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We also show that activation and reduction of Fyn kinase in oligodendrocytes increases and decreases sheath number per cell, respectively.
Yes kinase plays an important role in epiboly and indicate that Yes kinase participates in signaling by focal adhesion kinase during early development.
Fyn kinase plays an important role in epiboly during zebrafish development, possibly through its effects in calcium signaling.
Fyn, and possibly other Src (show SRC Proteins) family members are activated by dephosphorylation of the C-terminal tyrosine at fertilization
investigated signaling pathways in early development by comparison of the phosphoproteome of wild type embryos with Fyn/Yes knockdown embryos that display specific convergence and extension cell movement defects
Fyn-dependent phosphorylation of SHP-1 serine 591 inactivates the phosphatase, enabling activatory immunoreceptor signaling.
upregulated in fibrotic kidneys
Study identified the binding site between tau and fyn-SH3 may facilitate the development of compounds that can inhibit tau-fyn interactions, which presents an alternative therapeutic strategy for Alzheimer's disease; and provide evidence that a physiological correlation between phosphorylated tau at S202, S262, and S396/404 and fyn is not present in Alzheimer's disease brain.
FYN expression is regulated according to AD status and regulatory region haplotype, and genetic variants may be instrumental in the development of neurofibrillary tangles in AD and other tauopathies.
a substantial fraction of unligated CD36 (show CD36 Proteins) exists in nanoclusters, which not only promote TSP-1 (show THBS1 Proteins) binding but are also enriched with the downstream effector Fyn.
Upon SMAD4 (show SMAD4 Proteins) deletion, we detected high expression levels of FYN in vessel endothelial cells, suggesting the mechanism of the ovarian tumor cells cross the endothelial barrier and transform to an invasive phenotype
Study reveal that binding the phosphorylated tail of Fyn perturbs a residue cluster near the linker connecting the SH2 and SH3 domains of Fyn, which is known to be relevant in the regulation of the activity of Fyn.
The data suggest that miR (show MLXIP Proteins)-106b inhibits Amyloid-beta (1-42)-induced tau phosphorylation at Tyrosine 18 by targeting Fyn.
FYN was transcriptionally regulated by FOXO1 (show FOXO1 Proteins).
Results found that GluN2B (show GRIN2B Proteins) subunit-containing NMDARs were dominant in induced pluripotent stem cell-derived neurons and that tyrosine-protein kinase Fyn potentiated the function of GluN2B (show GRIN2B Proteins) subunit-containing NMDARs.
We conclude that the hypoxia-induced activation of caspase-9 (show CASP9 Proteins) is mediated by Src kinase (show CSK Proteins).
Fyn oncogene (show RAB1A Proteins) alternative spliced forms have been isolated from brain and spleen.
The protein phosphatase PP2A/Balpha binds to the microtubule-associated proteins Tau and MAP2 at a motif also recognized by the kinase Fyn.
PECAM-1 (show PECAM1 Proteins) and Fyn are essential components of a PECAM-1 (show PECAM1 Proteins)-based mechanosensory complex in endothelial cells.
The results of this study suggested the existence of a potential DEP-1 (show PTPRJ Proteins)-Fyn axis in the regulation of microglial functions.
These results suggested that Fyn has a regulatory role in iNOS (show NOS2 Proteins) expression in astrocytes during neuroinflammatory responses.
Somatodendritic accumulation of Tau in Alzheimer's disease is promoted by Fyn-mediated local protein translation.
loss of Fyn in the kidney prevents unilateral ureteral obstruction-induced tubulointerstitial fibrosis, mediated by a reduction in STAT3 (show STAT3 Proteins) phosphorylation
results show that Fyn kinase is an important positive effector of TGF-beta (show TGFB1 Proteins)-induced chemotaxis through the control of phosphatase PP2A (show PPP2R2B Proteins) activity and this is relevant to pathological processes that are related to TGF-beta (show TGFB1 Proteins)-dependent mast cell migration
In summary,MAGI-2 (show MAGI2 Proteins) and Fyn protect dendrin from Nedd4-2 (show NEDD4L Proteins)-mediated ubiquitination and from nuclear translocation, thereby maintaining the physiologic homeostasis of podocytes.
FYN is activated by oxidative stress and serves as a negative feedback regulator of NOX4 (show NOX4 Proteins) in cardiomyocytes during cardiac remodeling
The results of this study suggested that Fyn-mediated NR2B (show GRIN2B Proteins) signaling plays a critical role in regulation of prediabetic neuropathy and that the increased expression/function of NR2B (show GRIN2B Proteins) subunit-containing NMDARs may contribute to the progression of neuropathy in type 2 diabetes
Fyn acts as a regulatory nexus between solar UV, ROS (show ROS1 Proteins) and signal transduction during skin carcinogenesis.
We show that PTP-3, a LAR (show PTPRF Proteins) homolog in Caenorhabditis elegans, participates in Sema2A-regulated axon guidance. PTPdelta, a member of vertebrate LAR (show PTPRF Proteins) class PTPs (show PTS Proteins), is involved in Sema3A (show SEMA3A Proteins)-regulated cortical dendritic growth. In Sema3A (show SEMA3A Proteins) signaling, PTPdelta activates Fyn and Src (show SRC Proteins) kinases by dephosphorylating their C-terminal Tyr (show TYR Proteins) residues.
This gene is a member of the protein-tyrosine kinase oncogene family. It encodes a membrane-associated tyrosine kinase that has been implicated in the control of cell growth. The protein associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. Alternatively spliced transcript variants encoding distinct isoforms exist.
protein-tyrosine kinase fyn
, proto-oncogene tyrosine-protein kinase fyn
, Fyn non-receptor tyrosine kinase
, proto-oncogene c-Fynb
, tyrosine-protein kinase fynb
, FYN oncogene related to SRC, FGR, YES
, proto-oncogene tyrosine-protein kinase fyn-like
, tyrosine-protein kinase Fyn-like
, proto-oncogene c-Fyn
, proto-oncogene tyrosine-protein kinase Fyn
, tyrosine-protein kinase Fyn
, OKT3-induced calcium influx regulator
, c-syn protooncogene
, proto-oncogene Syn
, src-like kinase
, src/yes-related novel
, tyrosine kinase p59fyn(T)
, fyn proto-oncogene
, c-fyn, fyn proto-oncogene
, protein-tyrosine kinase
, proto-oncogene c-Fyna
, tyrosine-protein kinase fyna
, Src Kinase p59