Specific for ~29k AQP2 protein phosphorylated at Ser261. Also recognizes the glycosylated form of AQP2 at ~ 37k. Immunolabeling of the AQP2 band is blocked by preadsorption with the phospho-peptide used as antigen but not by the corresponding dephospho-peptide.
Cross-Reactivity
Mouse (Murine), Rat (Rattus)
Predicted Reactivity
bovine, canine, chicken, human, non-human primate
Purification
Antigen Affinity Purified from Pooled Serum
Immunogen
Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser261 conjugated to KLH
Aquaporin 2 (AQP2) is a hormonally regulated water channel located in the renal collecting duct. Mutations in the AQP2 gene cause hereditary nephrogenic diabetes insipidus in humans (Iolascon et al.,2007). A vasopressin induced cAMP increase results in the phosphorylation of AQP2 at serine-256 and its translocation from the intracellular vesicles to the apical membrane of principal cells (van Balkom et al., 2002). Recently, serine-261 has been identified as a novel phosphorylation site on AQP2 and levels of phosphorylated S261 have been shown to decrease with vasopressin treatment suggesting its involvement in vasopressin-dependent AQP2 trafficking (Hoffert et al., 2007). Anti-Phospho-Ser261 Aquaporin 2 Western blot of rat kidney lysate showing specific immunolabeling of the ~ 29k and 37k glycosylated form of the AQP2 protein phosphorylated at Ser261. Immunolabeling is blocked by the phospho-peptide used as antigen (peptide) but not by the corresponding dephospho-peptide (not shown).