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Validated All-in-One™ qPCR Primer for FYN(NM_002037.3) Search again
Product ID:
HQP006484
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
SLK, SYN, p59-FYN
Gene Description:
FYN proto-oncogene, Src family tyrosine kinase
Target Gene Accession:
NM_002037.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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. [provided by RefSeq].
Gene References into function
- Association of Fyn and Lyn with the proline-rich domain of glycoprotein VI regulates intracellular signaling
- Src-kinase p59(fyn) play a role in anergy induction in CD8+ T cells.
- the distinct potential of Fyn and Lck to phosphorylate Sam68 is likely controlled by the interaction of the kinase SH3 domain with the linker and Sam68, possibly on a competitive binding basis.
- identification of novel isoform fynDelta7, in which exon 7 is absent
- The Fyn but not the Lck tyrosine kinase SH3 domain competes with CD2BP2 GYF-domain binding to the same CD2 proline-rich sequence in vitro. CD2BP2 is replaced by Fyn SH3 after CD2 is translocated into lipid rafts upon CD2 ectodomain clustering.
- High expression of FYN is restricted to low-stage tumors and predicts long-term survival. In culture, expression of active Fyn kinase induces differentiation and growth arrest of neuroblastoma cells.
- Data show that the SLAM-associated protein (SAP) SH2 domain binds to the SH3 domain of FynT and directly couples FynT to SLAM.
- There was an increase in both total area Fyn mRNA signal (17.7%, P<0.05) and cellular mRNA content (15.7%, P<0.05) in schizophrenic brains relative to controls.
- p250GAP is phosphorylated by Fyn in oligodendrocytes.
- upon ligation of integrin beta6 with fibronectin, beta6 complexed with Fyn and activated it, activating a pathway leading to activation of the matrix metalloproteinase-3 gene, and promoting oral SCC cell proliferation and experimental metastasis in vivo
- tr-kit promotes the formation of a multimolecular complex composed of Fyn, PLCgamma1 and Sam68, which allows phosphorylation of PLCgamma1 by Fyn, and may modulate RNA metabolism.
- Two Src kinases are selectively activated by TPO signaling in primary megakaryocytes, Fyn and Lyn, but only Fyn expression is significantly upregulated during MK differentiation, suggesting variable gene regulation.
- Our results indicate a possible association of alcohol dependence with a genotype of the SNP T137346C of the PTK fyn, with C being the risk allele.
- Tyrosine phosphorylated tau is distributed in Alzheimer disease brain differently from other phosphorylated tau. Evidence of differentially phosphorylated tau within degenerating neurons was found supporting a role for fyn in neurodegeneration
- LYN and FYN are downregulated by CBL in osteoblast differentiation induced by constitutive FGFR2 activation
- activation of Fyn is inhibited by NSAIDs and constitutively active Fyn reverses the NSAID-dependent stress kinase inhibition
- determined that Fyn phosphorylated MAP-2c on tyrosine 67
- Fyn kinase plays a key role in the UVB-induced phosphorylation of histone H3 at serine 10
- Alterations in Fyn localization might be associated with neurofibrillary pathology and synapse loss in Alzheimer's disease.
- PEDF downregulates Fyn through Fes, resulting in inhibition of FGF-2-induced capillary morphogenesis of endothelial cells
- calcium activates PLC-gamma1 via increased PIP3 formation mediated by c-src- and fyn-activated PI3K
- the Fyn-tau interaction has a role in neurodegeneration
- independent of one another Fyn and MAP-2c are able to induce process outgrowth and in concert can initiate and enhance process outgrowth in an additive manner.
- Increased Fyn expression is sufficient to trigger prominent neuronal deficits in FYN/human amyloid precursor protein transgenic mice in the context of even relatively moderate Abeta levels.
- Cells with single Src family kinase knockdown show that Src, Fyn and Yes kinases are all required for vascular endothelial growth factor (VEGF) mitogenic signaling in retinal microvascular endothelial cells.
- Fibronectin rigidity response involves force-dependent Fyn phosphorylation of p130Cas with rigidity-dependent displacement.
- Fyn suppresses the GTPase-activating protein (GAP) activity of wild-type brain-enriched Rho GTPase-activating protein TCGAP but not the Y406F mutant of TCGAP in a phosphorylation-dependent manner.
- Staurosporine binds to the ATP-binding site of Fyn in a similar manner as in the Lck- and Csk-complexes
- These results indicate that Fyn is activated by G-protein-coupled receptor stimulation and is responsible for transactivation of TrkA receptors on intracellular membranes.
- extracellular matrix fragments produced by apoptotic EC initiate a state of resistance to apoptosis in fibroblasts via an alpha2beta1 integrin/SFK (Src and Fyn)/phosphatidylinositol 3-kinase (PI3K)-dependent pathway
- Glucocorticoids causes dissociation of T-cell receptor associated protein complex containing LCK and FYN.
- TNF-alpha regulates the pulmonary vascular endothelial paracellular pathway, in part, through fyn activation.
- The extra-domain B binding D3 protein opens new biomedical opportunities for the in vivo imaging of solid tumorsand for the delivery of toxic agents to the tumoral vasculature.
- Polymorphisms of the Fyn gene is related to the function of glutamatergic system, and a performance on neuropsychological test of prefrontal cortex activity in schizophrenic patients.
- the mechanism of signal transduction by CD244 is to regulate FYN kinase recruitment and/or activity and the outcome of CD48/CD244 interactions is determined by which other receptors are engaged.
- Fyn is weakly phosphorylated in normal B cells, but strongly phosphorylated in myeloma B cells.
- The results of this study may suggest a relationship between the FYN gene polymorphisms and allergic asthma
- Chromosomal deletion, promoter hypermethylation and downregulation of FYN is associated with prostate cancer
- engagement of the SH2 domain on PAG renders FynT insensitive to Csk negative regulation
- Fyn, due in part to its effects on Dab1, regulates the phosphorylation, trafficking, and processing of APP and apoEr2.
- Up-regulation, in contrast to activation, of the ubiquitously expressed Src kinase, Fyn, by BCR-ABL1, is described.
- NS5A binds to the Fyn SH3 domain with what can be considered a high affinity SH3 domain-ligand interaction (629 nM), and this binding did not require the presence of domain I of NS5A (amino acid residues 32-250).
- DNMTs activity may have an indirect influence on the expression of Fyn without altering the methylation level of its promoter in Hut-78 T-lymphoma cells.
- H2O2 significantly inhibited Cl(-)/OH(-) exchange activity in Caco-2 cells. H(2)O(2)-mediated inhibition of Cl(-)/OH(-) exchange activity involved the Src kinase Fyn and PI3K (phosphoinositide 3-kinase)-dependent pathways.
- PECAM-1 and Fyn are essential components of a PECAM-1-based mechanosensory complex in endothelial cells
- Analysis reveals that the Fyn SH2 domain forms a noisy communication channel that couples residues located in the phosphopeptide and specificity binding sites and a number of residues at the other side of the domain.
- tyrosine phosphorylation of Neph1 mediated by Fyn results in significantly increased Neph1 and ZO-1 binding, suggesting a critical role for Neph1 tyrosine phosphorylation in reorganizing the Neph1-ZO-1 complex.