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The aquaporins are a family of water-selective membrane channels. Additionally we are shipping Aquaporin 9 Antibodies (44) and Aquaporin 9 Kits (21) and many more products for this protein.
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the dynamics of liver AQP9 involvement in male rodent glycerol homeostasis our model may be adapted to the human liver serving as an important module of a whole body-model of the glucose metabolism both in health and metabolic diseases.
these findings suggest that AQP9 is required for the development of sensitization during cutaneous acquired immune responses via regulating neutrophil function
Our findings implicate the involvement of AQP9 in H2O2 transport in human and mice cells.
Results suggest implication of AQP9 in liver steatosis. The reduction of hepatocyte AQP9 and, consequently, glycerol permeability might be a defensive mechanism to counteract further fat infiltration in liver parenchyma.
The identification of novel, high affinity AQP9 inhibitors in an intracellular binding site.
Aquaporin 9-deficiency results in decreased redox-sensitive erythrocyte cation channel (show TRPV1 Proteins) activity in mice.
Besides being markedly lower than that in Aqp9(+/+) mice, the liver glycerol permeability of the Aqp9 null mice did not increase during fasting.
AQP9 and unidentified UT-A urea channels constitute primary but redundant urea facilitators in murine hepatocytes
Our results not only confirm the presence of AQP9 in astrocytes but also suggest that changes in AQP9 expression alter glial energy metabolism
AQP9 plays an important role in the development of microgravity-induced bone loss, and may be a potential target for the prevention or management of microgravity-induced bone loss.
AQP3 (show AQP3 Proteins) was upregulated, and AQP7 (show AQP7 Proteins) and AQP9 (show AQP7 Proteins) were downregulated in hepatocellular carcinoma. A high expression of AQP3 (show AQP3 Proteins) and low expression of AQP7 (show AQP7 Proteins) was significantly associated with the aggressive features of hepatocellular carcinoma.
AQP9 (show AQP7 Proteins) decreases in hepatocellular carcinoma. Dibutrylyl cAMP increases AQP9 (show AQP7 Proteins) levels, suppressing tumor growth.
Our findings implicate the involvement of AQP9 (show AQP7 Proteins) in H2O2 transport in human and mice cells.
the human aquaglyceroporins, i.e., AQP3 (show AQP3 Proteins), AQP7 (show AQP7 Proteins), AQP9 (show AQP7 Proteins) and AQP10 can act as silicon transporters in both Xenopus laevis oocytes and HEK (show EPHA3 Proteins)-293 cells.
we suggest that AQP9 (show AQP7 Proteins) is involved in viral tropism and pathogenesis of Herpes simplex encephalitis
Oleic acid-induced hepatic steatosis in HepG2 cells is associated with the coordinated regulation of aquaporin 3 (show AQP3 Proteins) and aquaporin 9 via activation of p38 (show CRK Proteins) signaling
AQP9 (show AQP7 Proteins) downregulation together with the subsequent reduction in hepatic glycerol permeability in insulin (show INS Proteins)-resistant states emerges as a compensatory mechanism whereby the liver counteracts further triacylglycerol accumulation
The genetic polymorphisms in OCT2, AQP2 (show AQP2 Proteins), AQP9 (show AQP7 Proteins) and TMEM205 (show TMEM205 Proteins) may contribute to chemotherapy response in lung cancer patients.
REVIEW: the current knowledge on the role of the glycerol channels AQP7 (show AQP7 Proteins) and AQP9 (show AQP7 Proteins) in controlling glycerol metabolism in adipose tissue and liver
AQP9 (show AQP7 Proteins) expressing glioma cells were negative for the brain tumor stem cell marker CD15 (show FUT4 Proteins).
The full length coding sequences of porcine (Sus scrofa) AQP3 (show AQP3 Proteins), 7 and 9 and the genomic sequence of AQP3 (show AQP3 Proteins) including 6 exons and 5 introns, was cloned.
Several subtypes of the AQPs (AQP1, 5, and 9) are involved in regulation of water homeostasis in the reproductive system of gilts.
The aquaporins are a family of water-selective membrane channels. The protein encoded by this gene allows passage of a wide variety of noncharged solutes. It stimulates urea transport and osmotic water permeability\; there are contradicting reports about its role in providing glycerol permeability. The encoded protein may also play a role in specialized leukocyte functions such as immunological response and bactericidal activity.
, major intrisic-like protein
, neutral solute channel aquaporin 9
, small solute channel 1
, membrane water channel