| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DPP6 |
| Uniprot No | P42658 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-865aa |
| 氨基酸序列 | MASLYQRFTGKINTSRSFPAPPEASHLLGGQGPEEDGGAGAKPLGPRAQAAAPRERGGGGGGAGGRPRFQYQARSDGDEEDELVGSNPPQRNWKGIAIALLVILVICSLIVTSVILLTPAEDNSLSQKKKVTVEDLFSEDFKIHDPEAKWISDTEFIYREQKGTVRLWNVETNTSTVLIEGKKIESLRAIRYEISPDREYALFSYNVEPIYQHSYTGYYVLSKIPHGDPQSLDPPEVSNAKLQYAGWGPKGQQLIFIFENNIYYCAHVGKQAIRVVSTGKEGVIYNGLSDWLYEEEILKTHIAHWWSPDGTRLAYAAINDSRVPIMELPTYTGSIYPTVKPYHYPKAGSENPSISLHVIGLNGPTHDLEMMPPDDPRMREYYITMVKWATSTKVAVTWLNRAQNVSILTLCDATTGVCTKKHEDESEAWLHRQNEEPVFSKDGRKFFFIRAIPQGGRGKFYHITVSSSQPNSSNDNIQSITSGDWDVTKILAYDEKGNKIYFLSTEDLPRRRQLYSANTVGNFNRQCLSCDLVENCTYFSASFSHSMDFFLLKCEGPGVPMVTVHNTTDKKKMFDLETNEHVKKAINDRQMPKVEYRDIEIDDYNLPMQILKPATFTDTTHYPLLLVVDGTPGSQSVAEKFEVSWETVMVSSHGAVVVKCDGRGSGFQGTKLLHEVRRRLGLLEEKDQMEAVRTMLKEQYIDRTRVAVFGKDYGGYLSTYILPAKGENQGQTFTCGSALSPITDFKLYASAFSERYLGLHGLDNRAYEMTKVAHRVSALEEQQFLIIHPTADEKIHFQHTAELITQLIRGKANYSLQIYPDESHYFTSSSLKQHLYRSIINFFVECFRIQDKLLTVTAKEDEEED |
| 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. |
以下是关于DPP6重组蛋白的3篇参考文献摘要(基于公开研究内容模拟整理)：
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1. **文献名称**：*Structural Insights into DPP6-Mediated Modulation of Kv4 Channel Inactivation*
**作者**：Strop, P., et al.
**摘要**：该研究通过X射线晶体学解析了重组DPP6胞外结构域的三维结构，揭示了其与Kv4钾通道相互作用的分子基础，阐明了DPP6通过稳定通道开放态延缓失活的调控机制。
2. **文献名称**：*DPP6 Enhances Kv4.2 Channel Surface Expression and Gating Kinetics in a Heterologous System*
**作者**：Nadal, M.S., et al.
**摘要**：利用HEK293细胞表达重组DPP6与Kv4.2通道，研究发现DPP6显著提高通道蛋白的膜定位并加速其激活/失活动力学，表明其在调节神经元兴奋性中的关键作用。
3. **文献名称**：*DPP6 Isoforms Differentially Modulate Amyloid-β Neurotoxicity in Alzheimer's Models*
**作者**：Jerng, H.H., et al.
**摘要**：通过重组DPP6不同剪接变体在细胞模型中的表达，发现特定异构体可减轻β淀粉样蛋白诱导的神经元凋亡，提示DPP6在阿尔茨海默病病理中的潜在保护机制。
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*注：以上文献信息为模拟示例，实际引用时需以真实发表论文为准。建议通过PubMed或Web of Science查询最新研究。*
DPP6 (Dipeptidyl Peptidase-Like Protein 6), also known as dipeptidyl aminopeptidase-related protein, is a member of the serine protease family that lacks enzymatic activity due to amino acid substitutions in its catalytic domain. It is primarily recognized as an auxiliary subunit of voltage-gated potassium (Kv) channels, particularly Kv4 family channels, which regulate neuronal excitability and cardiac action potential repolarization. DPP6 modulates the biophysical properties of Kv4 channels by accelerating their inactivation kinetics and enhancing surface expression, thereby influencing electrical signaling in the brain and heart.
The recombinant DPP6 protein is engineered using heterologous expression systems (e.g., mammalian cells, insect cells, or E. coli) to produce purified, functional forms for research. Its structure typically includes extracellular domains critical for interactions with Kv4 channels, while transmembrane and cytoplasmic regions mediate regulatory effects. Recombinant DPP6 enables mechanistic studies of channel regulation, structural analyses (e.g., cryo-EM or X-ray crystallography), and drug discovery targeting channelopathies.
DPP6 has been implicated in neurological disorders (e.g., Alzheimer’s disease, autism spectrum disorders) and cardiac arrhythmias (e.g., Brugada syndrome). Dysregulation of DPP6-Kv4 complexes may disrupt ion homeostasis, contributing to pathological electrical activity. Research using recombinant DPP6 aids in elucidating its role in disease pathogenesis and developing therapeutic strategies. Additionally, DPP6 serves as a potential biomarker for neurodegenerative conditions, with its expression levels correlating with disease progression in preclinical models. Ongoing studies focus on its tissue-specific splicing variants and post-translational modifications, which may refine its functional diversity in different physiological contexts.
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