (e.g., in VPS26A), and potential as a therapeutic target. Its dual roles in membrane dynamics and disease pathways underscore its biological significance but highlight the need for deeper mechanistic exploration.
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