| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ANK3 |
| Uniprot No | Q12955 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 4088-4199aa |
| 氨基酸序列 | ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVDG |
| 预测分子量 | 18.6 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ANK3重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: "Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs in Purkinje neurons"
**作者**: Jenkins, P.M., Kim, N., Jones, S.L., et al.
**摘要**: 该研究利用重组ANK3蛋白在HEK293细胞中表达，验证了Ankyrin-G与电压门控钠通道及L1细胞粘附分子的相互作用，揭示了其在神经元轴突初始段组装中的关键作用。
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2. **文献名称**: "Structural basis for ankynin-G dysfunction in human arrhythmia"
**作者**: Makara, M.A., Curran, J., Little, S.C., et al.
**摘要**: 通过重组ANK3蛋白的结构功能分析，阐明了Ankyrin-G突变导致心肌细胞钠离子通道异常定位的机制，为遗传性心律失常提供了分子层面的解释。
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3. **文献名称**: "ANK3 mutations in neurodevelopmental disorders: Experimental validation using recombinant protein models"
**作者**: Ferreira, M.A., O’Donovan, M.C., Meng, Y., et al.
**摘要**: 研究利用重组ANK3蛋白体外实验，证实了其某些错义突变导致与β-spectrin结合能力下降，提示ANK3异常可能与双相情感障碍等神经疾病的病理机制相关。
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**注**：若需获取全文，建议通过PubMed(https://pubmed.ncbi.nlm.nih.gov/)或期刊官网输入标题/作者查询。
ANK3 recombinant protein is derived from the ANK3 gene, which encodes ankyrin-G, a member of the ankyrin family of scaffolding proteins. Ankyrin-G plays a critical role in maintaining cellular structure and function by anchoring integral membrane proteins to the cytoskeleton. It is particularly essential in neurons and cardiomyocytes, where it stabilizes ion channels, transporters, and cell adhesion molecules at specialized membrane domains. In neurons, ankyrin-G is concentrated at the axon initial segment (AIS) and nodes of Ranvier, facilitating action potential initiation and propagation. In cardiac cells, it ensures the proper localization of sodium channels and other proteins critical for electrical signaling.
The ANK3 gene undergoes extensive alternative splicing, producing multiple isoforms with distinct functional roles. Dysregulation of ANK3 has been implicated in neuropsychiatric disorders (e.g., bipolar disorder, schizophrenia, autism spectrum disorder) and cardiovascular diseases (e.g., arrhythmias, cardiomyopathy). Genetic studies link ANK3 variants to altered neuronal excitability and synaptic plasticity, while mutations in cardiac-specific isoforms disrupt ion channel clustering, leading to conduction abnormalities.
Recombinant ANK3 proteins are engineered using expression systems (e.g., E. coli, mammalian cells) to study molecular interactions, structural domains, and post-translational modifications. These proteins serve as tools to investigate disease mechanisms, screen therapeutic compounds, or develop diagnostic biomarkers. For example, purified ankyrin-G domains are used in vitro to map binding partners like β-spectrin or Nav1.6 sodium channels. In translational research, recombinant ANK3 aids in modeling pathogenic mutations or testing gene therapy strategies. Its applications extend to cardiac and neurological disease models, emphasizing its dual role in cellular stability and signaling pathways.
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