Anti srsf2

Manufactured by Merck Group

Sourced in United States

Anti-SRSF2 is a laboratory product from Merck Group that functions as an antibody targeting the SRSF2 protein. It is intended for use in research applications.

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Lab products found in correlation

Anti hnrnp a1, by Santa Cruz Biotechnology (2 mentions) Alexa488 labeled goat anti mouse igg, by Abcam (1 mentions) Anti mcl 1, by Santa Cruz Biotechnology (1 mentions) Anti synaptophysin, by Cell Signaling Technology (1 mentions) Anti grb2, by BD (1 mentions) Anti map2, by Cell Signaling Technology (1 mentions) Anti beta tubulin, by Cell Signaling Technology (1 mentions) β tubulin, by LI COR (1 mentions) Anti srsf1, by Thermo Fisher Scientific (1 mentions) Anti srsf3, by Santa Cruz Biotechnology (1 mentions) Mammalian protease inhibitor, by Merck Group (1 mentions) Bradford reagent, by Bioworld Technology (1 mentions) Methyl thiazolyl tetrazolium (mtt), by Thermo Fisher Scientific (1 mentions) Anti srsf1, by Santa Cruz Biotechnology (1 mentions) Anti α tubulin, by Abcam (1 mentions)

4 protocols using anti srsf2

Immunostaining of SRSF2 in cells

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Cells were grown on coverslips, washed with PBS and fixed for 20 min in 4% paraformaldehyde (PFA). Cells were then permeabilized in 0.5% Triton X-100 for 3 min. After blocking, cells were immunostained for 1 hr with a primary antibody, and after subsequent washes the cells were incubated for 1 hr with secondary fluorescent antibodies. Primary antibodies: anti-SRSF2 (Sigma). Secondary antibodies: Alexa488-labeled goat anti-mouse IgG (Abcam) and Alexa594-labeled goat anti-mouse. Nuclei were counterstained with Hoechst 33342 and coverslips were mounted in mounting medium.

Hochberg-Laufer H., Neufeld N., Brody Y., Nadav-Eliyahu S., Ben-Yishay R, & Shav-Tal Y. (2019). Availability of splicing factors in the nucleoplasm can regulate the release of mRNA from the gene after transcription. PLoS Genetics, 15(11), e1008459.

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Antibody Sources and Reagents

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Antibodies were obtained from the following sources; anti-MAP2, anti-beta-tubulin, and anti-synaptophysin from Cell Signaling Inc. (Beverly, MA), β-tubulin from LI-COR, Odyssey (Lincoln, NE), anti-SRSF1 from Invitrogen, anti-SRSF2 from Sigma Aldrich, anti-MCL1, anti-SRSF3, anti-SRSF4, and anti-HNRNP A1 from Santa Cruz Biotech, and anti-Grb2 from BD Biosciences. Mammalian protease inhibitors were obtained from Sigma-Aldrich (St Louis, MO). Bradford reagent was from BioWorld (Dublin, OH). MTT (3-(4,5-Dimethylthiazol-2-yl)-2,5-Diphenyltetrazolium Bromide) was obtained from Thermo Fisher Scientific (#M6494).

Sariyer R., De Simone F.I., Donadoni M., Hoek J.B., Chang S.L, & Sariyer I.K. (2017). Alcohol-mediated missplicing of Mcl-1 pre-mRNA is involved in neurotoxicity. Alcoholism, clinical and experimental research, 41(10), 1715-1724.

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Immunoblotting of SRSF2 in Cells

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Immunoblotting with anti-SRSF2 antibody was performed as previously described (34 (link)). Briefly, cells were harvested and lysed with lysis buffer for 30 min at 4°C. The supernatants were collected and separated on 12% SDS-PAGE, and then transferred to PDVF membrane. After blocking with 5% skim milk, membrane was incubated anti-SRSF2 (Millipore) or anti-U2AF65 antibodies. The signal was detected by enhanced chemiluminescence (ECL).

Moon H., Cho S., Loh T.J., Jang H.N., Liu Y., Choi N., Oh J., Ha J., Zhou J., Cho S., Kim D.E., Ye M.B., Zheng X, & Shen H. (2017). SRSF2 directly inhibits intron splicing to suppresses cassette exon inclusion. BMB Reports, 50(8), 423-428.

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Western Blot Analysis of Splicing Factors

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SH-SY5Y and HEK293T cells were lysed in the lysis buffer (0.1% triton X-100, 50 mM Tris-Cl, pH 7.5, 150 mM NaCl, 5 mM EDTA, 1 mM beta-mercaptoethanol) for 30 min at 4 °C, followed by treatment with 5x SDS loading dye and separation using 12% SDS-PAGE gel. After transferring to nitrocellulose membrane, hnRNP A1, SRSF1, SRSF2, SRSF6 and α-tubulin proteins were detected using anti-hnRNP A1 (Santa Cruz; sc-32301), anti-SRSF1 (Santa Cruz; sc-33652), anti-SRSF2 (Millipore, Burlington, VT, USA; 04-1550), anti-SRSF6 (Millipore; MABE152) and anti-α-tubulin (abcam, Cambridge, UK; ab18251) antibodies.

Liu Y., Kim D., Choi N., Oh J., Ha J., Zhou J., Zheng X, & Shen H. (2020). hnRNP A1 Regulates Alternative Splicing of Tau Exon 10 by Targeting 3′ Splice Sites. Cells, 9(4), 936.

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