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anti-Human PIKFYVE Anticorps:
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Human Polyclonal PIKFYVE Primary Antibody pour IHC (p), ELISA - ABIN543691
Ikonomov, Sbrissa, Mlak, Deeb, Fligger, Soans, Finley, Shisheva: Active PIKfyve associates with and promotes the membrane attachment of the late endosome-to-trans-Golgi network transport factor Rab9 effector p40. dans The Journal of biological chemistry 2003
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Human Monoclonal PIKFYVE Primary Antibody pour IF, IHC (p) - ABIN566937
Tsuruta, Green, Rousset, Dolmetsch: PIKfyve regulates CaV1.2 degradation and prevents excitotoxic cell death. dans The Journal of cell biology 2009
Show all 2 Pubmed References
Human Polyclonal PIKFYVE Primary Antibody pour IHC (p), WB - ABIN391254
Alesutan, Ureche, Laufer, Klaus, Zürn, Lindner, Strutz-Seebohm, Tavaré, Boehmer, Palmada, Lang, Seebohm, Lang: Regulation of the glutamate transporter EAAT4 by PIKfyve. dans Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 2010
Cloning of pip5k3 and report on its molecular characterization and expression pattern in adult fish as well as during development.
this study shows that PIKfyve coordinates the neutrophil immune response through the activation of the Rac GTPase
in PC-3 cells inhibition of PIKfyve by apilimod or depletion by siRNA increased the secretion of the exosomal fraction.
Here we identify the lipid kinase PIKfyve as a regulator of an alternative pathway that distributes engulfed contents in support of intracellular macromolecular synthesis during macropinocytosis, entosis, and phagocytosis. We find that PIKfyve regulates vacuole size in part through its downstream effector, the cationic transporter TRPML1
A cell-permeable tool for analysing APP intracellular domain function and manipulation of PIKfyve activity.
A novel heterozygous frameshift mutation (c.3151dupA) and a copy number variations in PIKFYVE gene have been found in two unrelated Fleck corneal dystrophy patients.
The PIKfyve complex is required for APP trafficking, suggesting a feedback loop in which APP, by binding to and stimulating phosphatidylinositol-3,5-bisphosphate vesicle formation may control its own trafficking.
APP functionally cooperates with PIKfyve in vivo. This regulation is required for maintaining endosomal and neuronal function.
data identify a novel role of the ArPIKfyve-Sac3 complex in the mechanisms controlling aggregate formation of Sph1 and suggest that Sac3 protein deficiency or overproduction may facilitate aggregation of aggregation-prone proteins
Data suggest PIKFYVE, MTMR3 (myotubularin related protein 3) and their product phosphatidylinositol 5-phosphate are involved in activation of RAC1 (rho family small GTP binding protein); this process regulates migration/invasion of carcinoma/sarcoma.
Data indicate that pharmacological or genetic inactivation of PIKfyve rapidly induces expression of the transcription repressor ATF3, which is necessary and sufficient for suppression of type I IFN expression.
Data indicate that AKT promotes EGFR recycling by phosphorylating and activating PIKfyve.
the present observations show that PKB in conjunction with PIKfyve activates Kir2.1 channels.
Production of phosphatidylinositol 5-phosphate via PIKfyve and MTMR3 regulates cell migration.
PIP5Kalpha promotes TLR4-associated microglial inflammation by mediating PIP(2)-dependent recruitment of TIRAP to the plasma membrane
The results provide the first experimental evidence that the principal pathway for PtdIns5P intracellular production is through PIKfyve.
A novel c.3060-3063 delCCTT (p.P968Vfs23) mutation in the PIKFYVE gene has been described in a five generation Greek family, which segregated with the fleck corneal dystrophy.
The recent advances in Arf6/PIP5K signaling and its linkage to cellular functions, are reviewed.
The first multicellular model for PIKFYVE loss, pointing to a role in lysosome maturation
REVIEW : PIKFYVE and other phosphoinositides regulatory proteins are implicated in human genetic diseases
A phylogenetic study revealing co-evolution of phosphoinositides kinases and phosphatases ; PIKFYVE is absent from several organisms and co-evolved with VAC14 and FIG4
enlarged vacuole formation in PIKfyve-deficient cells was not rescued by Ca2+ or over expression of TRPML1. It is likely that the acidification and vacuolation arrest is bifurcating downstream of PIKfyve
these studies identify a novel role for PIKfyve in controlling the delivery of proteins from the endosomal compartment to the melanosome, a role that is distinct from the role of PIKfyve in the reformation of lysosomes from endolysosomes.
The authors provide evidence that inactivation of PIKfyve by the selective inhibitor STA suppresses excessive mitochondrial reactive oxygen species production and apoptosis through a SIRT3-dependent pathway in cardiomyoblasts.
Thus, PIKfyve plays a role in preventing excessive lung inflammation through regulating alveolar macrophage function.
adipose tissue Pikfyve plays a key role in the mechanisms regulating glucose homeostasis and the PIKfyve pathway is critical in mammary epithelial differentiation during pregnancy and lactogenesis downstream of prolactin receptor signaling.
AP-3 recruitment to TLR9 endosomes was impaired by PIKfyve inhibition.
PIKfyve mediates vesicle motility through the regulation of vesicle integrity in neurons.
Loss of PIKfyve in platelets causes a lysosomal disease leading to inflammation and thrombosis in mice.
Vps34 is a main phosphatidylinositol 3-phosphate source for constitutive PIKfyve functionality.
Daam2-PIP5K function, application of which stimulates remyelination after white matter injury
PIP5Kbeta negatively regulates axon elongation and growth cone size and is involved in the cellular signaling pathway for Sema3A-triggered repulsion in DRG neurons.
PIKfyve is essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle.
Data indicate that type III phosphatidylinositol phosphate kinase (PIPKIII) is essential for embryonic development.
Data indicate that PTEN and PIKfyve are two major players in phagosomal PtdIns(3)P (phosphatidylinositol 3-phosphate) metabolism.
Analysis of tissues from the Pikfyve(beta-geo/beta-geo) mouse mutants reveals that Pikfyve is critical in neural tissues, heart, lung, kidney, thymus, and spleen
Phosphorylated derivatives of phosphatidylinositol (PtdIns) regulate cytoskeletal functions, membrane trafficking, and receptor signaling by recruiting protein complexes to cell- and endosomal-membranes. Humans have multiple PtdIns proteins that differ by the degree and position of phosphorylation of the inositol ring. This gene encodes an enzyme (PIKfyve\; also known as phosphatidylinositol-3-phosphate 5-kinase type III or PIPKIII) that phosphorylates the D-5 position in PtdIns and phosphatidylinositol-3-phosphate (PtdIns3P) to make PtdIns5P and PtdIns(3,5)biphosphate. The D-5 position also can be phosphorylated by type I PtdIns4P-5-kinases (PIP5Ks) that are encoded by distinct genes and preferentially phosphorylate D-4 phosphorylated PtdIns. In contrast, PIKfyve preferentially phosphorylates D-3 phosphorylated PtdIns. In addition to being a lipid kinase, PIKfyve also has protein kinase activity. PIKfyve regulates endomembrane homeostasis and plays a role in the biogenesis of endosome carrier vesicles from early endosomes. Mutations in this gene cause corneal fleck dystrophy (CFD)\; an autosomal dominant disorder characterized by numerous small white flecks present in all layers of the corneal stroma. Histologically, these flecks appear to be keratocytes distended with lipid and mucopolysaccharide filled intracytoplasmic vacuoles. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
, phosphatidylinositol-3-phosphate/phosphatidylinositol 5-kinase, type III
, 1-phosphatidylinositol 3-phosphate 5-kinase
, phosphatidylinositol 3-phosphate 5-kinase type III
, type III PIP kinase
, zinc finger, FYVE domain containing 29
, FYVE finger-containing phosphoinositide kinase
, phosphatidylinositol-3-phosphate 5-kinase type III
, phosphatidylinositol-4-phosphate 5-kinase, type III