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Aquaporins/major intrinsic protein (MIP) are a family of water-selective membrane channels. Additionally we are shipping Aquaporin 7 Proteins (5) and many more products for this protein.
Showing 10 out of 42 products:
Human Polyclonal AQP7 Primary Antibody for IF (p), IHC (p) - ABIN741255
Vicente-Carrillo, Ekwall, Álvarez-Rodríguez, Rodríguez-Martínez: Membrane Stress During Thawing Elicits Redistribution of Aquaporin 7 But Not of Aquaporin 9 in Boar Spermatozoa. in Reproduction in domestic animals = Zuchthygiene 2016
ex vivo studies in human primary adipocytes, demonstrate that perilipin 1 (show PLIN1 Antibodies) binds to AQP7, and that catecholamine activated protein kinase A phosphorylates the N-terminus of AQP7, thereby reducing complex formation
Aquaporins AQP3 (show AQP3 Antibodies), -7, -8, and -11 proteins were found in sperm cells and localized in the head (AQP7), in the middle piece (AQP8 (show AQP8 Antibodies)) and in the tail (AQP3 (show AQP3 Antibodies) and -11) in both the plasma membrane and in intracellular structures.
AQP3 (show AQP3 Antibodies) was upregulated, and AQP7 and AQP9 were downregulated in hepatocellular carcinoma. A high expression of AQP3 (show AQP3 Antibodies) and low expression of AQP7 was significantly associated with the aggressive features of hepatocellular carcinoma.
the human aquaglyceroporins, i.e., AQP3 (show AQP3 Antibodies), AQP7, AQP9 and AQP10 (show AQP10 Antibodies) can act as silicon transporters in both Xenopus laevis oocytes and HEK (show EPHA3 Antibodies)-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 Antibodies) 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.
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.
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 Antibodies) resistance in adipocytes, which is potentially correlated with the increased phosphorylation of PKB (show AKT2 Antibodies).
Xenopus oocytes microinjected with either AQP7 or AQP9 (show AQP9 Antibodies) 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 Antibodies) and aquaporin-7 signal pathways.
Aquaporin 7 expansion during uterine decidualization is associated with elevated uterine glycerol accumulation and glycerol kinase (show GK Antibodies) expression.
Coordinated regulation of fat-specific and liver-specific glycerol channels, aquaporin adipose and aquaporin 9 (show AQP9 Antibodies).
a modulatory effect of conjugated linoleic acids on aquaporin 7 messenger RNA abundance in dairy cows is not supported by our study
Data suggest that boar spermatozoa express AQP11 (show AQP11 Antibodies) and AQP7; amounts of AQP11 (show AQP11 Antibodies) (but not those of AQP7) are correlated with sperm motility, membrane integrity, and membrane fluidity. These studies were conducted in Spain in Pietrain boars.
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.
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