mouse anti cpsf2 Search Results


92
Santa Cruz Biotechnology mouse anti cpsf2
KEY RESOURCES TABLE
Mouse Anti Cpsf2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Abcam rabbit polyclonal cpsf2
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Rabbit Polyclonal Cpsf2, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Proteintech 1 ap rrid ab 2084368
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1 Ap Rrid Ab 2084368, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Santa Cruz Biotechnology goat anti cpsf2
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Goat Anti Cpsf2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
Bethyl cpsf2
Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
Cpsf2, supplied by Bethyl, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
Aviva Systems anti dido1
Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
Anti Dido1, supplied by Aviva Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Proteintech mouse anti β actin
Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
Mouse Anti β Actin, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Cell Signaling Technology Inc anti cd44 mouse monoclonal antibody
Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
Anti Cd44 Mouse Monoclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Santa Cruz Biotechnology mouse anti mrpl42
Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
Mouse Anti Mrpl42, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
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93
Santa Cruz Biotechnology mouse anti mrps27
Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
Mouse Anti Mrps27, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Santa Cruz Biotechnology mouse anti mrpl44
Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
Mouse Anti Mrpl44, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
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93
Proteintech rabbit anti cstf64
Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
Rabbit Anti Cstf64, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


KEY RESOURCES TABLE

Journal: Cell reports

Article Title: Non-canonical isoforms of the mRNA polyadenylation factor WDR33 regulate STING-mediated immune responses

doi: 10.1016/j.celrep.2024.113886

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: Mouse anti-CPSF2 , Santa Cruz Biotechnology , Cat# sc-165983; RRID: AB_2084371.

Techniques: Virus, Recombinant, Negative Control, Software

Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( CPSF2 ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.

Journal: Nucleic Acids Research

Article Title: eIF2D promotes 40S ribosomal subunit recycling during intrinsic ribosome destabilization

doi: 10.1093/nar/gkaf1322

Figure Lengend Snippet: Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( CPSF2 ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.

Article Snippet: Primary antibodies against MCTS1 (#GTX117793; GeneTex), DENR (203057-T46; Sino biologicals), eIF2D (12840-1-AP; Proteintech), CPSF2 (A301-581A; Bethyl Laboratories), HSP90 (610 419; BD Biosciences), and V5 epitope (R960CUS; Thermo Fisher Scientific) were used in this study.

Techniques: Control, Two Tailed Test, MANN-WHITNEY, Alternative Splicing, Clone Assay, Western Blot