Rabbit Polyclonal RENT1/hUPF1 antibody. Suitable for IP, WB and reacts with Human, Mouse samples. Cited in 7 publications.
View Alternative Names
KIAA0221, RENT1, UPF1, Regulator of nonsense transcripts 1, ATP-dependent helicase RENT1, Nonsense mRNA reducing factor 1, Up-frameshift suppressor 1 homolog, NORF1, hUpf1
- IP
Unknown
Immunoprecipitation - Anti-RENT1/hUPF1 antibody (AB86057)
Detection of RENT1/hUPF1 by Western Blot of Immunprecipitate.
ab86057 at 1µg/ml staining RENT1/hUPF1 in HeLa whole cell lysate immunoprecipitated using ab86057 at 3µg/mg lysate (1 mg/IP; 20% of IP loaded/lane).
Detection : Chemiluminescence with exposure time of 10 seconds.
All lanes:
Immunoprecipitation - Anti-RENT1/hUPF1 antibody (ab86057)
Predicted band size: 124 kDa
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- WB
Unknown
Western blot - Anti-RENT1/hUPF1 antibody (AB86057)
All lanes:
Western blot - Anti-RENT1/hUPF1 antibody (ab86057) at 0.04 µg/mL
Lane 1:
HeLa whole cell lysate at 50 µg
Lane 2:
HeLa whole cell lysate at 15 µg
Lane 3:
HeLa whole cell lysate at 5 µg
Lane 4:
NIH3T3 whole cell lysate at 50 µg
Predicted band size: 124 kDa
Observed band size: 134 kDa
false
Exposure time: 10s
- WB
CiteAb
Western blot - Anti-RENT1/hUPF1 antibody (AB86057)
RENT1/hUPF1 western blot using anti-RENT1/hUPF1 antibody ab86057. Publication image and figure legend from Trzaska, C., Amand, S., et al., 2020, Nat Commun, PubMed 32198346.
ab86057 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab86057 please see the product overview.
DAP interferes with the activity of FTSJ1.a Determination by tandem mass spectrometry of the amino acid incorporated at the PTC position. Firefly luciferase from HEK293FT cells transfected with the Fluc-int-UGA construct was immunoprecipitated and digested with trypsin. The MS/MS spectrum of the peptide containing the PTC position and the sequence determination are shown. The upper red and blue sequences indicate the amino acids validated, respectively, by detection of Nter and Cter peptide fragments (b and y ion series). Peptide fragments y6 and y7 clearly identify tryptophan (W) at the PTC position. The black peaks correspond to non-attributed mass-to-charge ratio (m/z) values. The green peaks are internal fragments that do not contain an extremity of the peptide. b The efficiency of UGA readthrough by DAP decreases with increasing amounts of FTSJ1 but not with increasing amounts of CTU1. Readthrough efficiency was determined by measuring luciferase activity in HeLa cells co-transfected with the firefly luciferase construct described in Fig. 1b and with increasing amounts of an expression vector for either FTSJ1 or CTU1 (0.5, 1, or 2 µg). The empty expression vector (E.v.) was used as control. The cells were then exposed to 0, 0.39, 0.78, 1.56, 6.25, 25, 100, 300, or 600 µM DAP for 24 h before measuring the luciferase activity. The experiment was performed twice and the results of both experiments (Exp1 and Exp2) are shown. c Western blot analysis of FTSJ1 and CTU1. d 2′-O-methylation analysis of tRNATrp, tRNASER, and tRNAGLN by RiboMethSeq. HeLa cells were incubated for 24 h with DMSO or with 25 µM DAP. A MethScore was attributed to each tRNA 2′-O-methylation in tRNA purified from HeLa cells treated with DAP (dark green histogram) or DMSO (light green histogram). The results of three independent experiments are indicated with the symbols square, point, or triangle. e Analysis of DAP affinity column eluates shows that DAP interacts with FTSJ1. HeLa-cell extract was incubated with DAP covalently bound to beads or with beads alone. Proteins bound to the columns were eluted with excess DAP and the eluates analyzed by western blot. A molecular weight marker is indicated to the left of each gel. p-values (p) were calculated using Student’s t-test. Source data are provided as a Source Data file.
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Reactivity data
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Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
RENT1/hUPF1 ensures the quality control of mRNA by facilitating the rapid degradation of defective transcripts and thereby preventing the synthesis of potentially harmful truncated proteins. As part of the NMD complex UPF1 partners with proteins like UPF2 and UPF3 to form a surveillance mechanism that maintains cellular homeostasis. The complex cooperates to distinguish transcripts that require elimination from those necessary for normal cellular function.
Pathways
RENT1/hUPF1 integrates into essential cellular pathways beyond just NMD. The protein also links to the mRNA decay and translation initiation pathways playing significant roles alongside proteins such as SMG1 and eRF1. In these pathways UPF1 regulates gene expression by modulating mRNA stability and protein synthesis ensuring that only correctly processed mRNAs translate into proteins.
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Publications (7)
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Life science alliance 7: PubMed38986569
2024
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The Journal of biological chemistry 299:104577 PubMed36871759
2023
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Nucleic acids research 49:11022-11037 PubMed34634811
2021
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Molecular biology of the cell 32:ar38 PubMed34586879
2021
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Nature communications 11:1509 PubMed32198346
2020
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Journal of cell science 130:3009-3022 PubMed28743738
2017
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Molecular cell 67:239-251.e6 PubMed28669802
2017
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