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pk mito orange  (New England Biolabs)


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    New England Biolabs pk mito orange
    OCIAD1 localizes predominantly in the outer membrane of mitochondria (A) Subcellular fractionation of HEK293 cells that expressed OCIAD1 FLAG and an empty vector. T, total; C, cytosol; M, mitochondria; US, ultracentrifugation supernatant; V, light membranes. (B) Extraction of proteins by sodium carbonate. Samples were analyzed by SDS-PAGE and western blot. Membr., membranes. (C) Localization of mitochondrial proteins, analyzed by limited degradation with proteinase K in intact mitochondria (250 mM sucrose), mitoplasts (5 mM sucrose), and mitochondrial lysates (1% Triton X-100). The samples were analyzed by SDS-PAGE and western blot. Mitos, mitochondria; Mitopl, mitoplasts; Sup, supernatant; OM, outer membrane; IM, inner membrane; IMS, intermembrane space. (D and E) Mitochondria isolated from HEK293 and HeLa (D) or U-2 OS (E) cells were treated with increasing concentrations of proteinase K. The samples were then analyzed with SDS-PAGE followed by western blotting. (F and G) Submitochondrial localization <t>of</t> <t>OCIAD1-SNAP</t> in HeLa cells visualized by live-cell 2D STED microscopy. Cells were transfected with a plasmid encoding OCIAD-SNAP and labeled with SNAP-cell 647-SiR and the inner membrane (IM) marker PK <t>Mito</t> Orange (PKMO). The image shows a 2D projection of the mitochondrial tubules. (F) Representative dual-color STED recording. (G) Fluorescence intensity line profiles were measured at the sites indicated by arrowheads in the composite view. The fluorescence intensity was estimated along the transparent dashed lines, normalized, and plotted. Scale bar: 1 μm. See also <xref ref-type=Figures S1 and . " width="250" height="auto" />
    Pk Mito Orange, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 98/100, based on 337 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pk+mito+orange/SNAP-Cell+647-SiR/pmc11672691-530-7-15
    Average 98 stars, based on 337 article reviews
    pk mito orange - by Bioz Stars, 2026-10
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    1) Product Images from "OCIAD1 and prohibitins regulate the stability of the TIM23 protein translocase"

    Article Title: OCIAD1 and prohibitins regulate the stability of the TIM23 protein translocase

    Journal: Cell Reports

    doi: 10.1016/j.celrep.2024.115038

    OCIAD1 localizes predominantly in the outer membrane of mitochondria (A) Subcellular fractionation of HEK293 cells that expressed OCIAD1 FLAG and an empty vector. T, total; C, cytosol; M, mitochondria; US, ultracentrifugation supernatant; V, light membranes. (B) Extraction of proteins by sodium carbonate. Samples were analyzed by SDS-PAGE and western blot. Membr., membranes. (C) Localization of mitochondrial proteins, analyzed by limited degradation with proteinase K in intact mitochondria (250 mM sucrose), mitoplasts (5 mM sucrose), and mitochondrial lysates (1% Triton X-100). The samples were analyzed by SDS-PAGE and western blot. Mitos, mitochondria; Mitopl, mitoplasts; Sup, supernatant; OM, outer membrane; IM, inner membrane; IMS, intermembrane space. (D and E) Mitochondria isolated from HEK293 and HeLa (D) or U-2 OS (E) cells were treated with increasing concentrations of proteinase K. The samples were then analyzed with SDS-PAGE followed by western blotting. (F and G) Submitochondrial localization of OCIAD1-SNAP in HeLa cells visualized by live-cell 2D STED microscopy. Cells were transfected with a plasmid encoding OCIAD-SNAP and labeled with SNAP-cell 647-SiR and the inner membrane (IM) marker PK Mito Orange (PKMO). The image shows a 2D projection of the mitochondrial tubules. (F) Representative dual-color STED recording. (G) Fluorescence intensity line profiles were measured at the sites indicated by arrowheads in the composite view. The fluorescence intensity was estimated along the transparent dashed lines, normalized, and plotted. Scale bar: 1 μm. See also <xref ref-type=Figures S1 and . " title="... 647-SiR and the inner membrane (IM) marker PK Mito Orange (PKMO). The image shows a 2D projection ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: OCIAD1 localizes predominantly in the outer membrane of mitochondria (A) Subcellular fractionation of HEK293 cells that expressed OCIAD1 FLAG and an empty vector. T, total; C, cytosol; M, mitochondria; US, ultracentrifugation supernatant; V, light membranes. (B) Extraction of proteins by sodium carbonate. Samples were analyzed by SDS-PAGE and western blot. Membr., membranes. (C) Localization of mitochondrial proteins, analyzed by limited degradation with proteinase K in intact mitochondria (250 mM sucrose), mitoplasts (5 mM sucrose), and mitochondrial lysates (1% Triton X-100). The samples were analyzed by SDS-PAGE and western blot. Mitos, mitochondria; Mitopl, mitoplasts; Sup, supernatant; OM, outer membrane; IM, inner membrane; IMS, intermembrane space. (D and E) Mitochondria isolated from HEK293 and HeLa (D) or U-2 OS (E) cells were treated with increasing concentrations of proteinase K. The samples were then analyzed with SDS-PAGE followed by western blotting. (F and G) Submitochondrial localization of OCIAD1-SNAP in HeLa cells visualized by live-cell 2D STED microscopy. Cells were transfected with a plasmid encoding OCIAD-SNAP and labeled with SNAP-cell 647-SiR and the inner membrane (IM) marker PK Mito Orange (PKMO). The image shows a 2D projection of the mitochondrial tubules. (F) Representative dual-color STED recording. (G) Fluorescence intensity line profiles were measured at the sites indicated by arrowheads in the composite view. The fluorescence intensity was estimated along the transparent dashed lines, normalized, and plotted. Scale bar: 1 μm. See also Figures S1 and .

    Techniques Used: Membrane, Fractionation, Plasmid Preparation, Extraction, SDS Page, Western Blot, Isolation, Microscopy, Transfection, Labeling, Marker, Fluorescence

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    Staining:

    Article Title: OCIAD1 and prohibitins regulate the stability of the TIM23 protein translocase
    Article Snippet: Cells were seeded in 3.5 cm glass bottom dishes (Ibidi GmbH, Gräfelfing, Germany) and cultivated over night at 37°C and 5% CO 2 . .. The cells were stained with 200 nM PK Mito Orange and 1 μM SNAP-cell 647-SiR (NEB) as described previously. .. Stimulated emission depletion (STED) nanoscopy was performed using a dual-color Expert Line STED microscope (Abberior Instruments, Göttingen, Germany) equipped with a 775 nm STED-Laser and an UPlanSApo 100×/1.40 Oil [infinity]/0.17/FN26.5 objective (Olympus, Tokyo, Japan).



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    OCIAD1 localizes predominantly in the outer membrane of mitochondria (A) Subcellular fractionation of HEK293 cells that expressed OCIAD1 FLAG and an empty vector. T, total; C, cytosol; M, mitochondria; US, ultracentrifugation supernatant; V, light membranes. (B) Extraction of proteins by sodium carbonate. Samples were analyzed by SDS-PAGE and western blot. Membr., membranes. (C) Localization of mitochondrial proteins, analyzed by limited degradation with proteinase K in intact mitochondria (250 mM sucrose), mitoplasts (5 mM sucrose), and mitochondrial lysates (1% Triton X-100). The samples were analyzed by SDS-PAGE and western blot. Mitos, mitochondria; Mitopl, mitoplasts; Sup, supernatant; OM, outer membrane; IM, inner membrane; IMS, intermembrane space. (D and E) Mitochondria isolated from HEK293 and HeLa (D) or U-2 OS (E) cells were treated with increasing concentrations of proteinase K. The samples were then analyzed with SDS-PAGE followed by western blotting. (F and G) Submitochondrial localization <t>of</t> <t>OCIAD1-SNAP</t> in HeLa cells visualized by live-cell 2D STED microscopy. Cells were transfected with a plasmid encoding OCIAD-SNAP and labeled with SNAP-cell 647-SiR and the inner membrane (IM) marker PK <t>Mito</t> Orange (PKMO). The image shows a 2D projection of the mitochondrial tubules. (F) Representative dual-color STED recording. (G) Fluorescence intensity line profiles were measured at the sites indicated by arrowheads in the composite view. The fluorescence intensity was estimated along the transparent dashed lines, normalized, and plotted. Scale bar: 1 μm. See also <xref ref-type=Figures S1 and . " width="250" height="auto" />
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    OCIAD1 localizes predominantly in the outer membrane of mitochondria (A) Subcellular fractionation of HEK293 cells that expressed OCIAD1 FLAG and an empty vector. T, total; C, cytosol; M, mitochondria; US, ultracentrifugation supernatant; V, light membranes. (B) Extraction of proteins by sodium carbonate. Samples were analyzed by SDS-PAGE and western blot. Membr., membranes. (C) Localization of mitochondrial proteins, analyzed by limited degradation with proteinase K in intact mitochondria (250 mM sucrose), mitoplasts (5 mM sucrose), and mitochondrial lysates (1% Triton X-100). The samples were analyzed by SDS-PAGE and western blot. Mitos, mitochondria; Mitopl, mitoplasts; Sup, supernatant; OM, outer membrane; IM, inner membrane; IMS, intermembrane space. (D and E) Mitochondria isolated from HEK293 and HeLa (D) or U-2 OS (E) cells were treated with increasing concentrations of proteinase K. The samples were then analyzed with SDS-PAGE followed by western blotting. (F and G) Submitochondrial localization <t>of</t> <t>OCIAD1-SNAP</t> in HeLa cells visualized by live-cell 2D STED microscopy. Cells were transfected with a plasmid encoding OCIAD-SNAP and labeled with SNAP-cell 647-SiR and the inner membrane (IM) marker PK <t>Mito</t> Orange (PKMO). The image shows a 2D projection of the mitochondrial tubules. (F) Representative dual-color STED recording. (G) Fluorescence intensity line profiles were measured at the sites indicated by arrowheads in the composite view. The fluorescence intensity was estimated along the transparent dashed lines, normalized, and plotted. Scale bar: 1 μm. See also <xref ref-type=Figures S1 and . " width="250" height="auto" />
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    Image Search Results


    OCIAD1 localizes predominantly in the outer membrane of mitochondria (A) Subcellular fractionation of HEK293 cells that expressed OCIAD1 FLAG and an empty vector. T, total; C, cytosol; M, mitochondria; US, ultracentrifugation supernatant; V, light membranes. (B) Extraction of proteins by sodium carbonate. Samples were analyzed by SDS-PAGE and western blot. Membr., membranes. (C) Localization of mitochondrial proteins, analyzed by limited degradation with proteinase K in intact mitochondria (250 mM sucrose), mitoplasts (5 mM sucrose), and mitochondrial lysates (1% Triton X-100). The samples were analyzed by SDS-PAGE and western blot. Mitos, mitochondria; Mitopl, mitoplasts; Sup, supernatant; OM, outer membrane; IM, inner membrane; IMS, intermembrane space. (D and E) Mitochondria isolated from HEK293 and HeLa (D) or U-2 OS (E) cells were treated with increasing concentrations of proteinase K. The samples were then analyzed with SDS-PAGE followed by western blotting. (F and G) Submitochondrial localization of OCIAD1-SNAP in HeLa cells visualized by live-cell 2D STED microscopy. Cells were transfected with a plasmid encoding OCIAD-SNAP and labeled with SNAP-cell 647-SiR and the inner membrane (IM) marker PK Mito Orange (PKMO). The image shows a 2D projection of the mitochondrial tubules. (F) Representative dual-color STED recording. (G) Fluorescence intensity line profiles were measured at the sites indicated by arrowheads in the composite view. The fluorescence intensity was estimated along the transparent dashed lines, normalized, and plotted. Scale bar: 1 μm. See also <xref ref-type=Figures S1 and . " width="100%" height="100%">

    Journal: Cell Reports

    Article Title: OCIAD1 and prohibitins regulate the stability of the TIM23 protein translocase

    doi: 10.1016/j.celrep.2024.115038

    Figure Lengend Snippet: OCIAD1 localizes predominantly in the outer membrane of mitochondria (A) Subcellular fractionation of HEK293 cells that expressed OCIAD1 FLAG and an empty vector. T, total; C, cytosol; M, mitochondria; US, ultracentrifugation supernatant; V, light membranes. (B) Extraction of proteins by sodium carbonate. Samples were analyzed by SDS-PAGE and western blot. Membr., membranes. (C) Localization of mitochondrial proteins, analyzed by limited degradation with proteinase K in intact mitochondria (250 mM sucrose), mitoplasts (5 mM sucrose), and mitochondrial lysates (1% Triton X-100). The samples were analyzed by SDS-PAGE and western blot. Mitos, mitochondria; Mitopl, mitoplasts; Sup, supernatant; OM, outer membrane; IM, inner membrane; IMS, intermembrane space. (D and E) Mitochondria isolated from HEK293 and HeLa (D) or U-2 OS (E) cells were treated with increasing concentrations of proteinase K. The samples were then analyzed with SDS-PAGE followed by western blotting. (F and G) Submitochondrial localization of OCIAD1-SNAP in HeLa cells visualized by live-cell 2D STED microscopy. Cells were transfected with a plasmid encoding OCIAD-SNAP and labeled with SNAP-cell 647-SiR and the inner membrane (IM) marker PK Mito Orange (PKMO). The image shows a 2D projection of the mitochondrial tubules. (F) Representative dual-color STED recording. (G) Fluorescence intensity line profiles were measured at the sites indicated by arrowheads in the composite view. The fluorescence intensity was estimated along the transparent dashed lines, normalized, and plotted. Scale bar: 1 μm. See also Figures S1 and .

    Article Snippet: The cells were stained with 200 nM PK Mito Orange and 1 μM SNAP-cell 647-SiR (NEB) as described previously.

    Techniques: Membrane, Fractionation, Plasmid Preparation, Extraction, SDS Page, Western Blot, Isolation, Microscopy, Transfection, Labeling, Marker, Fluorescence