NEK7 Protein, Human (His-SUMO)

NEK7 Protein, a pivotal kinase, crucially drives mitotic cell cycle progression by enhancing centrosome microtubule nucleation, ensuring robust spindle formation, and aiding cytokinesis. Its phosphorylation of EML4 at 'Ser-146' facilitates chromosome congression. NEK7 extends its impact by phosphorylating RPS6KB1 and activating NLRP3 inflammasome assembly, promoting CASP1 activation. Independently, NEK7 unlocks NLRP3 within the microtubule organizing center, ensuring mutual exclusivity between inflammasome response and cell division by interacting with NEK9. These multifaceted functions position NEK7 as a key orchestrator in mitotic progression and the inflammasome response, highlighting its regulatory significance. NEK7 Protein, Human (His-SUMO) is the recombinant human-derived NEK7 protein, expressed by E. coli. The total length of NEK7 Protein, Human (His-SUMO) is 302 a.a., with molecular weight of 50 kDa.

NEK7 protein, a pivotal kinase, plays a crucial role in mitotic cell cycle progression by contributing to the microtubule nucleation activity of the centrosome, ensuring robust mitotic spindle formation, and facilitating cytokinesis. Its diverse functions include the phosphorylation of EML4 at 'Ser-146,' promoting dissociation from microtubules during mitosis and thereby facilitating efficient chromosome congression. NEK7 extends its impact beyond mitotic events by phosphorylating RPS6KB1 and serving as an essential activator of the NLRP3 inflammasome assembly. Independently of its kinase activity, NEK7 unlocks NLRP3 within the microtubule organizing center, promoting the formation of the NLRP3:PYCARD complex and activation of CASP1. Notably, NEK7 acts as a cellular switch, ensuring mutual exclusivity between the inflammasome response and cell division; its interaction with NEK9 prevents interaction with NLRP3 and inflammasome activation during mitosis. These multifaceted functions position NEK7 as a key orchestrator in both mitotic progression and the inflammasome response, highlighting its regulatory significance in diverse cellular processes.

The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.

Human

E. coli

Q8TDX7 (M1-S302)

140609

50 kDa

Greater than 90% as determined by reducing SDS-PAGE

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.