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p53 mammalian expression vector  (GenScript corporation)

 
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    GenScript corporation p53 mammalian expression vector
    Cofactor depletion exacerbates protein aggregation and amyloidogenesis. (A) Coaggregation of NQO1 and its different variants with Aβ1–42 in vitro (n = 3, mean ± SD). apo, apoprotein; apo-Δ50, C-terminally truncated apoprotein; MUT, P187S mutant; MUT-Δ50, C-terminally truncated P187S mutant; WT-Δ50, C-terminally truncated wild-type NQO1. The amount of wild-type NQO1 that coaggregated with the amyloid <t>(+Aβ)</t> was set as 1. Proteins were detected using anti-NQO1 antibody (NQO1) or anti-amyloid antibody (Aβ). (B) The aggregation of transiently transfected <t>Aβ-EGFP</t> (Aβ) in B16 cells was measured using a sedimentation assay. The ratios of Aβ-EGFP in different fractions were normalized to the ratio of Aβ-EGFP in the lysate before ultracentrifugation and are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated. (C) The aggregation of transiently transfected Aβ-EGFP in B16 cells was quantified microscopically. One typical cell with aggregated Aβ-EGFP is shown. (Scale bar: 50 μm.) The fractions of cells containing aggregates under normal and riboflavin-deficient conditions are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated.
    P53 Mammalian Expression Vector, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p53 mammalian expression vector/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    p53 mammalian expression vector - by Bioz Stars, 2026-03
    90/100 stars

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    1) Product Images from "Recognition of enzymes lacking bound cofactor by protein quality control"

    Article Title: Recognition of enzymes lacking bound cofactor by protein quality control

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.1611994113

    Cofactor depletion exacerbates protein aggregation and amyloidogenesis. (A) Coaggregation of NQO1 and its different variants with Aβ1–42 in vitro (n = 3, mean ± SD). apo, apoprotein; apo-Δ50, C-terminally truncated apoprotein; MUT, P187S mutant; MUT-Δ50, C-terminally truncated P187S mutant; WT-Δ50, C-terminally truncated wild-type NQO1. The amount of wild-type NQO1 that coaggregated with the amyloid (+Aβ) was set as 1. Proteins were detected using anti-NQO1 antibody (NQO1) or anti-amyloid antibody (Aβ). (B) The aggregation of transiently transfected Aβ-EGFP (Aβ) in B16 cells was measured using a sedimentation assay. The ratios of Aβ-EGFP in different fractions were normalized to the ratio of Aβ-EGFP in the lysate before ultracentrifugation and are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated. (C) The aggregation of transiently transfected Aβ-EGFP in B16 cells was quantified microscopically. One typical cell with aggregated Aβ-EGFP is shown. (Scale bar: 50 μm.) The fractions of cells containing aggregates under normal and riboflavin-deficient conditions are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated.
    Figure Legend Snippet: Cofactor depletion exacerbates protein aggregation and amyloidogenesis. (A) Coaggregation of NQO1 and its different variants with Aβ1–42 in vitro (n = 3, mean ± SD). apo, apoprotein; apo-Δ50, C-terminally truncated apoprotein; MUT, P187S mutant; MUT-Δ50, C-terminally truncated P187S mutant; WT-Δ50, C-terminally truncated wild-type NQO1. The amount of wild-type NQO1 that coaggregated with the amyloid (+Aβ) was set as 1. Proteins were detected using anti-NQO1 antibody (NQO1) or anti-amyloid antibody (Aβ). (B) The aggregation of transiently transfected Aβ-EGFP (Aβ) in B16 cells was measured using a sedimentation assay. The ratios of Aβ-EGFP in different fractions were normalized to the ratio of Aβ-EGFP in the lysate before ultracentrifugation and are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated. (C) The aggregation of transiently transfected Aβ-EGFP in B16 cells was quantified microscopically. One typical cell with aggregated Aβ-EGFP is shown. (Scale bar: 50 μm.) The fractions of cells containing aggregates under normal and riboflavin-deficient conditions are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated.

    Techniques Used: In Vitro, Mutagenesis, Transfection, Sedimentation, One-tailed Test



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    Cofactor depletion exacerbates protein aggregation and amyloidogenesis. (A) Coaggregation of NQO1 and its different variants with Aβ1–42 in vitro (n = 3, mean ± SD). apo, apoprotein; apo-Δ50, C-terminally truncated apoprotein; MUT, P187S mutant; MUT-Δ50, C-terminally truncated P187S mutant; WT-Δ50, C-terminally truncated wild-type NQO1. The amount of wild-type NQO1 that coaggregated with the amyloid <t>(+Aβ)</t> was set as 1. Proteins were detected using anti-NQO1 antibody (NQO1) or anti-amyloid antibody (Aβ). (B) The aggregation of transiently transfected <t>Aβ-EGFP</t> (Aβ) in B16 cells was measured using a sedimentation assay. The ratios of Aβ-EGFP in different fractions were normalized to the ratio of Aβ-EGFP in the lysate before ultracentrifugation and are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated. (C) The aggregation of transiently transfected Aβ-EGFP in B16 cells was quantified microscopically. One typical cell with aggregated Aβ-EGFP is shown. (Scale bar: 50 μm.) The fractions of cells containing aggregates under normal and riboflavin-deficient conditions are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated.
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    Cofactor depletion exacerbates protein aggregation and amyloidogenesis. (A) Coaggregation of NQO1 and its different variants with Aβ1–42 in vitro (n = 3, mean ± SD). apo, apoprotein; apo-Δ50, C-terminally truncated apoprotein; MUT, P187S mutant; MUT-Δ50, C-terminally truncated P187S mutant; WT-Δ50, C-terminally truncated wild-type NQO1. The amount of wild-type NQO1 that coaggregated with the amyloid (+Aβ) was set as 1. Proteins were detected using anti-NQO1 antibody (NQO1) or anti-amyloid antibody (Aβ). (B) The aggregation of transiently transfected Aβ-EGFP (Aβ) in B16 cells was measured using a sedimentation assay. The ratios of Aβ-EGFP in different fractions were normalized to the ratio of Aβ-EGFP in the lysate before ultracentrifugation and are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated. (C) The aggregation of transiently transfected Aβ-EGFP in B16 cells was quantified microscopically. One typical cell with aggregated Aβ-EGFP is shown. (Scale bar: 50 μm.) The fractions of cells containing aggregates under normal and riboflavin-deficient conditions are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Recognition of enzymes lacking bound cofactor by protein quality control

    doi: 10.1073/pnas.1611994113

    Figure Lengend Snippet: Cofactor depletion exacerbates protein aggregation and amyloidogenesis. (A) Coaggregation of NQO1 and its different variants with Aβ1–42 in vitro (n = 3, mean ± SD). apo, apoprotein; apo-Δ50, C-terminally truncated apoprotein; MUT, P187S mutant; MUT-Δ50, C-terminally truncated P187S mutant; WT-Δ50, C-terminally truncated wild-type NQO1. The amount of wild-type NQO1 that coaggregated with the amyloid (+Aβ) was set as 1. Proteins were detected using anti-NQO1 antibody (NQO1) or anti-amyloid antibody (Aβ). (B) The aggregation of transiently transfected Aβ-EGFP (Aβ) in B16 cells was measured using a sedimentation assay. The ratios of Aβ-EGFP in different fractions were normalized to the ratio of Aβ-EGFP in the lysate before ultracentrifugation and are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated. (C) The aggregation of transiently transfected Aβ-EGFP in B16 cells was quantified microscopically. One typical cell with aggregated Aβ-EGFP is shown. (Scale bar: 50 μm.) The fractions of cells containing aggregates under normal and riboflavin-deficient conditions are plotted (n = 3, mean ± SD). The significance of the difference between the means was determined using a one-tailed t test and is indicated.

    Article Snippet: P53 and Aβ-EGFP mammalian expression vectors were purchased from GenScript.

    Techniques: In Vitro, Mutagenesis, Transfection, Sedimentation, One-tailed Test