Aquaporin-3 (AQP3) Antibody Review





  • an efficient glycerol transporter. PMID: 17597824

  • a water/glycerol transporter expressed at the basolateral membrane of colonic epithelial cells. PMID: 17573386

  • a water/solute channel that can transport not only water but also various cryoprotectants. PMID: 17325454

  • the water- and glycerol-transporting protein. PMID: 17003427

  • the predominant aquaporin in human skin. PMID: 16918518

  • known as an integral membrane channel in epidermal keratinocytes, facilitates water and glycerol movement into and out of the skin. PMID: 16848764

  • a water/solute channel that can also transport various cryoprotectants. PMID: 16797525

  • a membrane protein, is known to permeabilize water and other small molecules such as glycerol and urea and is localized in the bowel, skin, kidney, and erythrocytes. PMID: 16651733

  • an aquaglyceroporin expressed in erythrocytes and several other tissues. PMID: 15456785

  • a recently described water channel that is also found in large airway cell membrane, could play a role in the pathogenesis and particularly that of bronchorrhea in bronchiectasis. PMID: 12556012

Normal Expression

  • In teleost gill, AQP3 is expressed in 'chloride' cells, and in some species, in other epithelial cell types, where it may have a number of different functions including the prevention of dehydration. In eel esophagus, immunohistochemistry shows that AQP3 is expressed in surface epithelial cells in the anterior esophagus, but in mucus cells within the epithelium of the posterior esophagus. In eel intestine, AQP3 is found in macrophage-like cells and probably plays no part in osmoregulatory processes. In the rectum, as in the posterior esophagus AQP3 is expressed in mucus cells. In eel kidney, AQP3 is expressed in a subset of renal tubules, and localizes to the apical pole of tubule cells. PMID: 17126580

  • In normal lung tissues, immunohistochemical expression of AQP3 was demonstrated in bronchial basal cells, alveolar type II cells, bronchiolar epithelial cells, and secretory cells of submucosal glands. PMID: 17056099

  • It has been shown that aquaporin-3, a water channel, is expressed in mouse embryos. This type of aquaporin transports not only water but also neutral solutes, including cell-permeating cryoprotectants. PMID: 16942765

  • AQP3 was found to be present in gill, kidney, liver, brain, heart, and spleen but not in whole blood. PMID: 16909214

  • AQP3 is abundantly expressed in keratinocytes of mammalian skin epidermis. Mice lacking AQP3 have dry skin and reduced SC hydration. PMID: 16872579

  • we demonstrate that AQP3 is also expressed in cultured human skin fibroblasts, which under normal wound healing processes migrate from surrounding tissues to close the wound. PMID: 16848764

  • Using IHC, we identified AQP3 protein expression in placenta syncytiotrophoblasts and cytotrophoblasts, chorion cytotrophoblasts, and amnion epithelia. PMID: 16638588

  • Aquaporin-1,3 were widely expressed in the cochlea and endolymphatic sac of guinea pig. PMID: 16494013

  • AQP3 is selectively expressed on the surface of basal cells. PMID: 16043462

  • In skin, the aquaglyceroporin AQP3 is expressed in the basal layer of epidermal keratinocytes. PMID: 15966863

  • Aquaporin-3 is expressed in developmental zebrafish embryos (Danio rerio). PMID: 15533783

  • AQP3 localizes to epithelial cells in the human small intestine and colon. PMID: 15375592

  • AQP3 is expressed not only in large airways, but also in bronchioles, and is related to water movement in pulmonary oedema. PMID: 15248066

  • AQP-2 and -3 circumferentially lined the epithelial cell membranes except for the apical membrane of the epithelial cells adjacent to the lumens of both ureter and bladder. PMID: 11997319

Abnormal Expression

  • In lung carcinomas, AQP3 expression was observed in 59 (70.2%) of 84 adenocarcinomas. Squamous cell carcinoma and large cell carcinoma had rather low positive ratios (35.8% and 13.4%, respectively). In adenocarcinomas, AQP3 was detected in all tumors of bronchioloalveolar subtype. Papillary subtype also showed a higher positive ratio of AQP3 compared with that in acinar and solid with mucin subtypes. In addition, AQP3 expression was related to tumor differentiation and clinical stage in adenocarcinomas. PMID: 17056099

  • Increased expression of AQP3 was found in eczema compared with healthy skin and this may contribute to water loss. PMID: 16918518


  • AQP3 water channels serve as an essential pathway for volume-regulatory water transport in, human epithelial cells. PMID: 16596446

  • AQP-3 may play an important functional role in osmoregulation the teleostean gill but is unlikely to be responsible for the increases in intestinal water absorption that occur following SW acclimation. PMID: 12151371



Immunoblotting (IB)

  • The expression of AQP2 and AQP3 was determined in the kidney by immunoblotting and immunohistochemistry. PMID: 17213730

  • Immunoblot analysis showed that glycosylated AQP3 protein was increased 4-10 h after treatment. PMID: 15248066

  • Immunoblot analysis showed that rabbit antibody against the human AQP3 reacted with a protein of approximately 30 kDa molecular weight in extracts of normal human skeletal muscles. PMID: 12769265

Immuno-Electron Microscopy (IEM)

  • Immunogold labelling electron microscopy revealed that the gold particles indicating the presence of AQP3 molecules were located mainly at the inside surface of muscle plasma membrane. PMID: 12769265

  • The water/small solute-transporting protein aquaporin-3 (AQP3) was found by immunofluorescence and immunogold electron microscopy to be expressed at the plasma membrane of epidermal keratinocytes in mouse skin. PMID: 11880378

Immunocytochemistry (ICC)

  • Light-microscopic immunocytochemistry of branchial epithelia revealed that tilapia AQP3 was expressed in gill chloride cells of FW- and SW-adapted tilapia. Electron-microscopic immunocytochemistry further demonstrated that tilapia AQP3 was localized in the basolateral membrane of gill chloride cells. PMID: 16000537

Immunohistochemistry (IHC)

  • By using immunohistochemical techniques applied to confocal microscopy, the presence of aquaporin 3 water channel in the epidermis of Triturus italicus (Amphibia, Urodela) has been shown. PMID: 17548266

  • AQP3 expression in human fetal membranes of normal term pregnancy was studied by reverse transcription polymerase chain reaction (RT-PCR) and immunohistochemistry (IHC). PMID: 16638588

  • Immunohistochemical examination revealed that AQP1 was expressed in endothelia, AQP3 in the basal cells of the large airways and in cuboidal cells in the bronchioles, AQP4 in the basolateral membrane of airway cells and AQP5 in type-I pneumocytes. PMID: 15248066

  • We have, therefore, performed this quantitative immunohistochemistry study on endobronchial biopsies to evaluate the expression and clinical relevance of AQP3 in patients with idiopathic bronchiectasis (n = 25, 15 F, 64.3 +/- 11.5 years) and control subjects (n = 14, 5 F, 57.5 +/- 12.0 years). PMID: 12556012

  • AQP3 protein was detected in the human peritoneal tissue by immunohistological staining using specific, affinity-purified polyclonal anti-AQP3 antibodies. PMID: 12234316

Immunoprecipitation (IP)

  • Using sucrose gradient centrifugation, immunoprecipitation analysis, and confocal microscopy, we found that aquaporin 3 and phospholipase D2 colocalized in caveolin-rich membrane microdomains. PMID: 14675200

Western Blot (WB)

  • The expression of AQP3 mRNA and protein was determined by Northern blot and Western blot, respectively. PMID: 12542607

  • Reverse transcriptase-polymerase chain reaction, Western analysis, and immunohistochemistry were used to determine expression and localization of AQP1 and AQP3. PMID: 12388974