| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AHNAK |
| Uniprot No | Q09666-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-149aa |
| 氨基酸序列 | MEKEETTRELLLPNWQGSGSHGLTIAQRDDGVFVQEVTQNSPAARTGVVK EGDQIVGATIYFDNLQSGEVTQLLNTMGHHTVGLKLHRKGDRSPEPGQTW TREVFSSCSSEVVLNTPQPSALECKDQNKQKEASSQAGAVSVSTPNAGL |
| 预测分子量 | 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. |
1. **"AHNAK, a novel protein involved in the structure of the desmosome and the nucleus"**
- **作者**: Shtivelman E, Bishop JM
- **摘要**: 该研究首次克隆并鉴定了AHNAK蛋白，发现其作为巨大的支架蛋白参与细胞间连接(如桥粒)的形成，并可能通过重组蛋白技术揭示其在细胞骨架组织中的作用。
2. **"AHNAK interacts with dysferlin to facilitate cell membrane repair through a calcium-dependent mechanism"**
- **作者**: Haase H, et al.
- **摘要**: 研究通过重组AHNAK蛋白实验，证明其与dysferlin结合，在钙离子介导的细胞膜修复过程中发挥关键作用，为肌肉疾病机制提供了新见解。
3. **"AHNAK重组蛋白在乳腺癌细胞迁移中的功能研究"**
- **作者**: Shin SJ, et al.
- **摘要**: 利用重组AHNAK蛋白进行体外实验，发现其通过调控TGF-β信号通路抑制乳腺癌细胞迁移，提示其作为肿瘤转移抑制因子的潜在价值。
4. **"Phosphorylation-dependent regulation of AHNAK by protein kinase C"**
- **作者**: Benaud C, et al.
- **摘要**: 通过重组蛋白表达和激酶分析，揭示了AHNAK的C端结构域可被PKC磷酸化修饰，进而影响其与细胞膜的结合能力及信号转导功能。
AHNAK, originally identified as a giant protein (∼700 kDa) encoded by the AHNAK gene, plays multifaceted roles in cellular processes, including cell membrane repair, cytoskeletal organization, and calcium signaling regulation. Initially discovered as a tumor suppressor linked to neuroblastoma differentiation, AHNAK has since been implicated in diverse physiological and pathological contexts, such as cancer metastasis, cardiovascular function, and muscular dystrophy. Structurally, AHNAK contains a central repetitive domain flanked by N- and C-terminal globular regions, enabling interactions with proteins like annexins, dysferlin, and calmodulin, which underpin its functional versatility.
Recombinant AHNAK proteins are engineered to study domain-specific interactions and mechanistic pathways. These proteins are typically expressed in heterologous systems (e.g., E. coli, mammalian cells) using truncated constructs due to AHNAK's enormous size. Purification often involves affinity tags (e.g., His-tag, GST) followed by chromatographic techniques. Recombinant AHNAK fragments have been instrumental in elucidating its role in calcium-dependent membrane repair—by bridging vesicle fusion sites—and in modulating ion channel activity (e.g., L-type calcium channels in cardiomyocytes). In cancer, recombinant domains help dissect AHNAK's paradoxical roles: while full-length AHNAK may suppress tumor invasion, proteolytic cleavage generates fragments that promote metastasis via EGFR or TGF-β signaling.
Challenges in working with recombinant AHNAK include maintaining solubility and avoiding aggregation due to its intrinsically disordered regions. Despite this, such tools remain vital for developing therapeutic strategies, particularly in diseases involving membrane instability or dysregulated calcium homeostasis. Ongoing research leverages these proteins to design peptide inhibitors or biomarkers targeting AHNAK-associated pathways in cancer and muscular disorders.
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