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Recombinant Human Serine/threonine-protein kinase WNK3 (EC 2.7.11.1) Fragment (aa 135-495) is a high-purity protein encompassing the complete protein kinase domain (aa 147-405). This fragment serves as an essential tool for investigating kinase activity, regulatory mechanisms in electrolyte homeostasis, and cellular responses to osmotic stress, enabling focused functional and structural studies.

Serine/threonine-protein kinase WNK3 is a key component of the WNK3-SPAK/OSR1 kinase cascade, crucial for regulating electrolyte balance and cellular volume under hyperosmotic stress. It functions as a molecular crowding sensor by undergoing liquid-liquid phase separation to form membraneless compartments, concentrating and activating downstream kinases OXSR1/OSR1 and STK39/SPAK. These kinases modulate ion cotransporters (e.g., SLC12A family members), promoting ion influx via Na-K-Cl cotransporters and inhibiting efflux via K-Cl cotransporters. WNK3 also acts as a scaffold, influencing membrane localization of transporters and channels like KCNJ1 and SLC26A9, and enhances Ca²⁺ influx through TRPV5/TRPV6. Predominantly cytoplasmic, it localizes to stress-induced membraneless compartments. This fragment retains the kinase domain, enabling targeted research into phosphorylation-dependent signaling and osmotic stress responses.