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Proteintech rabbit anti erf3b
Rabbit Anti Erf3b, supplied by Proteintech, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+erf3b/GSPT2+Antibody/pmc03677241-353-24-27
Average 90 stars, based on 4 article reviews

rabbit anti erf3b - by Bioz Stars, 2026-11

90/100 stars

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Article Title: Phosphorylation at intrinsically disordered regions of PAM2 motif-containing proteins modulates their interactions with PABPC1 and influences mRNA fate
Article Snippet: To detect V5-tagged or HA-tagged proteins, membranes were incubated with horseradish peroxidase (HRP)-conjugated monoclonal anti-V5 antibody (1/5000; Invitrogen) or HRP-conjugated monoclonal anti-HA antibody (1/1000; Roche), respectively. .. For detecting endogenous proteins, membranes were first incubated with rabbit anti-Caf1-B peptide antibody (1/1000) ( Yamashita et al. 2005 ), rabbit anti-Ago2 (1/1000; Biosensis), rabbit anti-eRF3b (1/2000; Proteintech), rabbit anti-Pan2-B peptide (1/2000) ( Yamashita et al. 2005 ), rabbit anti-PABPC1 (1/4000; a gift from R. Lloyd, Baylor College of Medicine), or mouse anti-β-actin-HRP monoclonal antibody (1/10,000; Santa Cruz). .. Secondary HRP-conjugated goat anti-rabbit antibodies (1/4000; Bethyl) or goat anti-mouse antibodies (1/5000; Bio-Rad) were used for detection with chemiluminescence reagent (peroxide/luminol enhancer; Pierce).

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Effect of siRNA knockdown of eRF3a and eRF3b on TP53 PTC readthrough. ( A ) HDQ-P1 cells with a homozygous nonsense mutation in the TP53 gene (R213X) were transfected with either non-target siRNA or several ON-TARGETplus siRNAs targeting eRF3a . Levels of SURF complex components eRF3a, eRF1, UPF1 and SMG1 were measured 96 h after transfection. GAPDH was used as loading control. ( B ) p53 levels (full-length, FL-p53; truncated, TR-p53) were measured in the same extracts as in A . Vinculin was used as loading control. ( C ) p53 and vinculin levels were measured in transfected cells exposed to 20 μg/ml G418 for 48 h. ( D ) eRF3a and eRF3b levels were measured in HDQ-P1 and H1299-p53 R213X cell extracts. ( E, F ) H1299-p53 R213X cells were transfected with non-target siRNA or several ON-TARGETplus siRNAs targeting eRF3a ( E ) or eRF3b ( F ). eRF3a and eRF3b levels were measured 96 h after transfection. 48 h after transfection, samples were exposed to 20 μg/ml G418 for another 48 h and p53 and vinculin levels were determined. Protein levels in all panels were measured using automated capillary electrophoresis western analysis. In this and subsequent figures, equal amounts of protein lysate were loaded in all capillaries in each panel, except where indicated. The amounts of eRF3a, eRF3b, eRF1, UPF1 and SMG1 are expressed as percentage of levels in untreated cells. As FL-p53 is essentially undetectable in untreated HDQ-P1 cells in most experiments, FL-p53 levels are expressed relative to the amount of FL-p53 in cells treated with 20 μg/ml G418. Dashed lines indicate different capillaries.

Journal: Nucleic Acids Research

Article Title: Effect of small molecule eRF3 degraders on premature termination codon readthrough

doi: 10.1093/nar/gkab194

Figure Lengend Snippet: Effect of siRNA knockdown of eRF3a and eRF3b on TP53 PTC readthrough. ( A ) HDQ-P1 cells with a homozygous nonsense mutation in the TP53 gene (R213X) were transfected with either non-target siRNA or several ON-TARGETplus siRNAs targeting eRF3a . Levels of SURF complex components eRF3a, eRF1, UPF1 and SMG1 were measured 96 h after transfection. GAPDH was used as loading control. ( B ) p53 levels (full-length, FL-p53; truncated, TR-p53) were measured in the same extracts as in A . Vinculin was used as loading control. ( C ) p53 and vinculin levels were measured in transfected cells exposed to 20 μg/ml G418 for 48 h. ( D ) eRF3a and eRF3b levels were measured in HDQ-P1 and H1299-p53 R213X cell extracts. ( E, F ) H1299-p53 R213X cells were transfected with non-target siRNA or several ON-TARGETplus siRNAs targeting eRF3a ( E ) or eRF3b ( F ). eRF3a and eRF3b levels were measured 96 h after transfection. 48 h after transfection, samples were exposed to 20 μg/ml G418 for another 48 h and p53 and vinculin levels were determined. Protein levels in all panels were measured using automated capillary electrophoresis western analysis. In this and subsequent figures, equal amounts of protein lysate were loaded in all capillaries in each panel, except where indicated. The amounts of eRF3a, eRF3b, eRF1, UPF1 and SMG1 are expressed as percentage of levels in untreated cells. As FL-p53 is essentially undetectable in untreated HDQ-P1 cells in most experiments, FL-p53 levels are expressed relative to the amount of FL-p53 in cells treated with 20 μg/ml G418. Dashed lines indicate different capillaries.

Article Snippet: DO-1 mouse anti-p53 antibody (1:400, Santa Cruz sc-126), mouse anti-vinculin antibody (1:600, R&D Systems MAB6896), rabbit anti-eRF3a (1:100, Thermo Fisher Scientific PA5–62621), rabbit anti-eRF3b (1:100, Thermo Fisher Scientific PA5–60824), mouse anti-FLAG M2 (1:100, Sigma F1804), rabbit anti-GAPDH (1:800, Abcam ab128915), mouse anti-TPP1 (1:1000, Abcam ab54685), rabbit anti-Dystrophin (1:400, Abcam ab15277), rabbit anti-UPF1 (1:1000, Abcam ab109363), rabbit anti-SMG1 (1:50, Cell signaling 4993) and mouse anti-eRF1 (1:100, Novus Biologicals 4F9H12) were used.

Techniques: Mutagenesis, Transfection, Electrophoresis, Western Blot

Effect of CC-885 and CC-90009 on IDUA PTC readthrough. ( A, B ) Fibroblasts derived from an unaffected individual were exposed to various concentrations of CC-885 ( A ) or CC-90009 ( B ) without or with 20 μg/ml G418 for 48 h and cell viability was measured using the MTT assay in triplicate samples (±SD, n = 3). ( C, D ) GM00798 primary fibroblasts derived from a MPS I-H patient with IDUA nonsense mutations (W402X/W402X) were exposed to the indicated concentrations of CC-885 ( C ) or CC-90009 ( D ) for 72 h and eRF3a, eRF3b and eRF1 levels were measured. GAPDH was used as loading control. ( E, F ) GM00798 fibroblasts were exposed to the same concentrations of CC-885 ( E ) and CC-90009 ( F ) as in C and D , with or without 20 μg/ml G418 for 72 h and α- l -iduronidase activity was measured in triplicate samples (±SD) and plotted as % of the activity measured in WT fibroblasts. * indicates statistically significant difference to untreated samples ( P < 0.01).

Journal: Nucleic Acids Research

Article Title: Effect of small molecule eRF3 degraders on premature termination codon readthrough

doi: 10.1093/nar/gkab194

Figure Lengend Snippet: Effect of CC-885 and CC-90009 on IDUA PTC readthrough. ( A, B ) Fibroblasts derived from an unaffected individual were exposed to various concentrations of CC-885 ( A ) or CC-90009 ( B ) without or with 20 μg/ml G418 for 48 h and cell viability was measured using the MTT assay in triplicate samples (±SD, n = 3). ( C, D ) GM00798 primary fibroblasts derived from a MPS I-H patient with IDUA nonsense mutations (W402X/W402X) were exposed to the indicated concentrations of CC-885 ( C ) or CC-90009 ( D ) for 72 h and eRF3a, eRF3b and eRF1 levels were measured. GAPDH was used as loading control. ( E, F ) GM00798 fibroblasts were exposed to the same concentrations of CC-885 ( E ) and CC-90009 ( F ) as in C and D , with or without 20 μg/ml G418 for 72 h and α- l -iduronidase activity was measured in triplicate samples (±SD) and plotted as % of the activity measured in WT fibroblasts. * indicates statistically significant difference to untreated samples ( P < 0.01).

Techniques: Derivative Assay, MTT Assay, Activity Assay

Effect of CC-885 and CC-90009 on DMD PTC readthrough. ( A, B ) Myoblasts derived from an unaffected individual were exposed to various concentrations of CC-885 ( A ) or CC-90009 ( B ) for 48 h and cell viability was measured using the MTT assay in triplicate samples (± S.D.). ( C, D ) HSK001 myoblasts derived from a DMD patient with a DMD nonsense mutation (E2035X) were differentiated into myotubes and exposed to the indicated concentrations of CC-885 ( C ) or CC-90009 ( D ) for 72 h and eRF3a, eRF3b and eRF1 levels were determined. ( E–H ) HSK001 myotubes were exposed to the indicated concentrations of CC-885 ( E , G ) or CC-90009 ( F , H ), alone ( E , F ) or in combination with 20 μg/ml G418 ( G , H ) for 72 h and dystrophin levels were determined. Dystrophin levels are expressed relative to the amount of dystrophin measured in samples treated with 20 μg/ml G418. GAPDH was used as loading control.

Journal: Nucleic Acids Research

Article Title: Effect of small molecule eRF3 degraders on premature termination codon readthrough

doi: 10.1093/nar/gkab194

Figure Lengend Snippet: Effect of CC-885 and CC-90009 on DMD PTC readthrough. ( A, B ) Myoblasts derived from an unaffected individual were exposed to various concentrations of CC-885 ( A ) or CC-90009 ( B ) for 48 h and cell viability was measured using the MTT assay in triplicate samples (± S.D.). ( C, D ) HSK001 myoblasts derived from a DMD patient with a DMD nonsense mutation (E2035X) were differentiated into myotubes and exposed to the indicated concentrations of CC-885 ( C ) or CC-90009 ( D ) for 72 h and eRF3a, eRF3b and eRF1 levels were determined. ( E–H ) HSK001 myotubes were exposed to the indicated concentrations of CC-885 ( E , G ) or CC-90009 ( F , H ), alone ( E , F ) or in combination with 20 μg/ml G418 ( G , H ) for 72 h and dystrophin levels were determined. Dystrophin levels are expressed relative to the amount of dystrophin measured in samples treated with 20 μg/ml G418. GAPDH was used as loading control.

Techniques: Derivative Assay, MTT Assay, Mutagenesis

Effect of CC-885 and CC-90009 on COL17A1 PTC readthrough. ( A, B ) HaCaT keratinocytes derived from an unaffected individual were exposed to various concentrations of CC-885 ( A ) or CC-90009 ( B ) with or without 100 μg/ml gentamicin sulfate for 48 h and cell viability was measured using the MTT assay in triplicate samples (±SD). Concentrations of CC-885 and CC-90009 are in nanomolar. ( C, D ) JEB01 keratinocytes derived from a JEB patient with a COL17A1 nonsense mutation (R688X/R688X) were exposed to the indicated concentrations of CC-885 ( C ) or CC-90009 ( D ) for 72 h and eRF3a, eRF3b and eRF1 levels were determined using automated capillary electrophoresis western analysis. GAPDH was used as loading control. ( E, F ) JEB01 keratinocytes were exposed to the indicated concentrations of CC-885 ( E ) or CC-90009 ( F ) in the presence or absence of 100 or 300 μg/ml gentamicin sulfate for 72 h and Collagen XVII levels were measured by SDS-PAGE followed by traditional western blotting. β -actin was used as loading control.

Journal: Nucleic Acids Research

Article Title: Effect of small molecule eRF3 degraders on premature termination codon readthrough

doi: 10.1093/nar/gkab194

Figure Lengend Snippet: Effect of CC-885 and CC-90009 on COL17A1 PTC readthrough. ( A, B ) HaCaT keratinocytes derived from an unaffected individual were exposed to various concentrations of CC-885 ( A ) or CC-90009 ( B ) with or without 100 μg/ml gentamicin sulfate for 48 h and cell viability was measured using the MTT assay in triplicate samples (±SD). Concentrations of CC-885 and CC-90009 are in nanomolar. ( C, D ) JEB01 keratinocytes derived from a JEB patient with a COL17A1 nonsense mutation (R688X/R688X) were exposed to the indicated concentrations of CC-885 ( C ) or CC-90009 ( D ) for 72 h and eRF3a, eRF3b and eRF1 levels were determined using automated capillary electrophoresis western analysis. GAPDH was used as loading control. ( E, F ) JEB01 keratinocytes were exposed to the indicated concentrations of CC-885 ( E ) or CC-90009 ( F ) in the presence or absence of 100 or 300 μg/ml gentamicin sulfate for 72 h and Collagen XVII levels were measured by SDS-PAGE followed by traditional western blotting. β -actin was used as loading control.

Techniques: Derivative Assay, MTT Assay, Mutagenesis, Electrophoresis, Western Blot, SDS Page

Effect of CC-885 and CC-90009 on TPP1 PTC readthrough. ( A, B ) GM16485 primary fibroblasts derived from a late infantile neuronal ceroid lipofuscinosis (CLN2) patient with TPP1 nonsense mutations (R127X/R208X) were exposed to the indicated concentrations of CC-885 ( A ) or CC-90009 ( B ) for 72 h and eRF3a, eRF3b and eRF1 levels were determined. ( C–F ) GM16485 fibroblasts were exposed to the indicated concentrations of CC-885 ( C , E ) or CC-90009 ( D , F ), alone ( C , D ) or in combination with 20 μg/ml G418 ( E , F ) for 72 h and TPP1 levels (proenzyme, P; mature, M) were measured. Total TPP1 levels (P + M) are expressed relative to the amount of total TPP1 in cells treated with 20 μg/ml G418. In panels A–F , GAPDH was used as loading control. In panel E , X indicates where lower amounts of protein were loaded because insufficient numbers of cells were recovered. ( G , H ) TPP1 activity from the same cell extracts as in C–F was determined in triplicate samples (±SD) and expressed as % activity relative to that of WT fibroblasts. * indicates statistically significant difference to untreated samples ( P < 0.01).

Journal: Nucleic Acids Research

Article Title: Effect of small molecule eRF3 degraders on premature termination codon readthrough

doi: 10.1093/nar/gkab194

Figure Lengend Snippet: Effect of CC-885 and CC-90009 on TPP1 PTC readthrough. ( A, B ) GM16485 primary fibroblasts derived from a late infantile neuronal ceroid lipofuscinosis (CLN2) patient with TPP1 nonsense mutations (R127X/R208X) were exposed to the indicated concentrations of CC-885 ( A ) or CC-90009 ( B ) for 72 h and eRF3a, eRF3b and eRF1 levels were determined. ( C–F ) GM16485 fibroblasts were exposed to the indicated concentrations of CC-885 ( C , E ) or CC-90009 ( D , F ), alone ( C , D ) or in combination with 20 μg/ml G418 ( E , F ) for 72 h and TPP1 levels (proenzyme, P; mature, M) were measured. Total TPP1 levels (P + M) are expressed relative to the amount of total TPP1 in cells treated with 20 μg/ml G418. In panels A–F , GAPDH was used as loading control. In panel E , X indicates where lower amounts of protein were loaded because insufficient numbers of cells were recovered. ( G , H ) TPP1 activity from the same cell extracts as in C–F was determined in triplicate samples (±SD) and expressed as % activity relative to that of WT fibroblasts. * indicates statistically significant difference to untreated samples ( P < 0.01).

Techniques: Derivative Assay, Activity Assay

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