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  • 94
    Cell Signaling Technology Inc monoclonal antibodies to bad
    Expression analysis of Bmf and Bim in different leukocyte subsets. (A) Cells of the indicated differentiation stages were isolated from WT mice by cell surface marker staining and FACS sorting. Cells were lysed, and proteins were size fractioned by SDS-PAGE and transferred onto nitrocellulose membranes. Protein expression was evaluated using <t>monoclonal</t> antibodies recognizing mouse Bmf, Bim, or ERK (loading control). Membranes were stripped before subsequent reprobing with <t>anti-Bim–</t> and -ERK–specific antibodies, respectively. (B) Total thymocytes and CD19 + B cells from WT and bmf −/− mice were analyzed for expression of Bim, <t>Bad,</t> and Puma. Reprobing with an anti-ERK–specific antibody served as loading control. (C) B cell subsets of the indicated differentiation stages were isolated from WT or Bmf-deficient mice by cell surface marker staining and FACS sorting and processed as in A.
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    Expression analysis of Bmf and Bim in different leukocyte subsets. (A) Cells of the indicated differentiation stages were isolated from WT mice by cell surface marker staining and FACS sorting. Cells were lysed, and proteins were size fractioned by SDS-PAGE and transferred onto nitrocellulose membranes. Protein expression was evaluated using <t>monoclonal</t> antibodies recognizing mouse Bmf, Bim, or ERK (loading control). Membranes were stripped before subsequent reprobing with <t>anti-Bim–</t> and -ERK–specific antibodies, respectively. (B) Total thymocytes and CD19 + B cells from WT and bmf −/− mice were analyzed for expression of Bim, <t>Bad,</t> and Puma. Reprobing with an anti-ERK–specific antibody served as loading control. (C) B cell subsets of the indicated differentiation stages were isolated from WT or Bmf-deficient mice by cell surface marker staining and FACS sorting and processed as in A.
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    Expression analysis of Bmf and Bim in different leukocyte subsets. (A) Cells of the indicated differentiation stages were isolated from WT mice by cell surface marker staining and FACS sorting. Cells were lysed, and proteins were size fractioned by SDS-PAGE and transferred onto nitrocellulose membranes. Protein expression was evaluated using <t>monoclonal</t> antibodies recognizing mouse Bmf, Bim, or ERK (loading control). Membranes were stripped before subsequent reprobing with <t>anti-Bim–</t> and -ERK–specific antibodies, respectively. (B) Total thymocytes and CD19 + B cells from WT and bmf −/− mice were analyzed for expression of Bim, <t>Bad,</t> and Puma. Reprobing with an anti-ERK–specific antibody served as loading control. (C) B cell subsets of the indicated differentiation stages were isolated from WT or Bmf-deficient mice by cell surface marker staining and FACS sorting and processed as in A.
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    Expression analysis of Bmf and Bim in different leukocyte subsets. (A) Cells of the indicated differentiation stages were isolated from WT mice by cell surface marker staining and FACS sorting. Cells were lysed, and proteins were size fractioned by SDS-PAGE and transferred onto nitrocellulose membranes. Protein expression was evaluated using <t>monoclonal</t> antibodies recognizing mouse Bmf, Bim, or ERK (loading control). Membranes were stripped before subsequent reprobing with <t>anti-Bim–</t> and -ERK–specific antibodies, respectively. (B) Total thymocytes and CD19 + B cells from WT and bmf −/− mice were analyzed for expression of Bim, <t>Bad,</t> and Puma. Reprobing with an anti-ERK–specific antibody served as loading control. (C) B cell subsets of the indicated differentiation stages were isolated from WT or Bmf-deficient mice by cell surface marker staining and FACS sorting and processed as in A.
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    Cell Signaling Technology Inc rabbit bad
    Expression analysis of Bmf and Bim in different leukocyte subsets. (A) Cells of the indicated differentiation stages were isolated from WT mice by cell surface marker staining and FACS sorting. Cells were lysed, and proteins were size fractioned by SDS-PAGE and transferred onto nitrocellulose membranes. Protein expression was evaluated using <t>monoclonal</t> antibodies recognizing mouse Bmf, Bim, or ERK (loading control). Membranes were stripped before subsequent reprobing with <t>anti-Bim–</t> and -ERK–specific antibodies, respectively. (B) Total thymocytes and CD19 + B cells from WT and bmf −/− mice were analyzed for expression of Bim, <t>Bad,</t> and Puma. Reprobing with an anti-ERK–specific antibody served as loading control. (C) B cell subsets of the indicated differentiation stages were isolated from WT or Bmf-deficient mice by cell surface marker staining and FACS sorting and processed as in A.
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    Image Search Results


    Expression analysis of Bmf and Bim in different leukocyte subsets. (A) Cells of the indicated differentiation stages were isolated from WT mice by cell surface marker staining and FACS sorting. Cells were lysed, and proteins were size fractioned by SDS-PAGE and transferred onto nitrocellulose membranes. Protein expression was evaluated using monoclonal antibodies recognizing mouse Bmf, Bim, or ERK (loading control). Membranes were stripped before subsequent reprobing with anti-Bim– and -ERK–specific antibodies, respectively. (B) Total thymocytes and CD19 + B cells from WT and bmf −/− mice were analyzed for expression of Bim, Bad, and Puma. Reprobing with an anti-ERK–specific antibody served as loading control. (C) B cell subsets of the indicated differentiation stages were isolated from WT or Bmf-deficient mice by cell surface marker staining and FACS sorting and processed as in A.

    Journal: The Journal of Experimental Medicine

    Article Title: Loss of the BH3-only protein Bmf impairs B cell homeostasis and accelerates γ irradiation–induced thymic lymphoma development

    doi: 10.1084/jem.20071658

    Figure Lengend Snippet: Expression analysis of Bmf and Bim in different leukocyte subsets. (A) Cells of the indicated differentiation stages were isolated from WT mice by cell surface marker staining and FACS sorting. Cells were lysed, and proteins were size fractioned by SDS-PAGE and transferred onto nitrocellulose membranes. Protein expression was evaluated using monoclonal antibodies recognizing mouse Bmf, Bim, or ERK (loading control). Membranes were stripped before subsequent reprobing with anti-Bim– and -ERK–specific antibodies, respectively. (B) Total thymocytes and CD19 + B cells from WT and bmf −/− mice were analyzed for expression of Bim, Bad, and Puma. Reprobing with an anti-ERK–specific antibody served as loading control. (C) B cell subsets of the indicated differentiation stages were isolated from WT or Bmf-deficient mice by cell surface marker staining and FACS sorting and processed as in A.

    Article Snippet: Membranes were probed with rabbit anti-Puma antiserum (Cell Signaling Technology), monoclonal antibodies to Bad (Cell Signaling Technology), active caspase-3 (Cell Signaling Technology), rat anti–mouse Bmf mAb (17A9) or rat anti–mouse, rat, human, monkey, dog Bim (3C5), generated at the WEHI and now commercially available from Alexis.

    Techniques: Expressing, Isolation, Marker, Staining, SDS Page