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anti-Mouse (Murine) ATP2A3 Anticorps:
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Human Monoclonal ATP2A3 Primary Antibody pour IHC (p), ELISA - ABIN559999
Corvazier, Bredoux, Kovács, Enouf: Expression of sarco/endoplasmic reticulum Ca(2+) ATPase (SERCA) 3 proteins in two major conformational states in native human cell membranes. dans Biochimica et biophysica acta 2009
Show all 3 Pubmed References
atp2a3/serca3 expression is restricted to the ectoderm throughout development
SERCA3-dependent Ca(2+) stores control a specific ADP secretion pathway.
ANP counter-regulates cardiac MR activation in hypertensive heart disease. An imbalance in cardiac ANP/GC-A (inhibition) and aldosterone/MR signaling (augmentation) favors adverse cardiac remodeling in chronic pressure overload.
This study evaluated the role of SERCA2b and SERCA3 in the control of the free calcium concentration in the endoplasmic reticulum and the role of SERCA3 in the control of insulin secretion.
identification of promoter region and binding site for Ets-1 in mouse SERCA3
Ablation does not impair insulin secretion but suggests distinct roles of different sarcoendoplasmic reticulum Ca(2+) pumps for Ca(2+) homeostasis in pancreatic beta-cells
regulation in insulin-secreting beta-cells by insulin receptor substrate 1
IRS-1 modulation of insulin secretion is associated with Ca(2+) signaling and expression of SERCA-2b and -3 genes in pancreatic islets. Direct link between insulin resistance and defective insulin secretion.
This study demonstrates that ATP2A3 might be one of the potential targets for salinomycin, which can inhibit Ca(2+) release and trigger ER stress to exert anti-cancer effects.
Sp1, Sp3, and Klf-4 transcription factors bind to ATP2A3 proximal promoter elements and regulate basal gene expression. The study showed that these factors participated in the increase of ATP2A3 expression during cancer cell differentiation.
Together, these data provide evidence for the interaction of Bcl-2 with SERCA3b in vitro and in cell culture, and for Bcl-2-dependent conformational and functional changes of SERCA3b.
ATP2A3 methylation was not altered between patients with type 2 diabetes and healthy men. Moreover, a glucose challenge did not alter ATP2A3 methylation.
we make a comprehensive analysis of the current knowledge of the role of the SERCA pumps in the pathophysiology of insulin-dependent diabetes mellitus type 1 (TIDM) and type 2 (T2DM) in the heart and beta-cells in the pancreas
Normal choroid plexus epithelial cells express SERCA3 abundantly, SERCA3 expression is strongly decreased in papillomas, and is absent in choroid plexus carcinoma, while expression in hyperplastic epithelium is high, similarly to normal epithelium.
aberrant SERCA3 expression is closely linked to the adenoma-adenocarcinoma sequence and progression of colorectal carcinomas.
The Ca2+-ATPase activity in cloned Plasmodiuim falciparum strain D6 protein is higher than in cloned strain W2 protein. The Ca2+-ATPase activity in isolates from malaria patients varied widely.
Loss of SERCA3 expression is associated with lung cancer.
High SERCA3 expression is associated with pathogenesis, invasion, metastasis of gastric carcinomas.
SERCA2 and SERCA3 isoforms have roles in the failing and failing human heart
Data show that low Ca2+-affinity SERCA3, and the high Ca2+-affinity SERCA2 enzymes are simultaneously expressed in B cells, and decreased SERCA3 expression during EBV-infection.
novel sarco/endoplasmic isoforms; data suggest that the SERCA3 gene products have a more widespread role in cellular Ca2+ signaling than previously appreciated
SERCA3 constitutes an interesting new differentiation marker that may prove useful for the analysis of the phenotype of gastrointestinal adenocarcinomas.
Results describe the catalytic cycle of three human SERCA3 isoenzymes: SERCA3a, b, and c.
A method is described for a calcium-activated ATPase technique to be peformed.
monoclonal antibody PL/IM430 inhibits SERCA3 activity by sterically preventing movement of the actuator domain into a catalytically critical position in the E2 conformation of the enzyme.
SERCA3 isoforms have a more widespread role in cellular Ca(2+) signaling: analysis of SERCA3f isoform
link SERCA3 expression to the state of differentiation of colonic epithelial cells
By increasing the rate of Ca2+ sequestration, up-regulation of SERCA 3 counteracts the cytosolic increase in Ca2+ concentration.
This gene encodes one of the SERCA Ca(2+)-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of muscle cells. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, and is involved in calcium sequestration associated with muscular excitation and contraction. Alternative splicing results in multiple transcript variants encoding different isoforms.
ATPase, Ca++ transporting, ubiquitous
, sarcoplasmic/endoplasmic reticulum calcium ATPase 3-like
, SR Ca(2+)-ATPase 3
, calcium pump 3
, sarcoendoplasmic reticulum Ca2+ ATPase type 3
, sarcoplasmic/endoplasmic reticulum calcium ATPase 3
, ATPase, Ca(2+)-transporting, ubiquitous
, adenosine triphosphatase, calcium
, calcium-translocating P-type ATPase
, sarco/endoplasmic reticulum Ca2+ -ATPase
, sarcoendoplasmic reticulum calcium ATPase