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analysis of phosphorylation-dependent interactions of AQP2 with 14-3-3theta; and -zeta
the activation of CaSR (show CASR Proteins) in the collecting duct prevents the cyclic AMP (show TMPRSS5 Proteins)-dependent increase in AQP2-phosphorylation at S256 and water permeability, counteracting the short-term vasopressin (show AVP Proteins) response.
Functional photoconvertible chimeric AQP-2 was successfully expressed in mpkCCD cells, in which forskolin induced apical trafficking and accumulation of chimeric AQP-2.
Suggest ERalpha (show ESR1 Proteins) in mediates the inhibitory effect of estradiol on AQP2 expression in collecting ducts.
Data suggest that the ability of prostaglandin E2 receptor EP4 (show PTGER4 Proteins) to promote aquaporin 2 (AQP2) membrane targeting and increase AQP2 abundance makes it a therapeutic target for the treatment of congenital diabetes insipidus.
Odontoblast-lineage cell line have high-cell viability under xylitol-induced hypertonic stress, which may be associated with TRPV1 (show TRPV1 Proteins) and AQP2 expressions.
The direct renin (show REN Proteins) inhibitor aliskiren increased water channel (show AQP4 Proteins) AQP2 expression in obstructed kidneys of UUO mice, at least partially by preventing NLRP3 (show NLRP3 Proteins) inflammasome activation in association with ureteral obstruction.
role for PKA signaling in both short- and long-term regulation of AQP2, characterizing a novel mouse model of diabetes insipidus
tankyrase likely to play an important role in vasopressin (show AVP Proteins)-induced AQP2 upregulation via beta-catenin (show CTNNB1 Proteins)-mediated transcription in the kidney collecting duct cells
Studied the effect of the total tannins extract of rhubarb on expression od aquaporin 2 and auqaporin 3 in diarrhoea mice.
Impaired endometrial receptivity in patients who underwent controlled ovarian stimulation is correlated with a decreased expression of AQP2.
Pretreatment with alkali (0.4 N NaOH) to disrupt exosome membranes allowed consistent ELISA measurements of urinary AQP2.
Findings indicate that SIRT1 (show SIRT1 Proteins) increases AQP2 expression in TNF-alpha (show TNF Proteins)-induced IMCD cells via the NF-kappaB (show NFKB1 Proteins)-dependent signalling pathway, which might provide novel insight to understanding the renoprotective effects of SIRT1 (show SIRT1 Proteins) in kidney diseases.
AQP2 polymorphisms (rs461872, rs7305534) were correlated with gastrointestinal toxicity of platinum-based chemotherapy in lung cancer patients
report a novel mutation of the AQP2 gene and highlight an important role of genetic testing for definite diagnosis
The study demonstrated the abnormal expression pattern of AQP1 (show AQP1 Proteins), AQP2, AQP3 (show AQP3 Proteins), and AQP4 (show AQP4 Proteins) in the kidney tissues of patients with nephrotic syndrome, providing a basis for an improved understanding of the role of aquaporins in the pathogenesis of this disease.
In most cases (90 %), inherited nephrogenic diabetes insipidus (NDI) is an X-linked disease, caused by mutations in the AVPR2 gene. * In rare occasions (10 %), it is caused by mutations in the AQP2 gene.
Partial congenital nephrogenic diabetes insipidus in the Swedish family is caused by an AQP2 variation that seems to disable the encoded AQP2-R254W protein to reach the subapical vesicle population as well as impairing its phosphorylation at S256
Taken together these results provide a possible molecular mechanism explaining the increased AQP2 membrane expression under RGZ treatment: in renal cells RGZ elicits Ca(2 (show CA2 Proteins)+) transients facilitating AQP2 exposure at the apical plasma membrane
U-AQP2/P-AVP (show AVP Proteins) is a novel predictor of response to TLV in patients with decompensated HF. AQP-defined responders may have a better prognosis on TLV treatment
Aquaporin 2 promotes cell migration and epithelial morphogenesis.
Data provide evidence supporting the role of S256 and S269 in the maintenance of AQP2 at the cell surface.
This gene encodes 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 forms of nephrogenic diabetes insipidus.
ADH water channel
, collecting duct water channel protein
, water channel protein for renal collecting duct
, water-channel aquaporin 2