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Aquaporins/major intrinsic protein (MIP) are a family of water-selective membrane channels. Additionally we are shipping Aquaporin 7 Antibodies (42) and many more products for this protein.
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AQP3 (show AQP3 Proteins) was upregulated, and AQP7 and AQP9 were downregulated in hepatocellular carcinoma. A high expression of AQP3 (show AQP3 Proteins) and low expression of AQP7 was significantly associated with the aggressive features of hepatocellular carcinoma.
the human aquaglyceroporins, i.e., AQP3 (show AQP3 Proteins), AQP7, AQP9 and AQP10 can act as silicon transporters in both Xenopus laevis oocytes and HEK (show EPHA3 Proteins)-293 cells.
a direct involvement of AQP7 in water and glycerol transport
AQP7-specific glycerol transport was furthermore found to be specifically inhibited.
REVIEW: the current knowledge on the role of the glycerol channels AQP7 and AQP9 in controlling glycerol metabolism in adipose tissue and liver
AQP7 overexpression may be related to insulin (show INS Proteins) sensitivity and glucose homeostasis in women with the polycystic ovary syndrome.
AQP7 is expressed in human and mouse oocytes and upregulated by cryoprotectants.
AQP7 is regulated in response to physical training in a gender-dependent manner in adipose tissue.
There is a coordinated regulation of adipose AQP7 and hepatic AQP9 gene expression that is distorted in metabolic syndrome X.
In all of the 33 investigated semen samples, we observed AQP7 binding to the sperm sur (show ABCC8 Proteins)-face with different intensity and modality.
upregulation of AQP7 plays an important role in improving of tolerance to hyperosmotic stress and survival of oocytes during cryopreservation by vitrification.
The over-expression of AQP7 contributes to improve insulin (show INS Proteins) resistance in adipocytes, which is potentially correlated with the increased phosphorylation of PKB (show AKT2 Proteins).
Xenopus oocytes microinjected with either AQP7 or AQP9 (show AQP9 Proteins) cRNA (cloned from mouse adipocyte and rat liver, respectively) exhibited a 10-fold increase in arsenite permeability, indicating that both aquaglyceroporins recognize and transport arsenite.
AQP7 may, directly or indirectly, play a role at a distal site in the exocytotic pathway.
AQP7 in skin dendritic cells is primarily involved in antigen uptake and in the subsequent migration of them and is responsible for antigen presentation and the promotion of downstream immune responses.
CM-chitin exerts anti-adipogenic effect on lipid accumulation through modulations of AMPK (show PRKAA1 Proteins) and aquaporin-7 signal pathways.
Aquaporin 7 expansion during uterine decidualization is associated with elevated uterine glycerol accumulation and glycerol kinase (show GK Proteins) expression.
Coordinated regulation of fat-specific and liver-specific glycerol channels, aquaporin adipose and aquaporin 9 (show AQP9 Proteins).
Epinephrine-stimulated glycerol secretion was also impaired in Aqp7 knockdown adipocytes
a modulatory effect of conjugated linoleic acids on aquaporin 7 messenger RNA abundance in dairy cows is not supported by our study
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.
Aquaporins/major intrinsic protein (MIP) are a family of water-selective membrane channels. Aquaporin 7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. Aquaporin 7 and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. Aquaporin 7 facilitates water, glycerol and urea transport. It may play an important role in sperm function.
, aquaporin 7
, aquaporin adipose