Our Anti-Aquaporin 2 (Ser264) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects rat Aquaporin 2 (Ser264) and is antigen affinity purified from pooled serum. It is great for use in WB, IHC.
Western blot of rat kidney lysate showing specific immunolabeling of the ~29 kDa and 37 kDa glycosylated form of the AQP2 protein phosphorylated at Ser264 in the vasopressin (AVP) treated lane (+), but not in the control lane (-).
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-264 has been identified as a novel phosphorylation site on AQP2 and shown to be regulated by vasopressin thus implicating this site as important in AQP2 trafficking and subcellular distribution (Fenton RA et al., 2008).
Antigen Affinity Purified from Pooled Serum
Polyclonal
IgG
IHC, WB
Rabbit
AQP2
29/37 kDa
Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser264 of rat aquaporin 2, conjugated to keyhole limpet hemocyanin (KLH).
Human, Mouse, Rat
Bovine, Canine, Chicken, Non-Human Primate
AB_2492042
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Liquid
Prepared from pooled rabbit serum by affinity purification via sequential chromatography on phospho and non-phosphopeptide affinity columns.
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
WB: 1:1000
IHC: 1:100
Unconjugated
Specific for endogenous levels of the ~29 kDa AQP2 protein phosphorylated at Ser264. Also recognizes the glycosylated form of AQP2 at ~37 kDa. Immunolabeling is blocked by preadsorption with the phosphopeptide used as antigen, but not by the corresponding non-phosphopeptide.
Phosphorylated
Ser264
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
Blue Ice
ADH water channel antibody, AQP 2 antibody, AQP CD antibody, AQP-2 antibody, AQP-CD antibody, AQP2 antibody, AQP2_HUMAN antibody, AQPCD antibody, Aquaporin 2 collecting duct antibody, Aquaporin CD antibody, Aquaporin-2 antibody, Aquaporin-CD antibody, Aquaporin2 antibody, Aquaporine 2 antibody, Collecting duct water channel protein antibody, MGC34501 antibody, Water channel aquaporin 2 antibody, Water channel protein for renal collecting duct antibody, WCH CD antibody, WCH-CD antibody, WCHCD antibody
Fenton, R.A., et al. 2007. Acute regulation of aquaporin-2 phosphorylation at serine-264 by vasopressin. Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3134-9.
Sakai, M., et al. 2020. Phosphorylation profile of human AQP2 in urinary exosomes by LC–MS/MS phosphoproteomic analysis. Clinical and Experimental Nephrology, pp.1-8.
Sakai, M., et al. 2020. Phosphorylation profile of human AQP2 in urinary exosomes by LC–MS/MS phosphoproteomic analysis. Clinical and Experimental Nephrology, pp.1-8.
Lei, L., et al. 2018. Manganese promotes intracellular accumulation of AQP2 via modulating F-actin polymerization and reduces urinary concentration in mice. American Journal of Physiology-Renal Physiology, Oct 18: ajprenal-00391.
Lei, L., et al. 2018. Manganese promotes intracellular accumulation of AQP2 via modulating F-actin polymerization and reduces urinary concentration in mice. American Journal of Physiology-Renal Physiology, Oct 18:ajprenal-00391.
Al-Butaineh, M.M, et al. 2016. Activation of the Metabolic Sensor AMP-Activated Protein Kinase Inhibits Aquaporin-2 Function in Kidney Principal Cells. American Journal of Physiology-Renal Physiology, ajprenal-00308.
Hoffert, J.D., et al. 2014. Global analysis of the effects of the V2 receptor antagonist satavaptan on protein phosphorylation in collecting duct. American Journal of Physiology-Renal Physiology, 306(4), 410-421.
Hoffert, J.D., et al. 2007. Dynamics of aquaporin-2 serine-261 phosphorylation in response to short-term vasopressin treatment in collecting duct. Am J Physiol Renal Physiol 292: F691-F700.
