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mini rotofor chamber  (Bio-Rad)


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    Structured Review

    Bio-Rad mini rotofor chamber
    Fig. 9 One-step purification of Chi54 and its mutated chitin- ases. a Silver staining after SDS-PAGE with culture super- natant of recombinant E. coli (lane 0) and samples obtained in each fraction of the <t>Rotofor</t> cell (lanes 6–20). b Silver staining after SDS-PAGE with samples obtained in fractions 18–20, where lanes 1–7 indicate pro- teins of Chi54, T218S, I270V, I270L, N401V, V493M, and S497E, respectively, and M indicates the molecular weight marker
    Mini Rotofor Chamber, 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/result/mini rotofor chamber/product/Bio-Rad
    Average 93 stars, based on 157 article reviews
    mini rotofor chamber - by Bioz Stars, 2026-05
    93/100 stars

    Images

    1) Product Images from "Cloning and high-level production of a chitinase from Chromobacterium sp. and the role of conserved or nonconserved residues on its catalytic activity."

    Article Title: Cloning and high-level production of a chitinase from Chromobacterium sp. and the role of conserved or nonconserved residues on its catalytic activity.

    Journal: Applied microbiology and biotechnology

    doi: 10.1007/s00253-006-0614-0

    Fig. 9 One-step purification of Chi54 and its mutated chitin- ases. a Silver staining after SDS-PAGE with culture super- natant of recombinant E. coli (lane 0) and samples obtained in each fraction of the Rotofor cell (lanes 6–20). b Silver staining after SDS-PAGE with samples obtained in fractions 18–20, where lanes 1–7 indicate pro- teins of Chi54, T218S, I270V, I270L, N401V, V493M, and S497E, respectively, and M indicates the molecular weight marker
    Figure Legend Snippet: Fig. 9 One-step purification of Chi54 and its mutated chitin- ases. a Silver staining after SDS-PAGE with culture super- natant of recombinant E. coli (lane 0) and samples obtained in each fraction of the Rotofor cell (lanes 6–20). b Silver staining after SDS-PAGE with samples obtained in fractions 18–20, where lanes 1–7 indicate pro- teins of Chi54, T218S, I270V, I270L, N401V, V493M, and S497E, respectively, and M indicates the molecular weight marker

    Techniques Used: Purification, Silver Staining, SDS Page, Recombinant, Molecular Weight, Marker



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    Fig. 9 One-step purification of Chi54 and its mutated chitin- ases. a Silver staining after SDS-PAGE with culture super- natant of recombinant E. coli (lane 0) and samples obtained in each fraction of the <t>Rotofor</t> cell (lanes 6–20). b Silver staining after SDS-PAGE with samples obtained in fractions 18–20, where lanes 1–7 indicate pro- teins of Chi54, T218S, I270V, I270L, N401V, V493M, and S497E, respectively, and M indicates the molecular weight marker
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    Fig. 9 One-step purification of Chi54 and its mutated chitin- ases. a Silver staining after SDS-PAGE with culture super- natant of recombinant E. coli (lane 0) and samples obtained in each fraction of the <t>Rotofor</t> cell (lanes 6–20). b Silver staining after SDS-PAGE with samples obtained in fractions 18–20, where lanes 1–7 indicate pro- teins of Chi54, T218S, I270V, I270L, N401V, V493M, and S497E, respectively, and M indicates the molecular weight marker
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    Purified 23K and 35K forms of the ORF3 protein. Sf9 cells were infected with ORF3NHA baculovirus recombinant. The ORF3NHA protein was purified by extraction with 1.5% CHAPS and preparative IEF with a Bio-Rad <t>Rotofor.</t> The purified ORF3NHA protein was resolved by SDS-18% PAGE and Coomassie blue R-250 staining. 35K band A and 23K band B were sequenced by using MALDI-TOF mass spectrometry.
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    Image Search Results


    Fig. 9 One-step purification of Chi54 and its mutated chitin- ases. a Silver staining after SDS-PAGE with culture super- natant of recombinant E. coli (lane 0) and samples obtained in each fraction of the Rotofor cell (lanes 6–20). b Silver staining after SDS-PAGE with samples obtained in fractions 18–20, where lanes 1–7 indicate pro- teins of Chi54, T218S, I270V, I270L, N401V, V493M, and S497E, respectively, and M indicates the molecular weight marker

    Journal: Applied microbiology and biotechnology

    Article Title: Cloning and high-level production of a chitinase from Chromobacterium sp. and the role of conserved or nonconserved residues on its catalytic activity.

    doi: 10.1007/s00253-006-0614-0

    Figure Lengend Snippet: Fig. 9 One-step purification of Chi54 and its mutated chitin- ases. a Silver staining after SDS-PAGE with culture super- natant of recombinant E. coli (lane 0) and samples obtained in each fraction of the Rotofor cell (lanes 6–20). b Silver staining after SDS-PAGE with samples obtained in fractions 18–20, where lanes 1–7 indicate pro- teins of Chi54, T218S, I270V, I270L, N401V, V493M, and S497E, respectively, and M indicates the molecular weight marker

    Article Snippet: The samples were loaded in a Mini Rotofor chamber (BioRad, Hercules, California) and run at 12 W constant power for 4 h with 0.1 M H3PO4 at the anode and 0.1 M NaOH at the cathode.

    Techniques: Purification, Silver Staining, SDS Page, Recombinant, Molecular Weight, Marker

    Purified 23K and 35K forms of the ORF3 protein. Sf9 cells were infected with ORF3NHA baculovirus recombinant. The ORF3NHA protein was purified by extraction with 1.5% CHAPS and preparative IEF with a Bio-Rad Rotofor. The purified ORF3NHA protein was resolved by SDS-18% PAGE and Coomassie blue R-250 staining. 35K band A and 23K band B were sequenced by using MALDI-TOF mass spectrometry.

    Journal:

    Article Title: Two Nonoverlapping Domains on the Norwalk Virus Open Reading Frame 3 (ORF3) Protein Are Involved in the Formation of the Phosphorylated 35K Protein and in ORF3-Capsid Protein Interactions

    doi: 10.1128/JVI.77.6.3569-3577.2003

    Figure Lengend Snippet: Purified 23K and 35K forms of the ORF3 protein. Sf9 cells were infected with ORF3NHA baculovirus recombinant. The ORF3NHA protein was purified by extraction with 1.5% CHAPS and preparative IEF with a Bio-Rad Rotofor. The purified ORF3NHA protein was resolved by SDS-18% PAGE and Coomassie blue R-250 staining. 35K band A and 23K band B were sequenced by using MALDI-TOF mass spectrometry.

    Article Snippet: The fractions containing proteins with pIs between 4.5 and 4.8 were pooled and refocused by using a Bio-Rad 18-ml mini Rotofor chamber at a constant power of 12 W with 0.5% ampholytes (pH range, 3 to 5) as described above.

    Techniques: Purification, Infection, Recombinant, Staining, Mass Spectrometry