|Application ||WB, IHC-P, E|
|Calculated MW||198416 Da|
|Antigen Region||1586-1616 aa|
|Other Names||Serine/threonine-protein kinase WNK3, Protein kinase lysine-deficient 3, Protein kinase with no lysine 3, WNK3, KIAA1566, PRKWNK3|
|Target/Specificity||This WNK3 (PRKWNK3) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1586-1616 amino acids from the C-terminal region of human WNK3 (PRKWNK3).|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||WNK3 (PRKWNK3) Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively (PubMed:16275913, PubMed:16275911, PubMed:16357011). Phosphorylates WNK4. Regulates the phosphorylation of SLC12A1 and SLC12A2. Increases Ca(2+) influx mediated by TRPV5 and TRPV6 by enhancing their membrane expression level via a kinase-dependent pathway (PubMed:18768590). Inhibits the activity of KCNJ1 by decreasing its expression at the cell membrane in a non-catalytic manner.|
|Tissue Location||Expressed in brain, lung, kidney, liver and pancreas, and in fetal tissues including placenta, fetal brain, lung and kidney. Very low levels of expression were also detected in fetal heart, thymus, liver and spleen. Isoform 1 is brain- specific. Isoform 3 is kidney-specific|
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Provided below are standard protocols that you may find useful for product applications.
Members of the 'with no lysine' (WNK) kinase family, such as WNK3, are serine-threonine protein kinases that lack the almost invariant catalytic lysine in subdomain II, which is important for binding ATP in the catalytic site. Instead, these kinases have a conserved lysine in subdomain I that is thought to provide this function (Holden et al., 2004 [PubMed 15194194]).[supplied by OMIM]
Verissimo, F., et al., Oncogene 20(39):5562-5569 (2001).
Nagase, T., et al., DNA Res. 7(4):273-281 (2000).
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