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AQP3 encodes the water channel protein aquaporin 3. Additionally we are shipping AQP3 Kits (43) and AQP3 Proteins (4) and many more products for this protein.
Showing 10 out of 112 products:
Human Polyclonal AQP3 Primary Antibody for ICC, IF - ABIN2486358
Gonen, Walz: The structure of aquaporins. in Quarterly reviews of biophysics 2006
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Human Polyclonal AQP3 Primary Antibody for ICC, IF - ABIN2486360
Knepper: The aquaporin family of molecular water channels. in Proceedings of the National Academy of Sciences of the United States of America 1994
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Human Polyclonal AQP3 Primary Antibody for ICC, IF - ABIN2486365
Sasaki, Ishibashi, Marumo: Aquaporin-2 and -3: representatives of two subgroups of the aquaporin family colocalized in the kidney collecting duct. in Annual review of physiology 1998
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Human Polyclonal AQP3 Primary Antibody for ICC, IF - ABIN2486366
Dibas, Mia, Yorio: Aquaporins (water channels): role in vasopressin-activated water transport. in Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.) 1998
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Cow (Bovine) Polyclonal AQP3 Primary Antibody for EIA, WB - ABIN2712108
Agre: The aquaporin water channels. in Proceedings of the American Thoracic Society 2006
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Human Polyclonal AQP3 Primary Antibody for IF (p), IHC (p) - ABIN673974
Zhang, Li, Liu, Guang, Yang, Mao, Zhu, Chen, Wang: The AQP-3 water channel and the ClC-3 chloride channel coordinate the hypotonicity-induced swelling volume in nasopharyngeal carcinoma cells. in The international journal of biochemistry & cell biology 2014
Enhanced water and cryoprotectant permeability of porcine oocytes after artificial expression of human and zebrafish aquaporin-3 channels.
Decreased glycerol efflux from the skeletal muscles in AQP3 knockout mice may result in low exercise capacity.
treatment of human HepG2 cells with TCDD also increased the expression of AQP3 mRNA and protein
AQP3-facilitated H2O2 transport is required for NF-kappaB (show NFKB1 Antibodies) activation in keratinocytes in the development of psoriasis.
Studied the effect of the total tannins extract of rhubarb on expression od aquaporin 2 (show AQP2 Antibodies) and auqaporin 3 in diarrhoea mice.
AQP3 has a pro-differentiative role in epidermal keratinocytes and PLD2 (show PLD2 Antibodies) activity is necessary for this effect.
analysis of the molecular link between the circadian clock and AQP3 function in mouse dorsal skin and HaCaT cells
In a mouse model of intestinal ischemia the level of miR (show MLXIP Antibodies)-874 expression was inversely related to AQP3 protein expression.
We therefore suggest that AQP3-mediated H(2)O(2) uptake is required for chemokine (show CCL1 Antibodies)-dependent T cell migration in sufficient immune response.
It was concluded that acyl-CoA binding protein (show DBI Antibodies) via aquaporin 3 is necessary for intact urine concentrating ability through efflux over the basolateral membrane of the collecting duct.
The results of this study suggest that Gypsum fibrosum plays an important role in the increased levels of cutaneous AQP3 expression enhanced by Byakkokaninjinto.
skin dryness observed in intrinsic and extrinsic aged skin may be explained, at least in part, by AQP3 downregulation. This may open new avenues sufficient to control skin texture and beauty. Its interaction in skin protein organization and gene polymorphism can also be tackled in future research
Data show that the expression of aquaporin (AQP) 1 (show AQP1 Antibodies), AQP3, AQP5 (show AQP5 Antibodies), epithelial Na+ channel (ENaC (show SCNN1A Antibodies)) and sodium potassium ATPase (show DNAH8 Antibodies) (Na-K-ATPase (show ATP1A1 Antibodies)) are altered in patients with acute respiratory failure (ARF (show CDKN2A Antibodies)) due to diffuse alveolar damage (DAD), and the cause of DAD does not seem to influence the level of impairment of these channels.
epigenetic signatures at AQP3 and SOCS3 (show SOCS3 Antibodies) engage in low-grade inflammation across different tissues, possible via JAK (show JAK3 Antibodies)/STAT (show STAT1 Antibodies) mediated pathways
RNA interference (RNAi) of aquaporin 3 (AQP3) retarded the growth and invasiveness of XWLC-05 lung cancer cells and decreased the activity of matrix metalloproteinase 2 (MMP2 (show MMP2 Antibodies)).
Taken together, our data, as a proof of principle, suggest that AQP3 can promote tumor growth of pancreatic cancer cells by activating the Mtor (show FRAP1 Antibodies) signaling pathway and provide a potential therapeutic target in the treatment of PDAC.
Aquaporins AQP3, -7, -8, and -11 proteins were found in sperm cells and localized in the head (AQP7 (show AQP7 Antibodies)), in the middle piece (AQP8 (show AQP8 Antibodies)) and in the tail (AQP3 and -11) in both the plasma membrane and in intracellular structures.
AQP3 was upregulated, and AQP7 (show AQP7 Antibodies) and AQP9 (show AQP7 Antibodies) were downregulated in hepatocellular carcinoma. A high expression of AQP3 and low expression of AQP7 (show AQP7 Antibodies) was significantly associated with the aggressive features of hepatocellular carcinoma.
AQP3 inhibition that induced glycerol uptake reduction and glycerol administration would rehabilitate the cell proliferation.
AQP3 increases in hepatocellular carcinoma. Auphen reduces AQP3 levels, suppressing tumor growth.
roles of AQP-3 in AQP-3 aquaglyceroporin and ClC-3 (show CLCN3 Antibodies) chloride channels complex
Data suggest that expression of AQP3 (aquaglyceroporin-3) in rumen mucosa can be modulated by dietary factors; here, AQP3 and UT-B (urea transporter B (show SLC14A1 Antibodies)) expression are upregulated with solid food intake (low-protein diet of plant forage) at weaning.
lack of AQP3 in bovine erythrocytes points to the lipid pathway as responsible for glycerol permeation and explains the low glycerol permeability and high E(a) for transport observed in ruminants.
The full length coding sequences of porcine (Sus scrofa) AQP3, 7 and 9 and the genomic sequence of AQP3 including 6 exons and 5 introns, was cloned.
This gene encodes the water channel protein aquaporin 3. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein, also known as aquaporin 0. Aquaporin 3 is localized at the basal lateral membranes of collecting duct cells in the kidney. In addition to its water channel function, aquaporin 3 has been found to facilitate the transport of nonionic small solutes such as urea and glycerol, but to a smaller degree. It has been suggested that water channels can be functionally heterogeneous and possess water and solute permeation mechanisms.
, 31.4 kDa water channel protein
, aquaporin 3 (GIL blood group)