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Aquaporin 5 (AQP5) is a water channel protein. Additionally we are shipping Aquaporin 5 Antibodies (78) and Aquaporin 5 Kits (34) and many more products for this protein.
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Adjusting AQP5 protein levels could be considered a therapeutic strategy for the treatment of acute pulmonary edema induced by H2S and other hazardous gases
GTP (show AK3 Proteins)-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 Proteins) 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 Proteins) 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 Proteins) 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 Proteins) and NF-kappaB (show NFKB1 Proteins)
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.
nuclear matrix protein 4 (show ZNF384 Proteins) overexpression increased Aquaporin 5 mRNA expression by 2.5-fold in HEK293 cells
Our results suggest that AQP5 but not AQP4 (show AQP4 Proteins) contributes to salivary secretion in patients with Sjogren's syndrome, including those with neuromyelitis optica complicated with Sjogren's syndrome.
The findings presented here add further support to mutations in AQP5 being responsible for this particular subtype of NEPPK (show KRT16 Proteins) and also have implications for the optimal initial genetic screening of other British individuals with this clinical diagnosis.
Suggest that sputum AQP1 (show AQP1 Proteins) and AQP5 could be used as diagnostic markers in mild-to-moderate adult-onset asthma.
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 Proteins)) phosphorylation at serine 133.
Aquaporin-5 is expressed in adipocytes with implications in adipose differentiation.
AQP5 is a significant component of lens fiber cell membranes, representing the second most abundant water channel (show AQP4 Proteins) in these cells.
aquaporin 5 appears to be a potential regulator of follicular fluid accumulation, under androgen control, and may be a key factor in antral follicle growth
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