gel filtration chromatography whole cell extracts  (GE Healthcare)

 
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    GE Healthcare gel filtration chromatography whole cell extracts
    Mrpl44 forms multimers as part of the large subunit of the mitoribosome. (A) HEK293T cells were co-transfected with Mrpl44FLAG and Mrpl44GFP; or FLAGBak and Mrpl44GFP, as a negative control. Lysates were immunoprecipitated with αFLAG, then blotted with an αGFP antibody to determine co-IP. Results are representative of three independent experiments. (B) NIH3T3 <t>whole</t> <t>cell</t> <t>extracts</t> were fractionated by HPLC on a Superose 6 column. The fractions were collected and alternate fractions from 14 to 30 were run on an SDS-PAGE <t>gel,</t> then blotted with antibodies against Mrpl44 as well as Mrpl12 and Mrps15, known components of the mitoribosome. (C) Mitochondrial fractions were obtained from Mrpl44FLAG NIH3T3 cells, and FLAGBak NIH3T3 cells, as a negative control, and immunoprecipitated with αFLAG agarose beads. RNA was then extracted and analysed for pulldown of the mitochondrial rRNA subunits by quantitative RT-PCR. The mean +/- SEM of three independent experiments is shown. Statistical analysis performed using multiple t-test with Holm-Sidak correction for multiple comparisons (*p
    Gel Filtration Chromatography Whole Cell Extracts, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gel filtration chromatography whole cell extracts/product/GE Healthcare
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gel filtration chromatography whole cell extracts - by Bioz Stars, 2020-08
    88/100 stars

    Related Products / Commonly Used Together

    pre-packed superose 6 gel-filtration column
    waters hplc system

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    1) Product Images from "A Role for the Mitochondrial Protein Mrpl44 in Maintaining OXPHOS Capacity"

    Article Title: A Role for the Mitochondrial Protein Mrpl44 in Maintaining OXPHOS Capacity

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0134326

    Mrpl44 forms multimers as part of the large subunit of the mitoribosome. (A) HEK293T cells were co-transfected with Mrpl44FLAG and Mrpl44GFP; or FLAGBak and Mrpl44GFP, as a negative control. Lysates were immunoprecipitated with αFLAG, then blotted with an αGFP antibody to determine co-IP. Results are representative of three independent experiments. (B) NIH3T3 whole cell extracts were fractionated by HPLC on a Superose 6 column. The fractions were collected and alternate fractions from 14 to 30 were run on an SDS-PAGE gel, then blotted with antibodies against Mrpl44 as well as Mrpl12 and Mrps15, known components of the mitoribosome. (C) Mitochondrial fractions were obtained from Mrpl44FLAG NIH3T3 cells, and FLAGBak NIH3T3 cells, as a negative control, and immunoprecipitated with αFLAG agarose beads. RNA was then extracted and analysed for pulldown of the mitochondrial rRNA subunits by quantitative RT-PCR. The mean +/- SEM of three independent experiments is shown. Statistical analysis performed using multiple t-test with Holm-Sidak correction for multiple comparisons (*p
    Figure Legend Snippet: Mrpl44 forms multimers as part of the large subunit of the mitoribosome. (A) HEK293T cells were co-transfected with Mrpl44FLAG and Mrpl44GFP; or FLAGBak and Mrpl44GFP, as a negative control. Lysates were immunoprecipitated with αFLAG, then blotted with an αGFP antibody to determine co-IP. Results are representative of three independent experiments. (B) NIH3T3 whole cell extracts were fractionated by HPLC on a Superose 6 column. The fractions were collected and alternate fractions from 14 to 30 were run on an SDS-PAGE gel, then blotted with antibodies against Mrpl44 as well as Mrpl12 and Mrps15, known components of the mitoribosome. (C) Mitochondrial fractions were obtained from Mrpl44FLAG NIH3T3 cells, and FLAGBak NIH3T3 cells, as a negative control, and immunoprecipitated with αFLAG agarose beads. RNA was then extracted and analysed for pulldown of the mitochondrial rRNA subunits by quantitative RT-PCR. The mean +/- SEM of three independent experiments is shown. Statistical analysis performed using multiple t-test with Holm-Sidak correction for multiple comparisons (*p

    Techniques Used: Transfection, Negative Control, Immunoprecipitation, Co-Immunoprecipitation Assay, High Performance Liquid Chromatography, SDS Page, Quantitative RT-PCR

    Related Articles

    High Performance Liquid Chromatography:

    Article Title: A Role for the Mitochondrial Protein Mrpl44 in Maintaining OXPHOS Capacity
    Article Snippet: .. Gel Filtration Chromatography Whole cell extracts were fractionated using a Waters HPLC system on a pre-packed Superose 6 gel-filtration column (300mm x 10mm internal diameter, GE Healthcare) equilibrated in 0.5% Triton X-100 in 20mM Tris-HCl, pH7.5, 150mM NaCl containing protease inhibitors. ..

    Filtration:

    Article Title: A Role for the Mitochondrial Protein Mrpl44 in Maintaining OXPHOS Capacity
    Article Snippet: .. Gel Filtration Chromatography Whole cell extracts were fractionated using a Waters HPLC system on a pre-packed Superose 6 gel-filtration column (300mm x 10mm internal diameter, GE Healthcare) equilibrated in 0.5% Triton X-100 in 20mM Tris-HCl, pH7.5, 150mM NaCl containing protease inhibitors. ..

    Chromatography:

    Article Title: A Role for the Mitochondrial Protein Mrpl44 in Maintaining OXPHOS Capacity
    Article Snippet: .. Gel Filtration Chromatography Whole cell extracts were fractionated using a Waters HPLC system on a pre-packed Superose 6 gel-filtration column (300mm x 10mm internal diameter, GE Healthcare) equilibrated in 0.5% Triton X-100 in 20mM Tris-HCl, pH7.5, 150mM NaCl containing protease inhibitors. ..

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    GE Healthcare gel filtration chromatography whole cell extracts
    Mrpl44 forms multimers as part of the large subunit of the mitoribosome. (A) HEK293T cells were co-transfected with Mrpl44FLAG and Mrpl44GFP; or FLAGBak and Mrpl44GFP, as a negative control. Lysates were immunoprecipitated with αFLAG, then blotted with an αGFP antibody to determine co-IP. Results are representative of three independent experiments. (B) NIH3T3 <t>whole</t> <t>cell</t> <t>extracts</t> were fractionated by HPLC on a Superose 6 column. The fractions were collected and alternate fractions from 14 to 30 were run on an SDS-PAGE <t>gel,</t> then blotted with antibodies against Mrpl44 as well as Mrpl12 and Mrps15, known components of the mitoribosome. (C) Mitochondrial fractions were obtained from Mrpl44FLAG NIH3T3 cells, and FLAGBak NIH3T3 cells, as a negative control, and immunoprecipitated with αFLAG agarose beads. RNA was then extracted and analysed for pulldown of the mitochondrial rRNA subunits by quantitative RT-PCR. The mean +/- SEM of three independent experiments is shown. Statistical analysis performed using multiple t-test with Holm-Sidak correction for multiple comparisons (*p
    Gel Filtration Chromatography Whole Cell Extracts, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gel filtration chromatography whole cell extracts/product/GE Healthcare
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gel filtration chromatography whole cell extracts - by Bioz Stars, 2020-08
    88/100 stars
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    Mrpl44 forms multimers as part of the large subunit of the mitoribosome. (A) HEK293T cells were co-transfected with Mrpl44FLAG and Mrpl44GFP; or FLAGBak and Mrpl44GFP, as a negative control. Lysates were immunoprecipitated with αFLAG, then blotted with an αGFP antibody to determine co-IP. Results are representative of three independent experiments. (B) NIH3T3 whole cell extracts were fractionated by HPLC on a Superose 6 column. The fractions were collected and alternate fractions from 14 to 30 were run on an SDS-PAGE gel, then blotted with antibodies against Mrpl44 as well as Mrpl12 and Mrps15, known components of the mitoribosome. (C) Mitochondrial fractions were obtained from Mrpl44FLAG NIH3T3 cells, and FLAGBak NIH3T3 cells, as a negative control, and immunoprecipitated with αFLAG agarose beads. RNA was then extracted and analysed for pulldown of the mitochondrial rRNA subunits by quantitative RT-PCR. The mean +/- SEM of three independent experiments is shown. Statistical analysis performed using multiple t-test with Holm-Sidak correction for multiple comparisons (*p

    Journal: PLoS ONE

    Article Title: A Role for the Mitochondrial Protein Mrpl44 in Maintaining OXPHOS Capacity

    doi: 10.1371/journal.pone.0134326

    Figure Lengend Snippet: Mrpl44 forms multimers as part of the large subunit of the mitoribosome. (A) HEK293T cells were co-transfected with Mrpl44FLAG and Mrpl44GFP; or FLAGBak and Mrpl44GFP, as a negative control. Lysates were immunoprecipitated with αFLAG, then blotted with an αGFP antibody to determine co-IP. Results are representative of three independent experiments. (B) NIH3T3 whole cell extracts were fractionated by HPLC on a Superose 6 column. The fractions were collected and alternate fractions from 14 to 30 were run on an SDS-PAGE gel, then blotted with antibodies against Mrpl44 as well as Mrpl12 and Mrps15, known components of the mitoribosome. (C) Mitochondrial fractions were obtained from Mrpl44FLAG NIH3T3 cells, and FLAGBak NIH3T3 cells, as a negative control, and immunoprecipitated with αFLAG agarose beads. RNA was then extracted and analysed for pulldown of the mitochondrial rRNA subunits by quantitative RT-PCR. The mean +/- SEM of three independent experiments is shown. Statistical analysis performed using multiple t-test with Holm-Sidak correction for multiple comparisons (*p

    Article Snippet: Gel Filtration Chromatography Whole cell extracts were fractionated using a Waters HPLC system on a pre-packed Superose 6 gel-filtration column (300mm x 10mm internal diameter, GE Healthcare) equilibrated in 0.5% Triton X-100 in 20mM Tris-HCl, pH7.5, 150mM NaCl containing protease inhibitors.

    Techniques: Transfection, Negative Control, Immunoprecipitation, Co-Immunoprecipitation Assay, High Performance Liquid Chromatography, SDS Page, Quantitative RT-PCR