L’anticorps Lapin Polyclonal anti-AQP2 a été validé pour WB et IHC. Il convient pour détecter AQP2 dans des échantillons de Rat. Il y a 2+ publications disponibles.
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.
Réactivité croisée
Souris, Rat (Rattus)
Homologie
bovine, canine, chicken, human, non-human primate
Purification
Antigen Affinity Purified from Pooled Serum
Immunogène
Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser261 conjugated to KLH
AQP2
Reactivité: Rat
WB, IHC, IF, ICC
Hôte: Lapin
Polyclonal
HRP
Indications d'application
Recommended Dilution: WB: 1:1000 Quality Control: Western blots performed on each lot.
Restrictions
For Research Use only
Format
Liquid
Buffer
100 μL in 10 mM HEPES ( pH 7.5), 150 mM NaCl, 100 μg per ml BSA and 50 % glycerol.
Stock
-20 °C
Hoffert, Fenton, Moeller, Simons, Tchapyjnikov, McDill, Yu, Pisitkun, Chen, Knepper: "Vasopressin-stimulated increase in phosphorylation at Ser269 potentiates plasma membrane retention of aquaporin-2." dans: The Journal of biological chemistry, Vol. 283, Issue 36, pp. 24617-27, (2008) (PubMed).
Hoffert, Nielsen, Yu, Pisitkun, Schleicher, Nielsen, Knepper: "Dynamics of aquaporin-2 serine-261 phosphorylation in response to short-term vasopressin treatment in collecting duct." dans: American journal of physiology. Renal physiology, Vol. 292, Issue 2, pp. F691-700, (2007) (PubMed).
Antigène
AQP2
(Aquaporin 2 (Collecting Duct) (AQP2))
Autre désignation
AQP2
Sujet
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).