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Anti phospho frs2 α tyr196

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Anti Phospho-FRS2-α (Tyr196) is a primary antibody that detects FRS2-α protein phosphorylated at tyrosine residue 196. It is designed for use in applications such as western blotting and immunohistochemistry.

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Lab products found in correlation

Ripa buffer, by Thermo Fisher Scientific (2 mentions) Ab10425, by Abcam (2 mentions) Anti phospho mek1 2, by Cell Signaling Technology (1 mentions) Ab51451, by Abcam (1 mentions) Ab75273, by Abcam (1 mentions) Human tgf β1, by R&D Systems (1 mentions) Sc 535, by Santa Cruz Biotechnology (1 mentions) Human fgf9, by R&D Systems (1 mentions) Human bmp4, by R&D Systems (1 mentions) Human bmp6, by R&D Systems (1 mentions) Anti total p44 42 mapk, by Cell Signaling Technology (1 mentions) Sc 7267, by Santa Cruz Biotechnology (1 mentions) Anti phospho p38, by Cell Signaling Technology (1 mentions) Anti fgfr4, by Cell Signaling Technology (1 mentions) Anti phospho erk1 2 thr202 tyr204, by Cell Signaling Technology (1 mentions)

Spelling variants of this product

Phospho-FRS2 (6 citations) Phospho-FRS2-α (3 citations)

4 protocols using anti phospho frs2 α tyr196

1

Investigating Intracellular Signaling Pathways

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Recombinant bovine FGF2, human FGF9, human TGFβ1, mouse noggin/Fc chimera, human BMP4, human BMP6, and anti-BMP antibody (MAB3552) were from R&D Systems (Minneapolis, MN). The following antibodies were all purchased from Cell Signaling Technology (Danvers, MA): anti–phospho-p44/42 MAPK E10 mouse monoclonal (#9106), anti–total p44/42 MAPK (#9102), anti–phospho-p38 (#9211), anti–phospho-MEK1/2 (#9154), anti–phospho Raf-1 (#9427), anti–phospho-FRS2-α(Tyr-196) (#3864), and anti–phospho-Smad1 (Ser463/465)/Smad5 (Ser463/465) (#9511). Other antibodies used were as follows: for CP49, rabbit anti-mouse CP49 polyclonal serum (#899 or #900; both generous gifts of Paul FitzGerald, University of California, Davis, CA); for phospho-tyrosine, 4G10 (a kind gift from Brian Druker, Oregon Health and Science University, Portland, OR); for luciferase, #G745A from Promega (Madison, WI); for GFP, JL-8 from Clontech (Mountain View, CA); for phospho-Smad3, ab51451 from Abcam (Cambridge, MA); for total Smad 1/5, ab75273 from Abcam; for total Raf-1, sc-7267 from Santa Cruz Biotechnology (Santa Cruz, CA); for total p38, sc-535 from Santa Cruz; and for total MEK, M17030 from Transduction Labs (Lexington, KT). UO126 (used at 15 μM), PD173074 (100 nM), and dorsomorphin (5 μM) were from Calbiochem (La Jolla, CA). All other reagents, including TPA, were from Sigma-Aldrich (St. Louis, MO).
Boswell B.A, & Musil L.S. (2015). Synergistic interaction between the fibroblast growth factor and bone morphogenetic protein signaling pathways in lens cells. Molecular Biology of the Cell, 26(13), 2561-2572.
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2

Characterizing FGFR1c Phosphorylation of FRS2

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We first evaluated the effect of the V429E mutation on the ability of FGFR1c to phosphorylate FRS2 using cell-based assay. WT and V429E FGFR1c were cloned into the lentiviral vector FUCRW following standard protocols. BaF3 cells were maintained as described23 (link) and transfected with FGFR1 pseudoviral stock in Hank's Balanced Salt Solution buffer. Stably transduced cells were treated with 1.5 nM of FGF1 for 10 min, rinsed in PBS and then lysed in RIPA buffer (Thermo Scientific). Cell extract (30 μg) was resolved by SDS-PAGE and analyzed by western blotting using anti FGFR1 (inhouse antibody raised in rabbit), anti-FRS2 (Abcam ab10425) and anti Phospho-FRS2-α (Tyr196) (Cell Signaling, #3864) antibodies.
Villanueva C., Jacobson-Dickman E., Xu C., Manouvrier S., Dwyer A.A., Sykiotis G.P., Beenken A., Liu Y., Tommiska J., Hu Y., Tiosano D., Gerard M., Leger J., Drouin-Garraud V., Lefebvre H., Polak M., Carel J.C., Phan-Hug F., Hauschild M., Plummer L., Rey J.P., Raivio T., Bouloux P., Sidis Y., Mohammadi M., de Roux N, & Pitteloud N. (2014). Congenital hypogonadotropic hypogonadism with split hand/foot malformation: a clinical entity with a high frequency of FGFR1 mutations. Genetics in medicine : official journal of the American College of Medical Genetics, 17(8), 651-659.
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3

Western Blot Analysis of FGFR4 Signaling

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Parental HCC cells and MKI-treated cells were subjected to Western blot analyses with anti-FGFR4 (Cell Signaling Technology), anti-phospho-FRS2α (Tyr196, Cell Signaling Technology), anti-phospho-ERK1/2 (Thr202/Tyr204, Cell Signaling Technology) and anti-tubulin (Oncogene Science, Cambridge, MA, USA) antibodies.
Kanzaki H., Chiba T., Ao J., Koroki K., Kanayama K., Maruta S., Maeda T., Kusakabe Y., Kobayashi K., Kanogawa N., Kiyono S., Nakamura M., Kondo T., Saito T., Nakagawa R., Ogasawara S., Suzuki E., Ooka Y., Muroyama R., Nakamoto S., Yasui S., Tawada A., Arai M., Kanda T., Maruyama H., Mimura N., Kato J., Zen Y., Ohtsuka M., Iwama A, & Kato N. (2021). The impact of FGF19/FGFR4 signaling inhibition in antitumor activity of multi-kinase inhibitors in hepatocellular carcinoma. Scientific Reports, 11, 5303.
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4

Characterizing FGFR1c Phosphorylation of FRS2

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We first evaluated the effect of the V429E mutation on the ability of FGFR1c to phosphorylate FRS2 using cell-based assay. WT and V429E FGFR1c were cloned into the lentiviral vector FUCRW following standard protocols. BaF3 cells were maintained as described23 (link) and transfected with FGFR1 pseudoviral stock in Hank's Balanced Salt Solution buffer. Stably transduced cells were treated with 1.5 nM of FGF1 for 10 min, rinsed in PBS and then lysed in RIPA buffer (Thermo Scientific). Cell extract (30 μg) was resolved by SDS-PAGE and analyzed by western blotting using anti FGFR1 (inhouse antibody raised in rabbit), anti-FRS2 (Abcam ab10425) and anti Phospho-FRS2-α (Tyr196) (Cell Signaling, #3864) antibodies.
Villanueva C., Jacobson-Dickman E., Xu C., Manouvrier S., Dwyer A.A., Sykiotis G.P., Beenken A., Liu Y., Tommiska J., Hu Y., Tiosano D., Gerard M., Leger J., Drouin-Garraud V., Lefebvre H., Polak M., Carel J.C., Phan-Hug F., Hauschild M., Plummer L., Rey J.P., Raivio T., Bouloux P., Sidis Y., Mohammadi M., de Roux N, & Pitteloud N. (2014). Congenital hypogonadotropic hypogonadism with split hand/foot malformation: a clinical entity with a high frequency of FGFR1 mutations. Genetics in medicine : official journal of the American College of Medical Genetics, 17(8), 651-659.
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