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anti-Human FYN Antibodies:
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Human Monoclonal FYN Primary Antibody for ICC, IF - ABIN269149
Taniguchi, Xia, Goldberg, Lee, Shah, Stavar, Masson, Momen, Shikatani, John, Husain, Fantus: Inhibition of Src kinase blocks high glucose-induced EGFR transactivation and collagen synthesis in mesangial cells and prevents diabetic nephropathy in mice. in Diabetes 2013
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Human Monoclonal FYN Primary Antibody for ICC, FACS - ABIN969159
Brignatz, Paronetto, Opi, Cappellari, Audebert, Feuillet, Bismuth, Roche, Arold, Sette, Collette: Alternative splicing modulates autoinhibition and SH3 accessibility in the Src kinase Fyn. in Molecular and cellular biology 2009
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Human Monoclonal FYN Primary Antibody for ELISA, WB - ABIN969160
Kitkumthorn, Yanatatsanajit, Kiatpongsan, Phokaew, Triratanachat, Trivijitsilp, Termrungruanglert, Tresukosol, Niruthisard, Mutirangura: Cyclin A1 promoter hypermethylation in human papillomavirus-associated cervical cancer. in BMC cancer 2006
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Human Polyclonal FYN Primary Antibody for IHC (p), ELISA - ABIN544385
Goldsmith, Hall, Atkinson: Identification of an alternatively spliced isoform of the fyn tyrosine kinase. in Biochemical and biophysical research communications 2002
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Human Monoclonal FYN Primary Antibody for WB - ABIN1944798
Kawakami, Pennington, Robbins: Isolation and oncogenic potential of a novel human src-like gene. in Molecular and cellular biology 1987
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Human Monoclonal FYN Primary Antibody for ICC, IHC (p) - ABIN94311
Queval, Nicolas, Beau: Role of Src kinases in mobilization of glycosylphosphatidylinositol-anchored decay-accelerating factor by Dr fimbria-positive adhering bacteria. in Infection and immunity 2011
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Human Monoclonal FYN Primary Antibody for ELISA, WB - ABIN966167
Lu, Zhu, Cvrljevic, Huang, Sarkaria, Ahkavan, Dang, Dinca, Plaisier, Oderberg, Lee, Chen, Caldwell, Xie, Loo, Seligson, Chakravari, Lee, Weinmann, Cloughesy, Nelson, Bergers, Graeber, Furnari, James, Cavenee, Johns, Mischel: Fyn and SRC are effectors of oncogenic epidermal growth factor receptor signaling in glioblastoma patients. in Cancer research 2009
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Human Polyclonal FYN Primary Antibody for ELISA, WB - ABIN268717
Semba, Nishizawa, Miyajima, Yoshida, Sukegawa, Yamanashi, Sasaki, Yamamoto, Toyoshima: yes-related protooncogene, syn, belongs to the protein-tyrosine kinase family. in Proceedings of the National Academy of Sciences of the United States of America 1986
Human Polyclonal FYN Primary Antibody for PLA, WB - ABIN515873
Liu, Chen, Chau, Jan, Chen, Hsu, Lin, Juang, Lu, Cheng, Chen, Chang, Ting, Kao, Hsiao, Huang: Analysis of protein-protein interactions in cross-talk pathways reveals CRKL protein as a novel prognostic marker in hepatocellular carcinoma. in Molecular & cellular proteomics : MCP 2013
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 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
miR-381 induces sensitivity of breast cancer cells to doxorubicin by inactivation of MAPK signaling via FYN
SPHK2 is highly expressed in the kidney interstitium of patients with renal fibrosis and highly correlates with disease progression. SPHK2 phosphorylates Fyn to activate downstream STAT3 and AKT, thereby promoting extracellular matrix synthesis, kidney fibroblast activation, and renal fibrosis.
Fyn and Lyn as important factors that promote Plasmacytoid dendritic cell responses.
Data suggest that Fyn tyrosine kinase (Fyn)-dependent phosphorylation at two critical tyrosines is a key feature of vertebrate plexin A1 (PlxnA1) and plexin A2 (PlxnA2) signal transduction.
Nav1.7 is a substrate for Fyn kinase.
Fyn binds to mGluR1a at a consensus binding motif located in the intracellular C-terminus (CT) of mGluR1a in vitro. Active Fyn phosphorylates mGluR1a at a conserved tyrosine residue in the CT region. In cerebellar neurons and transfected HEK293T cells, Fyn-mediated tyrosine phosphorylation of mGluR1a is constitutively active and facilitates surface expression of mGluR1a and potentiates mGluR1a postreceptor signaling.
High FYN expression is associated with pancreatic cancer metastasis.
Study was the first to demonstrate critical positive regulation of thyroid tumorigenesis by FYN, which could be a potential target gene for thyroid carcinoma treatment.
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 exists in nanoclusters, which not only promote TSP-1 binding but are also enriched with the downstream effector Fyn.
Upon SMAD4 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-106b inhibits Amyloid-beta (1-42)-induced tau phosphorylation at Tyrosine 18 by targeting Fyn.
FYN was transcriptionally regulated by FOXO1.
Results found that GluN2B subunit-containing NMDARs were dominant in induced pluripotent stem cell-derived neurons and that tyrosine-protein kinase Fyn potentiated the function of GluN2B subunit-containing NMDARs.
Data show that fyn proto-oncogene protein (FYN) expression is deregulated in acute myeloid leukemia and that higher expression of FYN, in combination with FLT3 protein-ITD mutation, resulted in enrichment of the STAT5 transcription factor signaling.
These results indicate that the microenvironment and growth patterns in an multicellular spheroid are complex and require MAPK and FYN kinase
We conclude that the hypoxia-induced activation of caspase-9 is mediated by Src kinase.
Fyn oncogene 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 and Fyn are essential components of a PECAM-1-based mechanosensory complex in endothelial cells.
Our findings suggest a mechanism, by which a decrease in miR-125a-3p during oocyte maturation facilitates GVBD by allowing Fyn up-regulation and the resulting stabilization of the interaction between actin and A-type lamins.
these results suggest that Nrf2 plays a central role in the prevention of Ang II-induced cardiomyopathy, and SFN prevents Ang II-induced cardiomyopathy partially via the Akt/GSK-3beta/Fyn-mediated Nrf2 activation.
This study reported that suppression of Fyn expression in mouse cerebral cortex led to migration defects of both early-born and late-born neurons.
ATF3 inhibit the expression and release of TNF-alpha, IL-1beta, IL-6, and IL-18 induced by Mycoplasma pneumonia in vitro and in vivo, which is associated with its negative regulation of Egr-1/Fyn signaling pathway.
The results of this study suggested the existence of a potential DEP-1-Fyn axis in the regulation of microglial functions.
These results suggested that Fyn has a regulatory role in iNOS 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 phosphorylation
results show that Fyn kinase is an important positive effector of TGF-beta-induced chemotaxis through the control of phosphatase PP2A activity and this is relevant to pathological processes that are related to TGF-beta-dependent mast cell migration
In summary,MAGI-2 and Fyn protect dendrin from Nedd4-2-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 in cardiomyocytes during cardiac remodeling
The results of this study suggested that Fyn-mediated NR2B signaling plays a critical role in regulation of prediabetic neuropathy and that the increased expression/function of NR2B subunit-containing NMDARs may contribute to the progression of neuropathy in type 2 diabetes
Fyn acts as a regulatory nexus between solar UV, ROS and signal transduction during skin carcinogenesis.
We show that PTP-3, a LAR homolog in Caenorhabditis elegans, participates in Sema2A-regulated axon guidance. PTPdelta, a member of vertebrate LAR class PTPs, is involved in Sema3A-regulated cortical dendritic growth. In Sema3A signaling, PTPdelta activates Fyn and Src kinases by dephosphorylating their C-terminal Tyr residues.
data show that Fyn kinase is activated after TLR4 triggering and exerts an important negative control on LPS-dependent TNF production in mast cells controlling the inactivation of PP2Ac and activation of PKCalpha/beta necessary for the secretion of TNF by VAMP3(+) carriers
Fyn deficiency alters retinal morphology and adhesion properties of Muller cells. Fyn deficiency parallels a decreased optokinetic response to visual stimuli in vivo.
Fyn mediates high glucose-induced actin cytoskeleton remodeling of podocytes via promoting ROCK activation and paxillin phosphorylation
MOBP synthesis is stimulated by Fyn activity.
Fyn expression was elevated in abortion-prone mice
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