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anti-Human ATP6AP2 Antibodies:
anti-Mouse (Murine) ATP6AP2 Antibodies:
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Human Polyclonal ATP6AP2 Primary Antibody for WB - ABIN1881092
Takahashi, Yamamoto, Hirose, Hiraishi, Shoji, Shibasaki, Kato, Kaneko, Sasano, Satoh, Totsune: Expression of (pro)renin receptor in human kidneys with end-stage kidney disease due to diabetic nephropathy. in Peptides 2010
Show all 5 Pubmed References
Human Polyclonal ATP6AP2 Primary Antibody for IHC, ELISA - ABIN185092
Ludwig, Kerscher, Brandt, Pfeiffer, Getlawi, Apps, Schägger: Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules. in The Journal of biological chemistry 1998
Show all 3 Pubmed References
High ATP6AP2 expression is associated with Renal Damage.
serum s(P)RR could be used as a marker for atherosclerotic conditions in hemodialysis patients
(P)RR may contribute to the homeostatic control of erythropoiesis.
Placental (P)RR can be involved in blood pressure regulation via the tissue RAS. On the other hand, plasma s(P)RR may be involved in the pathogenesis of decreased renal function in preeclampsia.
the present results suggest that ATP6AP2 rs5918007T might be susceptible factors for Essential Hypertension in Chinese Han population.
Study identifies a renin (show REN Antibodies)-angiotensin system-independent function for the (P)RR in the regulation of LDL metabolism by controlling the levels of SORT1 (show SORT1 Antibodies) and LDL receptor (show LDLR Antibodies).
Demonstrate that there are strong interactions between prorenin, ATP6AP2, and TGFB1 (show TGFB1 Antibodies) and that this system has a greater capacity in female amnion to stimulate profibrotic pathways, thus maintaining the integrity of the fetal membranes.
a novel GLP1R (show GLP1R Antibodies) Interacting Protein ATP6ap2
Crosstalk between (Pro)renin receptor and COX-2 (show COX2 Antibodies) in the renal medulla during angiotensin II-induced hypertension
This is the first demonstration that (P)RR may be profoundly involved in ductal tumorigenesis in the pancreas.
Ureter bud PRR (show PVRL1 Antibodies) performs essential functions during UB branching and collecting duct morphogenesis via control of a hierarchy of genes that control UB branching and terminal differentiation of the collecting duct cells.
ATP6AP2 disruption leads to cognitive impairment and neurodegeneration, mimicking aspects of the neuropathology associated with ATP6AP2 mutations in humans.
These findings demonstrate a cell-autonomous requirement for the PRR (show PVRL1 Antibodies) within nephron progenitors for progenitor maintenance.
Atp6ap2 may form a complex with H+-ATPases in proximal tubule and intercalated cells but that prorenin has no acute effect on H+-ATPase (show ATP6AP1 Antibodies) activity in intercalated cells.
Data suggest that high glucose (as in hyperglycemia) decreases autophagy and increases apoptosis in podocytes via activation of (pro)renin receptor (Atp6ap2) and PI3K/Akt (show AKT1 Antibodies)/mTOR (show FRAP1 Antibodies) signaling pathway.
ANG II (show AGT Antibodies) acts via AT1R (show AGTRAP Antibodies) to upregulate PRR (show PVRL1 Antibodies) expression both in cultured cells and in DOCA-salt hypertensive mice by increasing CREB (show CREB1 Antibodies) binding to the PRR (show PVRL1 Antibodies) promoter.
nephron PRR (show PVRL1 Antibodies) may be important in water regulation by modulating the AVP (show AVP Antibodies)/V2R (show AVPR2 Antibodies)/AQP2 (show AQP2 Antibodies) pathway
the v-ATPase (show ATP6V1H Antibodies) ATP6AP2 does not appear to have a fusion-promoting role in the formation of phagolysosomes
ATPase H+ transporting lysosomal accessory protein 2 is critical for granule cell fate and morphogenesis.
This gene encodes a protein that is associated with adenosine triphosphatases (ATPases). Proton-translocating ATPases have fundamental roles in energy conservation, secondary active transport, acidification of intracellular compartments, and cellular pH homeostasis. There are three classes of ATPases- F, P, and V. The vacuolar (V-type) ATPases have a transmembrane proton-conducting sector and an extramembrane catalytic sector. The encoded protein has been found associated with the transmembrane sector of the V-type ATPases.
ATPase H(+)-transporting lysosomal-interacting protein 2
, ATPase, H+ transporting, lysosomal (vacuolar proton pump) membrane sector associated protein M8-9
, ATPase, H+ transporting, lysosomal interacting protein 2
, ER-localized type I transmembrane adaptor
, V-ATPase M8.9 subunit
, embryonic liver differentiation factor 10
, renin receptor
, renin/prorenin receptor
, vacuolar ATP synthase membrane sector-associated protein M8-9
, vacuolar proton ATP synthase membrane sector associated protein M8-9
, (pro)renin receptor
, ATPase, H+ transporting, lysosomal interacting protein 1
, V-type proton ATPase subunit d 2
, V-ATPase subunit d 2
, vacuolar proton pump subunit d 2
, ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d
, ATPase, H+ transporting, lysosomal V0 subunit A2
, ATPase, H+ transporting, lysosomal V0 subunit a
, ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d2
, ATPase, H+ transporting, lysosomal accessory protein 2
, Renin receptor
, V-type proton ATPase subunit d 2-like
, v-type proton ATPase subunit d 2-like
, ATPase H(+)-transporting lysosomal accessory protein 2
, ATPase, H(+)-transporting, lysosomal-interacting protein 2
, ATPase, H+ transporting, lysosomal accessory protein 2 S homeolog