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Mouse Anti-AQP2 Recombinant Antibody (E-2) (CBMAB-A3358-YC)

Provided herein is a Mouse monoclonal antibody against Human Aquaporin 2. The antibody can be used for immunoassay techniques, such as WB, IP, IF, ELISA.
See all AQP2 antibodies
Published Data
Mouse Anti-AQP2 Recombinant Antibody (E-2) in IHC
Localization of follistatin protein and megalin, aquaporin 1 (AQP1), uromodulin (UMOD), or aquaporin 2 (AQP2) in ischemic kidneys was evaluated using serial sections. Cortex, CO; outer medulla, OM; inner medulla, IM. Bar = 50 μm. ...View More
Nagayama, I., Takayanagi, K., Hasegawa, H., & Maeshima, A. (2023). Tubule-Derived Follistatin Is Increased in the Urine of Rats with Renal Ischemia and Reflects the Severity of Acute Tubular Damage. Cells, 12(5), 801.
Mouse Anti-AQP2 Recombinant Antibody (E-2) in IF
Localization of β3-AR in the collecting duct, the thick ascending Limb and the proximal tubule in human kidney. Human kidney sections were stained with anti β3-AR antibodies (in red) and co-stained with antibodies against (A) AQP2, (B) NKCC2 and (C) AQP1 (all in green). Overlay shows the expression of β3-AR at the basolateral membrane of cells expressing apical AQP2 (collecting duct), apical NKCC2 (thick ascending limb) but not in the AQP1-expressing tubules (proximal tubule/descending limb). Magnification bar = 25 µm. ...View More
Milano, S., Maqoud, F., Rutigliano, M., Saponara, I., Carmosino, M., Gerbino, A., ... & Procino, G. (2023). β3 Adrenergic Receptor Agonist Mirabegron Increases AQP2 and NKCC2 Urinary Excretion in OAB Patients: A Pleiotropic Effect of Interest for Patients with X-Linked Nephrogenic Diabetes Insipidus. International Journal of Molecular Sciences, 24(2), 1136.
Mouse Anti-AQP2 Recombinant Antibody (E-2) in IF
TULP3 is required for trafficking of ARL13B- and ARL13B-dependent lipidated cargoes to mouse kidney epithelial cilia. Kidney sagittal sections at postnatal day 0, 5, or 24 were immunostained for ARL13B, acetylated tubulin (AcTUB) and Aquaporin 2 (AQP2) and counterstained for DNA. ...View More
Palicharla, V. R., Hwang, S. H., Somatilaka, B. N., Legué, E., Shimada, I. S., Familiari, N. E., ... & Mukhopadhyay, S. (2023). Interactions between TULP3 tubby domain and ARL13B amphipathic helix promote lipidated protein transport to cilia. Molecular biology of the cell, 34(3), ar18.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
E-2
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA

Basic Information

Immunogen
Amino acids 232-271 within a C-terminal cytoplasmic domain of AQP2 of human origin.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
IHC-P1:50-1:500
ELISA1:30-1:3,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Aquaporin 2
Introduction
AQP2 is a water channel protein located in the kidney collecting tubule. It belongs to the MIP/aquaporin family, some members of which are clustered together on chromosome 12q13. Mutations in this gene have been linked to autosomal dominant and recessive
Entrez Gene ID
Human359
Mouse11827
Rat25386
UniProt ID
HumanP41181
MouseP56402
RatP34080
Alternative Names
Aquaporin 2; Water Channel Protein For Renal Collecting Duct; Collecting Duct Water Channel Protein; Aquaporin 2 (Collecting Duct); ADH Water Channel; Aquaporin-CD;
Function
Forms a water-specific channel that provides the plasma membranes of renal collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient (PubMed:8140421, PubMed:7524315, PubMed:7510718, PubMed:15509592). Plays an essential role in renal water homeostasis (PubMed:8140421, PubMed:7524315, PubMed:15509592).
Biological Process
Cellular response to copper ion Source: UniProtKB
Cellular response to mercury ion Source: UniProtKB
Cellular response to water deprivation Source: Ensembl
Glycerol transport Source: UniProtKB
Metanephric collecting duct development Source: Ensembl
Protein homotetramerization Source: UniProtKB
Renal water homeostasis Source: UniProtKB
Renal water transport Source: Ensembl
Water transport Source: UniProtKB
Cellular Location
Apical cell membrane; Basolateral cell membrane; Cell membrane; Trans-Golgi network membrane; Cytoplasmic vesicle membrane. Shuttles from vesicles to the apical membrane (PubMed:15509592). Vasopressin-regulated phosphorylation is required for translocation to the apical cell membrane (PubMed:15509592). PLEKHA8/FAPP2 is required to transport AQP2 from the TGN to sites where AQP2 is phosphorylated (By similarity).
Involvement in disease
Diabetes insipidus, nephrogenic, autosomal (ANDI): A disorder caused by the inability of the renal collecting ducts to absorb water in response to arginine vasopressin. Characterized by excessive water drinking (polydipsia), excessive urine excretion (polyuria), persistent hypotonic urine, and hypokalemia. Inheritance can be autosomal dominant or recessive.
Topology
Cytoplasmic: 1-11 aa
Helical: 12-32 aa
Extracellular: 33-40 aa
Helical: 41-59 aa
Cytoplasmic: 60-64 aa
Discontinuously helical: 65-74 aa
Cytoplasmic: 75-85 aa
Helical: 86-107 aa
Extracellular: 108-127 aa
Helical: 128-148 aa
Cytoplasmic: 149-156 aa
Helical: 157-176 aa
Extracellular: 177-180 aa
Discontinuously helical: 181-193 aa
Extracellular: 194-201 aa
Helical: 202-222 aa
Cytoplasmic: 223-271 aa
PTM
Ser-256 phosphorylation is necessary and sufficient for expression at the apical membrane. Endocytosis is not phosphorylation-dependent.
N-glycosylated.

Ranieri, M., Di Mise, A., Centrone, M., D’Agostino, M., Tingskov, S. J., Venneri, M., ... & Tamma, G. (2021). Olive Leaf Extract (OLE) impaired vasopressin-induced aquaporin-2 trafficking through the activation of the calcium-sensing receptor. Scientific reports, 11(1), 1-13.

Kim, S., Jo, C. H., & Kim, G. H. (2021). Psychotropic drugs upregulate aquaporin-2 via vasopressin-2 receptor/cAMP/protein kinase A signaling in inner medullary collecting duct cells. American Journal of Physiology-Renal Physiology, 320(5), F963-F971.

Fenton, R. A., Murali, S. K., & Moeller, H. B. (2020). Advances in Aquaporin-2 trafficking mechanisms and their implications for treatment of water balance disorders. American Journal of Physiology-Cell Physiology, 319(1), C1-C10.

Ozer, E. S., Moeller, H. B., Karaduman, T., Fenton, R. A., & Mergen, H. (2020). Molecular characterization of an aquaporin-2 mutation causing a severe form of nephrogenic diabetes insipidus. Cellular and Molecular Life Sciences, 77(5), 953-962.

Ranieri, M., Di Mise, A., Tamma, G., & Valenti, G. (2019). Vasopressin–aquaporin-2 pathway: recent advances in understanding water balance disorders. F1000Research, 8.

Jung, H. J., & Kwon, T. H. (2019). New insights into the transcriptional regulation of aquaporin-2 and the treatment of X-linked hereditary nephrogenic diabetes insipidus. Kidney research and clinical practice, 38(2), 145.

Bräsen, J. H., Mederacke, Y. S., Schmitz, J., Diahovets, K., Khalifa, A., Hartleben, B., ... & Mederacke, I. (2019). Cholemic nephropathy causes acute kidney injury and is accompanied by loss of aquaporin 2 in collecting ducts. Hepatology, 69(5), 2107-2119.

Wu, Q., Moeller, H. B., Stevens, D. A., Sanchez-Hodge, R., Childers, G., Kortenoeven, M. L., ... & Fenton, R. A. (2018). CHIP regulates aquaporin-2 quality control and body water homeostasis. Journal of the American Society of Nephrology, 29(3), 936-948.

Roche, J. V., Survery, S., Kreida, S., Nesverova, V., Ampah-Korsah, H., Gourdon, M., ... & Törnroth-Horsefield, S. (2017). Phosphorylation of human aquaporin 2 (AQP2) allosterically controls its interaction with the lysosomal trafficking protein LIP5. Journal of Biological Chemistry, 292(35), 14636-14648.

Yui, N., Ando, F., Sasaki, S., & Uchida, S. (2017). Ser-261 phospho-regulation is involved in pS256 and pS269-mediated aquaporin-2 apical translocation. Biochemical and biophysical research communications, 490(3), 1039-1044.

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For research use only. Not intended for any clinical use.

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