p53 expression vector Search Results


90
Tianjin Saier Biotechnology sirna expression vectors psilencer/shr-p53
Sirna Expression Vectors Psilencer/Shr P53, supplied by Tianjin Saier Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Johns Hopkins HealthCare human p53 expression vectors
Human P53 Expression Vectors, supplied by Johns Hopkins HealthCare, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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
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New Brunswick Scientific p53 expression vectors
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 Expression Vectors, supplied by New Brunswick Scientific, 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 expression vectors/product/New Brunswick Scientific
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p53 expression vectors - by Bioz Stars, 2026-03
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Obio Technology Corp Ltd p53-expressing lentiviral vectors
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 Expressing Lentiviral Vectors, supplied by Obio Technology Corp Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Genolution Pharmaceuticals Inc porcine p53-specific shrna 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.
Porcine P53 Specific Shrna Expression Vector, supplied by Genolution Pharmaceuticals Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Genechem lentivirus-based cd155 expression vectors and sirna against cd155, cd96, and p53
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.
Lentivirus Based Cd155 Expression Vectors And Sirna Against Cd155, Cd96, And P53, supplied by Genechem, 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/lentivirus-based cd155 expression vectors and sirna against cd155, cd96, and p53/product/Genechem
Average 90 stars, based on 1 article reviews
lentivirus-based cd155 expression vectors and sirna against cd155, cd96, and p53 - by Bioz Stars, 2026-03
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90
Shanghai GenePharma lentiviral vectors expressing p53 shrnas
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.
Lentiviral Vectors Expressing P53 Shrnas, supplied by Shanghai GenePharma, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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