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    These lysates were also immunoprecipitated with
    the same anti-Tax-2B antibody. The input represents 1/10 of the immunoprecipitated lysate.
    Additional file 2: Tax-1 and Tax-2B colocalize with endogenous p300 in nuclear punctate structures.

    293T cells were either transfected or not with the vectors expressing Tax-1 or Tax-2B.

    The cells were fixed and analyzed by dual immunofluorescence staining
    with the anti-Tax-1 IgG2a monoclonal antibody or the anti-Tax-2B rabbit polyclonal antibody and an anti-p300 IgG1 monoclonal antibody.

    The secondary antibodies were goat anti-mouse IgG2a conjugated to
    Dylight 488, goat anti-mouse IgG1 antibody conjugated to Dylight 649 and goat anti-rabbit IgG antibody conjugated to Dylight 549.
    The images were collected using a laser scanning confocal microscope.
    DIC, differential inference contrast. Additional file 3: The wild type Tax-2B fusion to
    ubiquitin colocalizes with IKKγ in prominent cytoplasmic structures closely associated with the
    Golgi apparatus. 293T cells transfected or not with the vector expressing the Tax-2-Ub fusion were fixed and
    analyzed by dual immunofluorescence staining with anti-Tax-2B rabbit polyclonal antibody and (A) anti-GM130
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    The images were collected using a laser scanning confocal microscopy.
    DIC, differential inference contrast. Below are the links to the authors’ original
    submitted files for images. Open Access This article is published under license to BioMed Central Ltd.
    Turci, M., Lodewick, J., Di Gennaro, G. et al. Ubiquitination and sumoylation of the HTLV-2
    Tax-2B protein regulate its NF-κB activity: a comparative study with the HTLV-1 Tax-1 protein. Sorry,
    a shareable link is not currently available for this article.
    By using this website, you agree to our Terms and
    Conditions, California Privacy Statement, Privacy statement and Cookies policy.
    Manage cookies/Do not sell my data we use in the preference centre.
    2022 BioMed Central Ltd unless otherwise stated. Part of Springer Nature.

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