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rabbit anti upf1 antibody  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc rabbit anti upf1 antibody
    HBV transcripts are targeted by NMD through <t>UPF1</t> recognition in 293T cells (A) Degradation kinetics of major HBV transcripts. HEK293T cells were transfected with in vitro -transcribed (IVT-) HBV RNA, pgRNA RNA, 2.4 knt RNA, 2.1 knt RNA, or X RNA, and each RNA level was chased with RT-qPCR every 4 h up to 8 h h post transfection. Data are shown as ratios relative to the amount of cellular GAPDH mRNA, which was also determined by RT-qPCR. (B) RNA immunoprecipitation (RIP) with an anti-pUPF1 antibody. HEK293T cells were transfected with IVT-HBV RNA as described in the main text. Co-transfected IVT-GFP mRNA was used as an internal control. Subsequently, pUPF1-bound RNA was isolated with an anti-pUPF1 antibody, followed by RT-qPCR using a primer set for HBV RNAs and GFP mRNA. Data of HBV RNA precipitation are shown as ratios relative to co-precipitated GFP mRNA in each RIP experiment. (C) Intracellular HBV RNAs 1 h after RNA transfection. Data of input HBV RNAs are shown as ratios relative to intracellular GFP mRNA amounts. The data are presented as means with standard error of the mean (SEM) of at least three independent experiments. Statistical analysis was done by one-way ANOVA with Dunnett’s multiple comparisons test or two-way ANOVA with Sidak’s multiple comparisons test.
    Rabbit Anti Upf1 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+upf1+antibody/pmc12063116-2-0-4?v=Cell+Signaling+Technology+Inc
    Average 93 stars, based on 72 article reviews
    rabbit anti upf1 antibody - by Bioz Stars, 2026-08
    93/100 stars

    Images

    1) Product Images from "Cell-intrinsic regulation of HBV RNAs by the nonsense-mediated mRNA decay pathway controls viral replication"

    Article Title: Cell-intrinsic regulation of HBV RNAs by the nonsense-mediated mRNA decay pathway controls viral replication

    Journal: iScience

    doi: 10.1016/j.isci.2025.112460

    HBV transcripts are targeted by NMD through UPF1 recognition in 293T cells (A) Degradation kinetics of major HBV transcripts. HEK293T cells were transfected with in vitro -transcribed (IVT-) HBV RNA, pgRNA RNA, 2.4 knt RNA, 2.1 knt RNA, or X RNA, and each RNA level was chased with RT-qPCR every 4 h up to 8 h h post transfection. Data are shown as ratios relative to the amount of cellular GAPDH mRNA, which was also determined by RT-qPCR. (B) RNA immunoprecipitation (RIP) with an anti-pUPF1 antibody. HEK293T cells were transfected with IVT-HBV RNA as described in the main text. Co-transfected IVT-GFP mRNA was used as an internal control. Subsequently, pUPF1-bound RNA was isolated with an anti-pUPF1 antibody, followed by RT-qPCR using a primer set for HBV RNAs and GFP mRNA. Data of HBV RNA precipitation are shown as ratios relative to co-precipitated GFP mRNA in each RIP experiment. (C) Intracellular HBV RNAs 1 h after RNA transfection. Data of input HBV RNAs are shown as ratios relative to intracellular GFP mRNA amounts. The data are presented as means with standard error of the mean (SEM) of at least three independent experiments. Statistical analysis was done by one-way ANOVA with Dunnett’s multiple comparisons test or two-way ANOVA with Sidak’s multiple comparisons test.
    Figure Legend Snippet: HBV transcripts are targeted by NMD through UPF1 recognition in 293T cells (A) Degradation kinetics of major HBV transcripts. HEK293T cells were transfected with in vitro -transcribed (IVT-) HBV RNA, pgRNA RNA, 2.4 knt RNA, 2.1 knt RNA, or X RNA, and each RNA level was chased with RT-qPCR every 4 h up to 8 h h post transfection. Data are shown as ratios relative to the amount of cellular GAPDH mRNA, which was also determined by RT-qPCR. (B) RNA immunoprecipitation (RIP) with an anti-pUPF1 antibody. HEK293T cells were transfected with IVT-HBV RNA as described in the main text. Co-transfected IVT-GFP mRNA was used as an internal control. Subsequently, pUPF1-bound RNA was isolated with an anti-pUPF1 antibody, followed by RT-qPCR using a primer set for HBV RNAs and GFP mRNA. Data of HBV RNA precipitation are shown as ratios relative to co-precipitated GFP mRNA in each RIP experiment. (C) Intracellular HBV RNAs 1 h after RNA transfection. Data of input HBV RNAs are shown as ratios relative to intracellular GFP mRNA amounts. The data are presented as means with standard error of the mean (SEM) of at least three independent experiments. Statistical analysis was done by one-way ANOVA with Dunnett’s multiple comparisons test or two-way ANOVA with Sidak’s multiple comparisons test.

    Techniques Used: Transfection, In Vitro, Quantitative RT-PCR, RNA Immunoprecipitation, Control, Isolation

    HBV transcripts are targeted by NMD through UPF1 recognition in HBV-replicating cells (HepAD38.7) (A) Protein levels of NMD factors. The protein level was monitored in HepAD38.7 cells treated with each siRNA after 72 h HBV induction. The HBV induction was also assessed by HBc expression with western blot. (B) Degradation kinetics of pgRNA/3.5 knt RNA. Intracellularly accumulated pgRNA/3.5 knt RNA by Tet removal was measured with RT-qPCR every 2 h for 8 h after re-addition of Tet. The GAPDH mRNA level was also monitored with RT-qPCR. Data are shown as the ratio of pgRNA/3.5 knt RNA to GAPDH. (C) Northern blotting analysis of HBV-related transcripts in NMD-depleted HepAD38.7 cells. Total RNA was extracted and separated on an agarose gel under a denaturing condition. HBV-related transcripts or GAPDH mRNA was detected by the corresponding probe. (D) RNA immunoprecipitation (RIP) using an anti-pUPF1 antibody followed by RT-qPCR. The pUPF1-bound RNAs were isolated and then RT-qPCR analyses were conducted for pgRNA/3.5 knt RNA, vtRNA1-1, and alternative rpL3 mRNA. Data are presented as the fold increase over normal IgG-bound RNA in each target gene, or as mean values with SEM of at least three independent experiments. Statistical analysis was done by one-way ANOVA with Dunnett’s multiple comparisons test or two-way ANOVA with Sidak’s multiple comparisons test.
    Figure Legend Snippet: HBV transcripts are targeted by NMD through UPF1 recognition in HBV-replicating cells (HepAD38.7) (A) Protein levels of NMD factors. The protein level was monitored in HepAD38.7 cells treated with each siRNA after 72 h HBV induction. The HBV induction was also assessed by HBc expression with western blot. (B) Degradation kinetics of pgRNA/3.5 knt RNA. Intracellularly accumulated pgRNA/3.5 knt RNA by Tet removal was measured with RT-qPCR every 2 h for 8 h after re-addition of Tet. The GAPDH mRNA level was also monitored with RT-qPCR. Data are shown as the ratio of pgRNA/3.5 knt RNA to GAPDH. (C) Northern blotting analysis of HBV-related transcripts in NMD-depleted HepAD38.7 cells. Total RNA was extracted and separated on an agarose gel under a denaturing condition. HBV-related transcripts or GAPDH mRNA was detected by the corresponding probe. (D) RNA immunoprecipitation (RIP) using an anti-pUPF1 antibody followed by RT-qPCR. The pUPF1-bound RNAs were isolated and then RT-qPCR analyses were conducted for pgRNA/3.5 knt RNA, vtRNA1-1, and alternative rpL3 mRNA. Data are presented as the fold increase over normal IgG-bound RNA in each target gene, or as mean values with SEM of at least three independent experiments. Statistical analysis was done by one-way ANOVA with Dunnett’s multiple comparisons test or two-way ANOVA with Sidak’s multiple comparisons test.

    Techniques Used: Expressing, Western Blot, Quantitative RT-PCR, Northern Blot, Agarose Gel Electrophoresis, RNA Immunoprecipitation, Isolation



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    HBV transcripts are targeted by NMD through <t>UPF1</t> recognition in 293T cells (A) Degradation kinetics of major HBV transcripts. HEK293T cells were transfected with in vitro -transcribed (IVT-) HBV RNA, pgRNA RNA, 2.4 knt RNA, 2.1 knt RNA, or X RNA, and each RNA level was chased with RT-qPCR every 4 h up to 8 h h post transfection. Data are shown as ratios relative to the amount of cellular GAPDH mRNA, which was also determined by RT-qPCR. (B) RNA immunoprecipitation (RIP) with an anti-pUPF1 antibody. HEK293T cells were transfected with IVT-HBV RNA as described in the main text. Co-transfected IVT-GFP mRNA was used as an internal control. Subsequently, pUPF1-bound RNA was isolated with an anti-pUPF1 antibody, followed by RT-qPCR using a primer set for HBV RNAs and GFP mRNA. Data of HBV RNA precipitation are shown as ratios relative to co-precipitated GFP mRNA in each RIP experiment. (C) Intracellular HBV RNAs 1 h after RNA transfection. Data of input HBV RNAs are shown as ratios relative to intracellular GFP mRNA amounts. The data are presented as means with standard error of the mean (SEM) of at least three independent experiments. Statistical analysis was done by one-way ANOVA with Dunnett’s multiple comparisons test or two-way ANOVA with Sidak’s multiple comparisons test.
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    HBV transcripts are targeted by NMD through UPF1 recognition in 293T cells (A) Degradation kinetics of major HBV transcripts. HEK293T cells were transfected with in vitro -transcribed (IVT-) HBV RNA, pgRNA RNA, 2.4 knt RNA, 2.1 knt RNA, or X RNA, and each RNA level was chased with RT-qPCR every 4 h up to 8 h h post transfection. Data are shown as ratios relative to the amount of cellular GAPDH mRNA, which was also determined by RT-qPCR. (B) RNA immunoprecipitation (RIP) with an anti-pUPF1 antibody. HEK293T cells were transfected with IVT-HBV RNA as described in the main text. Co-transfected IVT-GFP mRNA was used as an internal control. Subsequently, pUPF1-bound RNA was isolated with an anti-pUPF1 antibody, followed by RT-qPCR using a primer set for HBV RNAs and GFP mRNA. Data of HBV RNA precipitation are shown as ratios relative to co-precipitated GFP mRNA in each RIP experiment. (C) Intracellular HBV RNAs 1 h after RNA transfection. Data of input HBV RNAs are shown as ratios relative to intracellular GFP mRNA amounts. The data are presented as means with standard error of the mean (SEM) of at least three independent experiments. Statistical analysis was done by one-way ANOVA with Dunnett’s multiple comparisons test or two-way ANOVA with Sidak’s multiple comparisons test.

    Journal: iScience

    Article Title: Cell-intrinsic regulation of HBV RNAs by the nonsense-mediated mRNA decay pathway controls viral replication

    doi: 10.1016/j.isci.2025.112460

    Figure Lengend Snippet: HBV transcripts are targeted by NMD through UPF1 recognition in 293T cells (A) Degradation kinetics of major HBV transcripts. HEK293T cells were transfected with in vitro -transcribed (IVT-) HBV RNA, pgRNA RNA, 2.4 knt RNA, 2.1 knt RNA, or X RNA, and each RNA level was chased with RT-qPCR every 4 h up to 8 h h post transfection. Data are shown as ratios relative to the amount of cellular GAPDH mRNA, which was also determined by RT-qPCR. (B) RNA immunoprecipitation (RIP) with an anti-pUPF1 antibody. HEK293T cells were transfected with IVT-HBV RNA as described in the main text. Co-transfected IVT-GFP mRNA was used as an internal control. Subsequently, pUPF1-bound RNA was isolated with an anti-pUPF1 antibody, followed by RT-qPCR using a primer set for HBV RNAs and GFP mRNA. Data of HBV RNA precipitation are shown as ratios relative to co-precipitated GFP mRNA in each RIP experiment. (C) Intracellular HBV RNAs 1 h after RNA transfection. Data of input HBV RNAs are shown as ratios relative to intracellular GFP mRNA amounts. The data are presented as means with standard error of the mean (SEM) of at least three independent experiments. Statistical analysis was done by one-way ANOVA with Dunnett’s multiple comparisons test or two-way ANOVA with Sidak’s multiple comparisons test.

    Article Snippet: Rabbit anti-UPF1 antibody , Cell Signaling Technology , Cat#9435; RRID: AB_10629662.

    Techniques: Transfection, In Vitro, Quantitative RT-PCR, RNA Immunoprecipitation, Control, Isolation

    HBV transcripts are targeted by NMD through UPF1 recognition in HBV-replicating cells (HepAD38.7) (A) Protein levels of NMD factors. The protein level was monitored in HepAD38.7 cells treated with each siRNA after 72 h HBV induction. The HBV induction was also assessed by HBc expression with western blot. (B) Degradation kinetics of pgRNA/3.5 knt RNA. Intracellularly accumulated pgRNA/3.5 knt RNA by Tet removal was measured with RT-qPCR every 2 h for 8 h after re-addition of Tet. The GAPDH mRNA level was also monitored with RT-qPCR. Data are shown as the ratio of pgRNA/3.5 knt RNA to GAPDH. (C) Northern blotting analysis of HBV-related transcripts in NMD-depleted HepAD38.7 cells. Total RNA was extracted and separated on an agarose gel under a denaturing condition. HBV-related transcripts or GAPDH mRNA was detected by the corresponding probe. (D) RNA immunoprecipitation (RIP) using an anti-pUPF1 antibody followed by RT-qPCR. The pUPF1-bound RNAs were isolated and then RT-qPCR analyses were conducted for pgRNA/3.5 knt RNA, vtRNA1-1, and alternative rpL3 mRNA. Data are presented as the fold increase over normal IgG-bound RNA in each target gene, or as mean values with SEM of at least three independent experiments. Statistical analysis was done by one-way ANOVA with Dunnett’s multiple comparisons test or two-way ANOVA with Sidak’s multiple comparisons test.

    Journal: iScience

    Article Title: Cell-intrinsic regulation of HBV RNAs by the nonsense-mediated mRNA decay pathway controls viral replication

    doi: 10.1016/j.isci.2025.112460

    Figure Lengend Snippet: HBV transcripts are targeted by NMD through UPF1 recognition in HBV-replicating cells (HepAD38.7) (A) Protein levels of NMD factors. The protein level was monitored in HepAD38.7 cells treated with each siRNA after 72 h HBV induction. The HBV induction was also assessed by HBc expression with western blot. (B) Degradation kinetics of pgRNA/3.5 knt RNA. Intracellularly accumulated pgRNA/3.5 knt RNA by Tet removal was measured with RT-qPCR every 2 h for 8 h after re-addition of Tet. The GAPDH mRNA level was also monitored with RT-qPCR. Data are shown as the ratio of pgRNA/3.5 knt RNA to GAPDH. (C) Northern blotting analysis of HBV-related transcripts in NMD-depleted HepAD38.7 cells. Total RNA was extracted and separated on an agarose gel under a denaturing condition. HBV-related transcripts or GAPDH mRNA was detected by the corresponding probe. (D) RNA immunoprecipitation (RIP) using an anti-pUPF1 antibody followed by RT-qPCR. The pUPF1-bound RNAs were isolated and then RT-qPCR analyses were conducted for pgRNA/3.5 knt RNA, vtRNA1-1, and alternative rpL3 mRNA. Data are presented as the fold increase over normal IgG-bound RNA in each target gene, or as mean values with SEM of at least three independent experiments. Statistical analysis was done by one-way ANOVA with Dunnett’s multiple comparisons test or two-way ANOVA with Sidak’s multiple comparisons test.

    Article Snippet: Rabbit anti-UPF1 antibody , Cell Signaling Technology , Cat#9435; RRID: AB_10629662.

    Techniques: Expressing, Western Blot, Quantitative RT-PCR, Northern Blot, Agarose Gel Electrophoresis, RNA Immunoprecipitation, Isolation

    GAPDH = glyceraldehyde 3-phosphate dehydrogenase; H/R = hypoxia/reoxygenation; NC = negative control; oe = overexpression; RT-qPCR = reverse transcription quantitative polymerase chain reaction; UPF1 = up-frameshift 1. ** p<0.01, *** p<0.001.

    Journal: Korean Circulation Journal

    Article Title: UPF1 Alleviates Myocardial Ischemia-Reperfusion Injury by Regulating SMURF2 -Mediated Ubiquitination Degradation of FOXA2

    doi: 10.4070/kcj.2024.0190

    Figure Lengend Snippet: GAPDH = glyceraldehyde 3-phosphate dehydrogenase; H/R = hypoxia/reoxygenation; NC = negative control; oe = overexpression; RT-qPCR = reverse transcription quantitative polymerase chain reaction; UPF1 = up-frameshift 1. ** p<0.01, *** p<0.001.

    Article Snippet: H9C2 cells were lysed and incubated with magnetic beads preconjugated with antibodies anti-UPF1 (#12040, CST) or anti-immunoglobulin G (IgG) (ab182931, Abcam).

    Techniques: Negative Control, Over Expression, Quantitative RT-PCR, Reverse Transcription, Real-time Polymerase Chain Reaction

    GAPDH = glyceraldehyde 3-phosphate dehydrogenase; FOXA2 = forkhead box A2; I/R = ischemia/reperfusion; NC = negative control; oe = overexpression; PAR4 = protease-activated receptor 4; SMURF2 = SMAD-specific E3 ubiquitin ligase 2; TTC = tetrazolium chloride; UPF1 = up-frameshift 1. *** p<0.001.

    Journal: Korean Circulation Journal

    Article Title: UPF1 Alleviates Myocardial Ischemia-Reperfusion Injury by Regulating SMURF2 -Mediated Ubiquitination Degradation of FOXA2

    doi: 10.4070/kcj.2024.0190

    Figure Lengend Snippet: GAPDH = glyceraldehyde 3-phosphate dehydrogenase; FOXA2 = forkhead box A2; I/R = ischemia/reperfusion; NC = negative control; oe = overexpression; PAR4 = protease-activated receptor 4; SMURF2 = SMAD-specific E3 ubiquitin ligase 2; TTC = tetrazolium chloride; UPF1 = up-frameshift 1. *** p<0.001.

    Article Snippet: H9C2 cells were lysed and incubated with magnetic beads preconjugated with antibodies anti-UPF1 (#12040, CST) or anti-immunoglobulin G (IgG) (ab182931, Abcam).

    Techniques: Negative Control, Over Expression, Ubiquitin Proteomics

    GAPDH = glyceraldehyde 3-phosphate dehydrogenase; H/R = hypoxia/reoxygenation; IgG = immunoglobulin G; NC = negative control; oe = overexpression; RT-qPCR = reverse transcription quantitative polymerase chain reaction; SMURF2 = SMAD-specific E3 ubiquitin ligase 2; UPF1 = up-frameshift 1. ** p<0.01, *** p<0.001.

    Journal: Korean Circulation Journal

    Article Title: UPF1 Alleviates Myocardial Ischemia-Reperfusion Injury by Regulating SMURF2 -Mediated Ubiquitination Degradation of FOXA2

    doi: 10.4070/kcj.2024.0190

    Figure Lengend Snippet: GAPDH = glyceraldehyde 3-phosphate dehydrogenase; H/R = hypoxia/reoxygenation; IgG = immunoglobulin G; NC = negative control; oe = overexpression; RT-qPCR = reverse transcription quantitative polymerase chain reaction; SMURF2 = SMAD-specific E3 ubiquitin ligase 2; UPF1 = up-frameshift 1. ** p<0.01, *** p<0.001.

    Article Snippet: H9C2 cells were lysed and incubated with magnetic beads preconjugated with antibodies anti-UPF1 (#12040, CST) or anti-immunoglobulin G (IgG) (ab182931, Abcam).

    Techniques: Negative Control, Over Expression, Quantitative RT-PCR, Reverse Transcription, Real-time Polymerase Chain Reaction, Ubiquitin Proteomics

    FOXA2 = forkhead box A2; GAPDH = glyceraldehyde 3-phosphate dehydrogenase; H/R = hypoxia/reoxygenation; NC = negative control; oe = overexpression; PAR4 = protease-activated receptor 4; SMURF2 = SMAD-specific E3 ubiquitin ligase 2; UPF1 = up-frameshift 1. * p<0.05, ** p<0.01, *** p<0.001.

    Journal: Korean Circulation Journal

    Article Title: UPF1 Alleviates Myocardial Ischemia-Reperfusion Injury by Regulating SMURF2 -Mediated Ubiquitination Degradation of FOXA2

    doi: 10.4070/kcj.2024.0190

    Figure Lengend Snippet: FOXA2 = forkhead box A2; GAPDH = glyceraldehyde 3-phosphate dehydrogenase; H/R = hypoxia/reoxygenation; NC = negative control; oe = overexpression; PAR4 = protease-activated receptor 4; SMURF2 = SMAD-specific E3 ubiquitin ligase 2; UPF1 = up-frameshift 1. * p<0.05, ** p<0.01, *** p<0.001.

    Article Snippet: H9C2 cells were lysed and incubated with magnetic beads preconjugated with antibodies anti-UPF1 (#12040, CST) or anti-immunoglobulin G (IgG) (ab182931, Abcam).

    Techniques: Negative Control, Over Expression, Ubiquitin Proteomics

    Journal: iScience

    Article Title: C9orf72 poly-PR forms anisotropic condensates causative of nuclear TDP-43 pathology

    doi: 10.1016/j.isci.2024.110937

    Figure Lengend Snippet:

    Article Snippet: UPF1 (rabbit polyclonal) , Proteintech , Cat# 23379-1-AP; RRID: AB_11232421.

    Techniques: Labeling, Virus, Recombinant, Transfection, Reverse Transcription, Lysis, Western Blot, Staining, Derivative Assay, Plasmid Preparation, Software, Imaging, Microscopy, Real-time Polymerase Chain Reaction