SU5402 - CAS 215543-92-3
Catalog number: B0084-087527
Category: Inhibitor
Please be kindly noted products are not for therapeutic use. We do not sell to patients.
Molecular Formula:
C17H16N2O3
Molecular Weight:
296.32054
COA:
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Targets:
VEGFR
Description:
SU5402 is a potent and selective vascular endothelial growth factor receptor (VEGFR) and fibroblast growth factor receptor (FGFR) inhibitor.
Purity:
0.98
Appearance:
Yellow solid powder
Synonyms:
SU-5402; SU 5402.
MSDS:
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InChIKey:
JNDVEAXZWJIOKB-JYRVWZFOSA-N
InChI:
InChI=1S/C17H16N2O3/c1-10-9-18-15(11(10)6-7-16(20)21)8-13-12-4-2-3-5-14(12)19-17(13)22/h2-5,8-9,18H,6-7H2,1H3,(H,19,22)(H,20,21)/b13-8-
Canonical SMILES:
CC1=CNC(=C1CCC(=O)O)C=C2C3=CC=CC=C3NC2=O
1.FAIMS and Phosphoproteomics of Fibroblast Growth Factor Signaling: Enhanced Identification of Multiply Phosphorylated Peptides.
Zhao H1, Cunningham DL1, Creese AJ1, Heath JK1, Cooper HJ1. J Proteome Res. 2015 Dec 4;14(12):5077-87. doi: 10.1021/acs.jproteome.5b00713. Epub 2015 Nov 5.
We have applied liquid chromatography high-field asymmetric waveform ion mobility spectrometry tandem mass spectrometry (LC-FAIMS-MS/MS) and liquid chromatography tandem mass spectrometry (LC-MS/MS) to the investigation of site-specific phosphorylation in fibroblast growth factor (FGF) signaling. We have combined a SILAC approach with chemical inhibition by SU5402 (an FGF receptor tyrosine kinase inhibitor) and dasatinib (a Src family kinase inhibitor). The results show that incorporation of FAIMS within the workflow results in (a) an increase in the relative proportion of phosphothreonine and phosphotyrosine sites identified, (b) an increase in phosphopeptide identifications from precursors with charge states ≥ +3 (with an associated increase in peptide length), and (c) an increase in the identification of multiply phosphorylated peptides. Approximately 20% of the phosphorylation sites identified via the FAIMS workflow had not been reported previously, and over 80% of those were from multiply phosphorylated peptides.
2.Enhanced Dentinogenesis of Pulp Progenitors by Early Exposure to FGF2.
Sagomonyants K1, Kalajzic I2, Maye P2, Mina M3. J Dent Res. 2015 Nov;94(11):1582-90. doi: 10.1177/0022034515599768. Epub 2015 Aug 14.
Members of the fibroblast growth factor (FGF) family play essential and important roles in primary and reparative dentinogenesis. Although there appears to be a general agreement on the effects of FGF signaling on the proliferation of pulp cells, there are conflicting results regarding its effects on odontoblast differentiation. We recently examined the effects of continuous exposure of dental pulp cells to FGF2 and showed that the effects of FGF2 on differentiation of progenitor cells into odontoblasts were stage specific and dependent on the stage of cell maturity. The purpose of this study was to gain further insight into cellular and molecular mechanisms regulating the stimulatory effects of FGF2 on odontoblast differentiation. To do so, we examined the effects of early and limited exposure of pulp cells from a series of green fluorescent protein (GFP) reporter transgenic mice that display stage-specific activation of transgenes during odontoblast differentiation to FGF2.
3.Activation of the FGFR1 signalling pathway by the Epstein-Barr virus-encoded LMP1 promotes aerobic glycolysis and transformation of human nasopharyngeal epithelial cells.
Lo AK1,2, Dawson CW2, Young LS3, Ko CW1, Hau PM1, Lo KW1. J Pathol. 2015 Oct;237(2):238-48. doi: 10.1002/path.4575. Epub 2015 Aug 3.
Non-keratinizing nasopharyngeal carcinoma (NPC) is closely associated with Epstein-Barr virus (EBV) infection. The EBV-encoded latent membrane protein 1 (LMP1) is believed to play an important role in NPC pathogenesis by virtue of its ability to activate multiple cell signalling pathways which collectively promote cell proliferation, transformation, angiogenesis, and invasiveness, as well as modulation of energy metabolism. In this study, we report that LMP1 increases cellular uptake of glucose and glutamine, enhances LDHA activity and lactate production, but reduces pyruvate kinase activity and pyruvate concentrations. LMP1 also increases the phosphorylation of PKM2, LDHA, and FGFR1, as well as the expression of PDHK1, FGFR1, c-Myc, and HIF-1α, regardless of oxygen availability. Collectively, these findings suggest that LMP1 promotes aerobic glycolysis. With respect to FGFR1 signalling, LMP1 not only increases FGFR1 expression, but also up-regulates FGF2, leading to constitutive activation of the FGFR1 signalling pathway.
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CAS 215543-92-3 SU5402

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