| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DOK7 |
| Uniprot No | Q18PE1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-504aa |
| 氨基酸序列 | MTEAALVEGQ VKLRDGKKWK SRWLVLRKPS PVADCLLMLV YKDKSERIKG LRERSSLTLE DICGLEPGLP YEGLVHTLAI VCLSQAIMLG FDSHEAMCAW DARIRYALGE VHRFHVTVAP GTKLESGPAT LHLCNDVLVL ARDIPPAVTG QWKLSDLRRY GAVPSGFIFE GGTRCGYWAG VFFLSSAEGE QISFLFDCIV RGISPTKGPF GLRPVLPDPS PPGPSTVEER VAQEALETLQ LEKRLSLLSH AGRPGSGGDD RSLSSSSSEA SHLDVSASSR LTAWPEQSSS SASTSQEGPR PAAAQAAGEA MVGASRPPPK PLRPRQLQEV GRQSSSDSGI ATGSHSSYSS SLSSYAGSSL DVWRATDELG SLLSLPAAGA PEPSLCTCLP GTVEYQVPTS LRAHYDTPRS LCLAPRDHSP PSQGSPGNSA ARDSGGQTSA GCPSGWLGTR RRGLVMEAPQ GSEATLPGPA PGEPWEAGGP HAGPPPAFFS ACPVCGGLKV NPPP |
| 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DOK7重组蛋白的模拟参考文献示例(内容为模拟，建议通过学术数据库验证)：
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1. **标题**: *DOK7 Recombinant Protein Enhances Neuromuscular Junction Formation in vitro*
**作者**: Beeson D, Higuchi O, Yamanashi Y
**摘要**: 研究通过表达DOK7重组蛋白，证明其能够促进体外培养的神经肌肉接头(NMJ)的形成。实验表明，DOK7通过激活MuSK酪氨酸激酶信号通路，调控突触相关基因的表达，为先天性肌无力综合征的治疗提供潜在策略。
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2. **标题**: *Structural and Functional Analysis of DOK7 Phosphotyrosine-Binding Domain*
**作者**: Okada K, Inoue A
**摘要**: 通过重组DOK7蛋白的晶体结构解析，揭示了其磷酸酪氨酸结合域(PTB)的关键作用。研究发现该结构域与MuSK激酶特异性结合，并阐明了DOK7在NMJ发育中自我聚集以激活下游信号的分子机制。
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3. **标题**: *Gene Therapy Using DOK7 Recombinant Protein Rescues Myasthenic Phenotypes in Mice*
**作者**: Arimura S, Ohno K
**摘要**: 利用携带DOK7重组蛋白的腺相关病毒(AAV)治疗DOK7缺陷型小鼠，显著改善肌肉无力和NMJ结构异常。研究为DOK7相关先天性肌无力的基因治疗提供了临床前证据。
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4. **标题**: *DOK7 Recombinant Protein Activates MuSK-Dependent Signaling in Muscle Cells*
**作者**: Bergamin E, Burden SJ
**摘要**: 通过体外实验证实，重组DOK7蛋白通过诱导MuSK二聚化并自磷酸化，激活下游ERK和AKT信号通路，从而促进肌管分化。研究强调了DOK7在肌肉发育中的核心调控作用。
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**注意**：以上文献信息为基于领域知识的模拟内容，实际文献请通过 **PubMed/Google Scholar** 检索关键词如“DOK7 recombinant protein”或“DOK7 MuSK”获取。
DOK7 (Docking Protein 7) is a cytoplasmic adaptor protein crucial for the formation and maintenance of the neuromuscular junction (NMJ), the synapse between motor neurons and skeletal muscle. It belongs to the DOK family of proteins, which mediate signal transduction by recruiting downstream effectors through phosphotyrosine-binding (PTB) and pleckstrin homology (PH) domains. DOK7 is specifically required for the activation and clustering of the muscle-specific receptor tyrosine kinase (MuSK), a key regulator of NMJ development. Upon agrin signaling, DOK7 interacts with MuSK to initiate autophosphorylation and downstream signaling cascades, leading to acetylcholine receptor (AChR) clustering and synaptic stability.
Mutations in the *DOK7* gene are linked to congenital myasthenic syndromes (CMS), a group of disorders characterized by muscle weakness and fatigability due to impaired NMJ transmission. Most pathogenic variants are autosomal recessive, disrupting DOK7-MuSK interactions or impairing its tyrosine phosphorylation sites. This highlights DOK7's essential role in neuromuscular signaling and its potential as a therapeutic target.
Recombinant DOK7 protein, typically produced in mammalian expression systems (e.g., HEK293 cells), retains functional domains necessary for MuSK binding and signaling. It is widely used in *in vitro* studies to investigate NMJ assembly, CMS mechanisms, and MuSK activation pathways. Additionally, recombinant DOK7 serves as a tool for drug screening aimed at enhancing NMJ function or compensating for pathogenic mutations. Recent research also explores its relevance in cancer biology, as aberrant DOK7 expression has been observed in certain tumors. The protein’s modular structure and signaling versatility make it a valuable subject for both basic research and translational applications in neurology and oncology.
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