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The aquaporins are a family of water-selective membrane channels. Additionally we are shipping Aquaporin 9 Antibodies (48) and Aquaporin 9 Proteins (5) and many more products for this protein.
Showing 10 out of 28 products:
Human AQP9 ELISA Kit for Sandwich ELISA - ABIN416728
Jennische, Eriksson, Lange, Trybala, Bergström: The anterior commissure is a pathway for contralateral spread of herpes simplex virus type 1 after olfactory tract infection. in Journal of neurovirology 2015
AQP-7 and -9 showed differential staining pattern in different stages of mouse estrus cycle. AQP-7 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 ELISA Kits).
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 ELISA Kits) 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
The identification of AQP9-induced tumor sensitivity to 5-Fluorouracil highlights the role of AQP9 in regulating chemosensitivity in colorectal cancer.
AQP9 overexpression decreased the protein levels of phosphatidylinositol-3-kinase (PI3K (show PIK3CA ELISA Kits)), leading to reduced phosphorylation of Akt (show AKT1 ELISA Kits), and subsequently the protein levels of forkhead box protein O1 (FOXO1 (show FOXO1 ELISA Kits)) were increased.
AQP9 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 acts as a channel for the protonated, neutral monocarboxylic acid species.
AQP9 is involved in the activation of the ERK (show EPHB2 ELISA Kits) pathway in androgen-independent prostate cancer cells.
trophoblast from gestational diabetes express higher amount of aquaporin 9.
AQP3 was upregulated, and AQP7 and AQP9 were downregulated in hepatocellular carcinoma. A high expression of AQP3 and low expression of AQP7 was significantly associated with the aggressive features of hepatocellular carcinoma.
AQP9 decreases in hepatocellular carcinoma. Dibutrylyl cAMP increases AQP9 levels, suppressing tumor growth.
the human aquaglyceroporins, i.e., AQP3 (show AQP3 ELISA Kits), AQP7, AQP9 and AQP10 can act as silicon transporters in both Xenopus laevis oocytes and HEK (show EPHA3 ELISA Kits)-293 cells.
The full length coding sequences of porcine (Sus scrofa) AQP3 (show AQP3 ELISA Kits), 7 and 9 and the genomic sequence of AQP3 (show AQP3 ELISA Kits) 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