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The aquaporins are a family of water-selective membrane channels. Additionally we are shipping Aquaporin 9 Kits (28) and Aquaporin 9 Proteins (5) and many more products for this protein.
Showing 10 out of 49 products:
Human Polyclonal AQP9 Primary Antibody for IF (p), IHC (p) - ABIN677123
Chau, Ng, Chan, Cheng, Fong, Tam, Kwong, Tse: Azacytidine sensitizes acute myeloid leukemia cells to arsenic trioxide by up-regulating the arsenic transporter aquaglyceroporin 9. in Journal of hematology & oncology 2015
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AQP-7 (show AQP7 Antibodies) and -9 showed differential staining pattern in different stages of mouse estrus cycle. AQP-7 (show AQP7 Antibodies) and -9-mediated glycerol transport in tanycyte cells might be under hormonal control to use glycerol as a potential energy substrate during mouse estrus cycle.
Intracranial hemorrhage increased AQP9 protein levels in the hippocampus. Lack of AQP9 impairs neovascularization and exaggerates neuronal death following ICH (show ACE Antibodies).
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 Antibodies) 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
AQP9 (show AQP7 Antibodies) overexpression decreased the protein levels of phosphatidylinositol-3-kinase (PI3K (show PIK3CA Antibodies)), leading to reduced phosphorylation of Akt (show AKT1 Antibodies), and subsequently the protein levels of forkhead box protein O1 (FOXO1 (show FOXO1 Antibodies)) were increased.
AQP9 (show AQP7 Antibodies) is down-regulated in hepatocellular carcinoma and its over-expression suppresses hepatoma cell invasion through inhibiting epithelial-to-mesenchymal transition.
pH-dependent substrate permeability, measurements of media alkalization, and proton decoupling that AQP9 (show AQP7 Antibodies) acts as a channel for the protonated, neutral monocarboxylic acid species.
AQP9 (show AQP7 Antibodies) is involved in the activation of the ERK (show EPHB2 Antibodies) pathway in androgen-independent prostate cancer cells.
trophoblast from gestational diabetes express higher amount of aquaporin 9.
AQP3 (show AQP3 Antibodies) was upregulated, and AQP7 (show AQP7 Antibodies) and AQP9 (show AQP7 Antibodies) were downregulated in hepatocellular carcinoma. A high expression of AQP3 (show AQP3 Antibodies) and low expression of AQP7 (show AQP7 Antibodies) was significantly associated with the aggressive features of hepatocellular carcinoma.
AQP9 (show AQP7 Antibodies) decreases in hepatocellular carcinoma. Dibutrylyl cAMP increases AQP9 (show AQP7 Antibodies) levels, suppressing tumor growth.
Our findings implicate the involvement of AQP9 (show AQP7 Antibodies) in H2O2 transport in human and mice cells.
the human aquaglyceroporins, i.e., AQP3 (show AQP3 Antibodies), AQP7 (show AQP7 Antibodies), AQP9 (show AQP7 Antibodies) and AQP10 (show AQP10 Antibodies) can act as silicon transporters in both Xenopus laevis oocytes and HEK (show EPHA3 Antibodies)-293 cells.
we suggest that AQP9 (show AQP7 Antibodies) is involved in viral tropism and pathogenesis of Herpes simplex encephalitis
The full length coding sequences of porcine (Sus scrofa) AQP3 (show AQP3 Antibodies), 7 and 9 and the genomic sequence of AQP3 (show AQP3 Antibodies) 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