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Aquaporin 5 (AQP5) is a water channel protein. Additionally we are shipping Aquaporin 5 Antibodies (76) and Aquaporin 5 Proteins (4) and many more products for this protein.
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GTP (show AK3 ELISA Kits)-dependent AQP5 expression could act as osmosensor
AQP5 promoter methylation is not a universal mechanism for AQP5 regulation.
The activation of P2X7 receptor (show P2RX7 ELISA Kits) was connected with an increase of aquaporin-5, whereas the inhibition of the receptor with oxidized ATP resulted in down regulation of aquaporin-5.
Lung AQP1 (show AQP1 ELISA Kits) and AQP5 expression were significantly decreased in mice with acute lung injury together with increased inflammatory reaction and apoptosis of alveolar epithelial and vascular endothelial cells
The co-regulation of pendrin (show SLC26A4 ELISA Kits) and AQP5 membrane expression under chronic K(+)-deficiency indicates that these two molecules could cooperate as an osmosensor to rapidly detect and respond to alterations in luminal fluid osmolality.
propose a new function of AQP5 as an inflammatory signal potentiator, which may be mediated by increased activation of ERK (show EPHB2 ELISA Kits) and NF-kappaB (show NFKB1 ELISA Kits)
AQP5 plays an important role in high altitude pulmonary edema formation induced by high altitude simulation.
Administration of cevimeline maintains the proper localization of AQP-5 in the acinar cells of the salivary glands of mice with Sjogren's syndrome.
this is the first report providing evidence that AQP5 facilitates maintenance of lens transparency and homeostasis by regulating osmotic swelling caused by glucose transporters and cotransporters under hyperglycemic stressful conditions.
The regulated AQP5 translocation may contribute to sweat secretion by increasing the water permeability of apical plasma membranes of sweat glands.
AQP5 plasma membrane abundance in transfected HEK293 cells is rapidly and reversibly regulated by at least three independent mechanisms involving phosphorylation at Ser156, protein kinase A activity and extracellular tonicity.
AQP5 can be both overexpressed and lost in subgroups of prostate cancers
AQP5 defined a subset of patients with Bcl-2-negative and p16-negative tumours with a poor clinical outcome.
Histamine downregulates AQP5 production in human nasal epithelial cells by inhibiting cyclic adenosine monophosphate-responsive element binding protein (CREB (show CREB1 ELISA Kits)) phosphorylation at serine 133.
Aquaporin-5 is expressed in adipocytes with implications in adipose differentiation.
These results indicate that NFAT5 (show NFAT5 ELISA Kits) plays important roles in proliferation and migration of human lung adenocarcinoma cells through regulating AQP5 expression, providing a new therapeutic option for lung adenocarcinoma therapy.
The hyperosmotic induction of AQP5 and VEGF (show VEGFA ELISA Kits) in retinal pigment epithelial cells was in part dependent on activation of NFAT5 (show NFAT5 ELISA Kits).
AQP5 was strongly localized in the apical membrane and weakly localized in the cytoplasm of secretory epithelial cells.
Study found a significant correlation between AQP1 (show AQP1 ELISA Kits), AQP3 (show AQP3 ELISA Kits), and AQP5 overexpression and lymph node metastasis in patients with surgically resected colon cancer.
The AQP5 protein is up-regulated in prostate cancer and is closely related to advanced stage, lymph node metastasis, and poor prognosis. AQP5 expression was associated with cell proliferation and migration.
AQP5 is a significant component of lens fiber cell membranes, representing the second most abundant water channel (show AQP4 ELISA Kits) in these cells.
AQP1 and 5 seem to be crucial for follicular development in pigs
Several subtypes of the AQPs (AQP1, 5, and 9) are involved in regulation of water homeostasis in the reproductive system of gilts.
Aquaporin 5 (AQP5) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. AQP0, AQP2, AQP5, and AQP6 are closely related and all map to 12q13.
major intrinsic protein of lens fiber
, aquaporin 5
, water channel