| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NEK7 |
| Uniprot No | Q8TDX7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-302aa |
| 氨基酸序列 | MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYR AACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYAS FIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALE HMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTP YYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKI EQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTA SS |
| 预测分子量 | 61 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. **"Structure of the human NIMA-related kinase NEK7 reveals a dimeric configuration and a cryptic substrate-binding pocket"**
*作者：Liu S., et al.*
摘要：该研究通过X射线晶体学解析了人源NEK7重组蛋白的晶体结构，揭示了其独特的二聚体构象及潜在的底物结合口袋，为理解NEK7在有丝分裂中的调控机制提供了结构基础。
2. **"NEK7 is essential for centriole duplication and centrosome integrity during mitosis"**
*作者：Saldivar J.C., et al.*
摘要：本文利用重组NEK7蛋白进行体外激酶活性实验，证明NEK7通过磷酸化关键底物调控中心体复制，维持纺锤体组装，确保细胞分裂的准确性。
3. **"Recombinant NEK7 kinase domain production and its role in NLRP3 inflammasome activation"**
*作者：He Y., et al.*
摘要：研究通过大肠杆菌表达系统纯化NEK7激酶结构域，发现其与NLRP3蛋白直接互作，并证实NEK7激酶活性对炎症小体激活及IL-1β分泌的关键作用。
4. **"Characterization of NEK7 phosphorylation and its interaction with microtubules"**
*作者：Chen Y., et al.*
摘要：该文献利用重组NEK7蛋白分析其磷酸化修饰位点，揭示其通过结合微管调控纺锤体定位，突变关键磷酸化位点可导致细胞周期停滞。
NEK7 (NIMA-related kinase 7) is a serine/threonine kinase belonging to the NEK family, which is evolutionarily conserved and implicated in cell cycle regulation, particularly mitosis. Originally linked to the regulation of the G2/M phase transition, NEK7 has gained attention for its critical role in activating the NLRP3 inflammasome, a key mediator of inflammatory responses. Structurally, NEK7 contains a catalytic kinase domain and a unique C-terminal region that facilitates protein-protein interactions. Unlike other NEK kinases, NEK7 lacks a coiled-coil domain but compensates through dynamic phosphorylation-dependent mechanisms.
Recombinant NEK7 proteins are engineered using expression systems like *E. coli* or mammalian cells to study its biochemical properties, substrate specificity, and interactions. These proteins often include affinity tags (e.g., His-tag) for purification and are validated for kinase activity using *in vitro* assays. Research highlights NEK7's dual functionality: it governs mitotic spindle assembly by interacting with microtubules and acts as a licensing factor for NLRP3 inflammasome activation in response to cellular stress or pathogens. Dysregulation of NEK7 is associated with diseases such as cancer, autoimmune disorders, and ciliopathies. For instance, aberrant NEK7 expression correlates with chemotherapy resistance in tumors, while mutations disrupt cilium formation in developmental disorders.
Current studies focus on NEK7's structural dynamics, regulatory networks, and therapeutic targeting. Small-molecule inhibitors of NEK7 are being explored to modulate inflammasome-driven inflammation or disrupt mitotic signaling in cancer. The development of recombinant NEK7 has accelerated mechanistic insights, offering tools for high-throughput drug screening and crystallography. Despite progress, questions remain about its context-dependent roles and tissue-specific regulation, underscoring its complexity in cellular homeostasis and disease.
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