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U2af2

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U2AF2 is a protein involved in pre-mRNA splicing. It functions as a part of the spliceosome complex, which is responsible for removing introns from pre-mRNA molecules.

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Lab products found in correlation

Py397 fak, by Abcam (2 mentions) U2af2, by Santa Cruz Biotechnology (2 mentions) Anti ubiquitin p4d1, by Santa Cruz Biotechnology (2 mentions) Cd44 clone 2c5, by Thermo Fisher Scientific (2 mentions) Src py416, by Cell Signaling Technology (2 mentions) Horseradish peroxidase hrp conjugated secondary antibody, by Abcam (2 mentions) Vegfa, by Abcam (1 mentions)

5 protocols using u2af2

1

Immunohistochemical Analysis of Protein Expression

Cited 2 times
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IHC was performed and the results were semi-quantified as previously described [23 (link)]. Briefly, the paraffin-embedded tissue sections were labeled with primary antibody against ISL2 (1:100; Abcam), U2AF2 (1:100; Abcam), VEGFA (1:100; Abcam), and CD31 (1:100; Abcam). The sections were then treated with an immunohistochemical labeling kit (MaxVision Biotechnology, Fuzhou, China) and photographed with a light microscope (Olympus, Tokyo, Japan). The German immunohistochemical score was used to evaluate the staining intensity and expression levels [25 (link)].
Jiang Y., Zhou J., Zhao J., Zhang H., Li L., Li H., Chen L., Hu J., Zheng W, & Jing Z. (2020). The U2AF2 /circRNA ARF1/miR-342–3p/ISL2 feedback loop regulates angiogenesis in glioma stem cells. Journal of Experimental & Clinical Cancer Research : CR, 39, 182.
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2

Western Blot Analysis of Protein Expression

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Western blotting analysis of protein expression was described previously5 (link). CD44 (clone 2C5), CD82 (Life Technologies), U2AF2 (Abcam, Eugene, OR), FAK (Abcam, Eugene, OR), pY397 FAK (Abcam, Eugene, OR), Src (Santa Cruz, Dallas, TX), pY416 Src (Cell Signaling Technology, Danvers, MA), and RhoA (Abcam, Eugene, OR) were detected with corresponding primary monoclonal antibodies (1:1000 diluted in blocking buffer). For examining the effect of CD82 overexpression on U2AF2 ubiquitination, melanoma cells were treated with 10 μM MG132 for 6 hr before U2AF2 was immunoprecipitated, resolved in SDS-PAGE, transferred to a nitrocellulose membrane and developed with anti-ubiquitin P4D1 (1:1,000, Santa Cruz) and anti-U2AF2 antibodies.
Zhang P., Feng S., Liu G., Wang H., Fu A., Zhu H., Ren Q., Wang B., Xu X., Bai H, & Dong C. (2016). CD82 suppresses CD44 alternative splicing-dependent melanoma metastasis by mediating U2AF2 ubiquitination and degradation. Oncogene, 35(38), 5056-5069.
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3

Generation and Purification of Anti-CD44v8-10 Antibodies

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Polyclonal antibodies against CD44v8-10 molecule were generated and purified as described previously46 (link), 47 (link). Briefly, New Zealand White female rabbits were immunized with a GST-CD44v8-10 fusion protein, and the resulting anti-CD44v8-10 antibody was immunoaffinity purified with a GST-CD44v8-10 affinity column. FFPE from patient and mouse samples were incubated with commercial antibodies, anti-CD44v7/8 (VFF-17, Serotec, Inc., Raleigh, NC), CD44v9 (11.24, IgG 1), CD44v10 (Millipore, Billerica, MA), U2AF2 (Abcam, Eugene, OR) or CD82 (Novus Biologicals, Littleton, CO) or immunopurified anti-CD44v8-10. Then, the samples were incubated with horseradish peroxidase (HRP) conjugated-secondary antibodies (Abcam, Eugene, OR). The target proteins were detected with 3,3′diaminobenzidine (DAB). Nuclei counterstained with hematoxylin. The gray values of staining were quantified with ImageJ.
Zhang P., Feng S., Liu G., Wang H., Fu A., Zhu H., Ren Q., Wang B., Xu X., Bai H, & Dong C. (2016). CD82 suppresses CD44 alternative splicing-dependent melanoma metastasis by mediating U2AF2 ubiquitination and degradation. Oncogene, 35(38), 5056-5069.
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4

Generation and Purification of Anti-CD44v8-10 Antibodies

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Polyclonal antibodies against CD44v8-10 molecule were generated and purified as described previously46 (link), 47 (link). Briefly, New Zealand White female rabbits were immunized with a GST-CD44v8-10 fusion protein, and the resulting anti-CD44v8-10 antibody was immunoaffinity purified with a GST-CD44v8-10 affinity column. FFPE from patient and mouse samples were incubated with commercial antibodies, anti-CD44v7/8 (VFF-17, Serotec, Inc., Raleigh, NC), CD44v9 (11.24, IgG 1), CD44v10 (Millipore, Billerica, MA), U2AF2 (Abcam, Eugene, OR) or CD82 (Novus Biologicals, Littleton, CO) or immunopurified anti-CD44v8-10. Then, the samples were incubated with horseradish peroxidase (HRP) conjugated-secondary antibodies (Abcam, Eugene, OR). The target proteins were detected with 3,3′diaminobenzidine (DAB). Nuclei counterstained with hematoxylin. The gray values of staining were quantified with ImageJ.
Zhang P., Feng S., Liu G., Wang H., Fu A., Zhu H., Ren Q., Wang B., Xu X., Bai H, & Dong C. (2016). CD82 suppresses CD44 alternative splicing-dependent melanoma metastasis by mediating U2AF2 ubiquitination and degradation. Oncogene, 35(38), 5056-5069.
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5

Western Blot Analysis of Protein Expression

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Western blotting analysis of protein expression was described previously5 (link). CD44 (clone 2C5), CD82 (Life Technologies), U2AF2 (Abcam, Eugene, OR), FAK (Abcam, Eugene, OR), pY397 FAK (Abcam, Eugene, OR), Src (Santa Cruz, Dallas, TX), pY416 Src (Cell Signaling Technology, Danvers, MA), and RhoA (Abcam, Eugene, OR) were detected with corresponding primary monoclonal antibodies (1:1000 diluted in blocking buffer). For examining the effect of CD82 overexpression on U2AF2 ubiquitination, melanoma cells were treated with 10 μM MG132 for 6 hr before U2AF2 was immunoprecipitated, resolved in SDS-PAGE, transferred to a nitrocellulose membrane and developed with anti-ubiquitin P4D1 (1:1,000, Santa Cruz) and anti-U2AF2 antibodies.
Zhang P., Feng S., Liu G., Wang H., Fu A., Zhu H., Ren Q., Wang B., Xu X., Bai H, & Dong C. (2016). CD82 suppresses CD44 alternative splicing-dependent melanoma metastasis by mediating U2AF2 ubiquitination and degradation. Oncogene, 35(38), 5056-5069.
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