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Product Name
Recombinant WNK1 protein (His tag)
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Description
Recombinant Human WNK1 Kinase Domain (aa 208-583) is a high-purity protein fragment encompassing the complete serine/threonine-protein kinase domain of WNK1. This product is engineered for researchers studying kinase activity, regulatory volume increase mechanisms, and blood pressure regulation pathways, providing a focused tool for structural and functional analyses.
WNK1 (With No Lysine [K] 1) is a key serine/threonine-protein kinase that functions as a molecular crowding sensor and central component of the WNK1-SPAK/OSR1 kinase cascade. It regulates blood pressure and cellular responses to hyperosmotic stress by undergoing liquid-liquid phase separation to form membraneless compartments, concentrating downstream kinases OXSR1/OSR1 and STK39/SPAK. This cascade phosphorylates ion cotransporters (SLC12A family) to promote ion influx during regulatory volume increase. Beyond this pathway, WNK1 phosphorylates substrates like SYT2 and PCF11 to regulate membrane binding and mRNA export, respectively, and acts as a scaffold protein to modulate transporters including SLC4A4 and TRPV4. The full-length protein localizes to the cytoplasm, nucleus, and mitotic spindle, with roles in angiogenesis, autophagy, and mitosis. The provided fragment (aa 208-583) contains the intact kinase domain (aa 221-479), enabling targeted investigation of WNK1's catalytic functions.
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Protein name
Serine/threonine-protein kinase WNK1
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Uniprot ID
Q9H4A3
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Gene Name
WNK1; HSN2; KDP; KIAA0344; PRKWNK1
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Source/Expression Host
E. coli
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Expression Plasmid/cDNA
DNA encoding 208-583 aa (Q9H4A3) were fused with 6His tag.
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Protein Species
Human
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Molecular weight
Predictes a molecular mass of 45.11 kDa. In SDS-PAGE under reducing conditions, it migrates as an approximately 50 kDa band.
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Purity
>89%, by SDS-PAGE with Coomassie Brilliant Blue staining.
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Activity
Not tested.
Related Products / Services
Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"