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rotofor ief apparatus bio rad  (Bio-Rad)


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    Bio-Rad rotofor ief apparatus bio rad
    Rotofor Ief Apparatus Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 157 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rotofor+ief+apparatus+bio+rad/pmc04950035-188-1-4?v=Bio-Rad
    Average 93 stars, based on 157 article reviews
    rotofor ief apparatus bio rad - by Bioz Stars, 2026-07
    93/100 stars

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    FIG. 3. Analysis of Triton X-114 extracts by preparative <t>IEF</t> and determination of the N-terminal sequence of the 29-kDa protein. The aqueous phases of the Triton extracts were separated into 20 fractions by preparative IEF with the <t>Rotofor</t> cell. Each fraction was analyzed by SDS-PAGE (A) and immunoblotting (B). The gels were stained with Coomassie blue. The PVDF membrane was incubated with patient sera and visualized with anti-human IgM. Lane 1, pooled fractions from fractions 1 to 3; lanes 2, fraction 5; lanes 3, fraction 6; lanes 4, fraction 7; lanes 5, pooled fractions 11 and 12; lanes 6, pooled fractions 17 and 18; lanes 7, pooled fractions 19 and 20; lanes 8, Triton X-114 extract, aqueous phase.
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    FIG. 3. Analysis of Triton X-114 extracts by preparative <t>IEF</t> and determination of the N-terminal sequence of the 29-kDa protein. The aqueous phases of the Triton extracts were separated into 20 fractions by preparative IEF with the <t>Rotofor</t> cell. Each fraction was analyzed by SDS-PAGE (A) and immunoblotting (B). The gels were stained with Coomassie blue. The PVDF membrane was incubated with patient sera and visualized with anti-human IgM. Lane 1, pooled fractions from fractions 1 to 3; lanes 2, fraction 5; lanes 3, fraction 6; lanes 4, fraction 7; lanes 5, pooled fractions 11 and 12; lanes 6, pooled fractions 17 and 18; lanes 7, pooled fractions 19 and 20; lanes 8, Triton X-114 extract, aqueous phase.
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    FIG. 3. Analysis of Triton X-114 extracts by preparative IEF and determination of the N-terminal sequence of the 29-kDa protein. The aqueous phases of the Triton extracts were separated into 20 fractions by preparative IEF with the Rotofor cell. Each fraction was analyzed by SDS-PAGE (A) and immunoblotting (B). The gels were stained with Coomassie blue. The PVDF membrane was incubated with patient sera and visualized with anti-human IgM. Lane 1, pooled fractions from fractions 1 to 3; lanes 2, fraction 5; lanes 3, fraction 6; lanes 4, fraction 7; lanes 5, pooled fractions 11 and 12; lanes 6, pooled fractions 17 and 18; lanes 7, pooled fractions 19 and 20; lanes 8, Triton X-114 extract, aqueous phase.

    Journal: Clinical and Vaccine Immunology

    Article Title: Mycobacterium tuberculosis HBHA Protein Reacts Strongly with the Serum Immunoglobulin M of Tuberculosis Patients

    doi: 10.1128/cvi.00103-06

    Figure Lengend Snippet: FIG. 3. Analysis of Triton X-114 extracts by preparative IEF and determination of the N-terminal sequence of the 29-kDa protein. The aqueous phases of the Triton extracts were separated into 20 fractions by preparative IEF with the Rotofor cell. Each fraction was analyzed by SDS-PAGE (A) and immunoblotting (B). The gels were stained with Coomassie blue. The PVDF membrane was incubated with patient sera and visualized with anti-human IgM. Lane 1, pooled fractions from fractions 1 to 3; lanes 2, fraction 5; lanes 3, fraction 6; lanes 4, fraction 7; lanes 5, pooled fractions 11 and 12; lanes 6, pooled fractions 17 and 18; lanes 7, pooled fractions 19 and 20; lanes 8, Triton X-114 extract, aqueous phase.

    Article Snippet: The Triton-soluble proteins were fractionated in a preparative isoelectric focusing (IEF) apparatus (Rotofor Cell; Bio-Rad, Hercules, CA).

    Techniques: Sequencing, SDS Page, Western Blot, Staining, Membrane, Incubation