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thrap3 proteintech 19744 1 ap wb  (Proteintech)
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Proteintech thrap3 proteintech 19744 1 ap wb
Thrap3 Proteintech 19744 1 Ap Wb, 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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thrap3  (Santa Cruz Biotechnology)
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Thrap3, supplied by Santa Cruz Biotechnology, 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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thrap3  (Proteintech)
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Proteintech thrap3
A KEGG pathway enrichment analysis of genes affected by NLRP7 mutation in hiPSCs. The RNA-seq data was derived from the study of Alici-Garipcan et al. . B Representative western blot analysis of NLRP7, γH2A.X, PARP1, PRPF8, <t>THRAP3</t> and DDX39B in p-WT and p-NLRP7 −/− . C Representative immunofluorescent images of p-WT and p-NLRP7 −/− for the DNA damage marker γH2A.X (green). The nuclei were counterstained with DAPI and are shown in blue. Increased γH2A.X + cells are detected in p-NLRP7 −/− . Scale bar, 50 μm. BOX, Scale bar, 10 μm. D Quantification of the γH2A.X foci in the immunofluorescent staining shown in ( C ). Non-parametric test. E Comet assay reveals severe DNA damage in the p-NLRP7 −/− . Genomic DNA was stained with DAPI and imaged after single-cell electrophoresis. More than 200 cells were analyzed in each group. F Quantification for the length of the tail movement. Data are shown as mean ± SEM. ** P < 0.001, Non-parametric test. G Representative immunofluorescent images of p-WT and p-NLRP7 −/− for the apoptosis marker active caspase 3 (Red). Scale bar, 50 μm. BOX, Scale bar, 10 μm. H Quantification of the Active Caspase 3 in the immunofluorescent staining shown in ( G ). Data are shown as mean ± SEM. Student’s t -test.
Thrap3, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/thrap3/product/Proteintech
Average 94 stars, based on 1 article reviews
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ddx39b  (Proteintech)
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Proteintech ddx39b
A KEGG pathway enrichment analysis of genes affected by NLRP7 mutation in hiPSCs. The RNA-seq data was derived from the study of Alici-Garipcan et al. . B Representative western blot analysis of NLRP7, γH2A.X, PARP1, PRPF8, <t>THRAP3</t> and DDX39B in p-WT and p-NLRP7 −/− . C Representative immunofluorescent images of p-WT and p-NLRP7 −/− for the DNA damage marker γH2A.X (green). The nuclei were counterstained with DAPI and are shown in blue. Increased γH2A.X + cells are detected in p-NLRP7 −/− . Scale bar, 50 μm. BOX, Scale bar, 10 μm. D Quantification of the γH2A.X foci in the immunofluorescent staining shown in ( C ). Non-parametric test. E Comet assay reveals severe DNA damage in the p-NLRP7 −/− . Genomic DNA was stained with DAPI and imaged after single-cell electrophoresis. More than 200 cells were analyzed in each group. F Quantification for the length of the tail movement. Data are shown as mean ± SEM. ** P < 0.001, Non-parametric test. G Representative immunofluorescent images of p-WT and p-NLRP7 −/− for the apoptosis marker active caspase 3 (Red). Scale bar, 50 μm. BOX, Scale bar, 10 μm. H Quantification of the Active Caspase 3 in the immunofluorescent staining shown in ( G ). Data are shown as mean ± SEM. Student’s t -test.
Ddx39b, supplied by Proteintech, 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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thrap3 rabbit pab a9396 antibody  (ABclonal Biotechnology)
90
ABclonal Biotechnology thrap3 rabbit pab a9396 antibody
(A) Top hits from dsRNA immunoprecipitation-mass spectrometry (IP-MS) of TC83 and TC83/E1 IDsyn in Raw264.7. Raw264.7 cells were infected with TC83 or TC83/E1 IDsyn at an MOI of 0.1, and viral dsRNA isolated from lysates at 24 hpi using J2 dsRNA antibody or IgG isotype control. RNA-bound proteins were identified by MS, and fold-enrichment of spectral counts relative to IgG controls was calculated. Prioritized hits were chosen based on fold enrichment scores, total spectral counts, and whether targets are known RNA binding proteins (RBPbase hits). (B) Hits equally enriched in TC83 and TC83/E1 IDsyn . (C) STRING network analysis of top proteomics hits. Candidates meeting the cutoff criteria (A) were subjected to Protein-Protein Interaction Networks Functional Enrichment Analysis. Candidate proteins identified in the screen are highlighted in red and interacting proteins in blue. (D) Enriched biological process GO terms that with a p-value >0.001, along with the observed gene count present in the STRING network (E-H) Raw264.7 were transfected with control (NSC) or pooled (3 siRNA) gene specific siRNAs targeting (E) <t>Thrap3,</t> (F) Fbl, (G) Ubap2l, or (H) Dhx38 for 24 hours. Cells were infected TC83 or TC83/E1 ID-syn at an MOI of 0.1, cell culture supernatants collected at 24hpi, and infectious virus titered by FFA. All siRNAs were assayed simultaneously but for visual clarity, data for each gene is shown separately along with the shared control siRNA samples. Each experiment was performed in triplicate three times independently and the mean and SD are graphed. Statistical analysis was performed using unpaired t-test. ** >0.001, ***>0.0001. Fold change and p-values are indicated on each graph.
Thrap3 Rabbit Pab A9396 Antibody, supplied by ABclonal 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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Image Search Results


A KEGG pathway enrichment analysis of genes affected by NLRP7 mutation in hiPSCs. The RNA-seq data was derived from the study of Alici-Garipcan et al. . B Representative western blot analysis of NLRP7, γH2A.X, PARP1, PRPF8, THRAP3 and DDX39B in p-WT and p-NLRP7 −/− . C Representative immunofluorescent images of p-WT and p-NLRP7 −/− for the DNA damage marker γH2A.X (green). The nuclei were counterstained with DAPI and are shown in blue. Increased γH2A.X + cells are detected in p-NLRP7 −/− . Scale bar, 50 μm. BOX, Scale bar, 10 μm. D Quantification of the γH2A.X foci in the immunofluorescent staining shown in ( C ). Non-parametric test. E Comet assay reveals severe DNA damage in the p-NLRP7 −/− . Genomic DNA was stained with DAPI and imaged after single-cell electrophoresis. More than 200 cells were analyzed in each group. F Quantification for the length of the tail movement. Data are shown as mean ± SEM. ** P < 0.001, Non-parametric test. G Representative immunofluorescent images of p-WT and p-NLRP7 −/− for the apoptosis marker active caspase 3 (Red). Scale bar, 50 μm. BOX, Scale bar, 10 μm. H Quantification of the Active Caspase 3 in the immunofluorescent staining shown in ( G ). Data are shown as mean ± SEM. Student’s t -test.

Journal: Communications Biology

Article Title: NLRP7 maintains the genomic stability during early human embryogenesis via mediating alternative splicing

doi: 10.1038/s42003-025-07571-5

Figure Lengend Snippet: A KEGG pathway enrichment analysis of genes affected by NLRP7 mutation in hiPSCs. The RNA-seq data was derived from the study of Alici-Garipcan et al. . B Representative western blot analysis of NLRP7, γH2A.X, PARP1, PRPF8, THRAP3 and DDX39B in p-WT and p-NLRP7 −/− . C Representative immunofluorescent images of p-WT and p-NLRP7 −/− for the DNA damage marker γH2A.X (green). The nuclei were counterstained with DAPI and are shown in blue. Increased γH2A.X + cells are detected in p-NLRP7 −/− . Scale bar, 50 μm. BOX, Scale bar, 10 μm. D Quantification of the γH2A.X foci in the immunofluorescent staining shown in ( C ). Non-parametric test. E Comet assay reveals severe DNA damage in the p-NLRP7 −/− . Genomic DNA was stained with DAPI and imaged after single-cell electrophoresis. More than 200 cells were analyzed in each group. F Quantification for the length of the tail movement. Data are shown as mean ± SEM. ** P < 0.001, Non-parametric test. G Representative immunofluorescent images of p-WT and p-NLRP7 −/− for the apoptosis marker active caspase 3 (Red). Scale bar, 50 μm. BOX, Scale bar, 10 μm. H Quantification of the Active Caspase 3 in the immunofluorescent staining shown in ( G ). Data are shown as mean ± SEM. Student’s t -test.

Article Snippet: The primary antibodies and appropriate fluorohore-conjugated secondary antibodies used in this study are as follows: OCT4 (Santa Cruz, sc-5279), NANOG (Thermo Fisher Scientific, PA1-097X), NLRP7 (Abcam, ab105405), KLF17 (ATLAS ANTIBODIES, HPA024629), CDX2 (Abcam, ab76541), GATA3 (Abcam, ab199428), KRT7 (Abcam, ab68459), HLA-G (Santa Cruz, sc-21799), BrdU (BD Biosciences, 347580), γH2A.X (Cell Signaling Technology, 9718S), γH2A.X (abmart, M63324), Active-Caspase 3 (Cell Signaling Technology, 9661S), Rad51 (Abcam, ab133534), Flag (Proteintech, 66008-4-Ig), Flag (abmart, M20008S), DDX39B (Proteintech, 14798-1-AP), THRAP3 (Proteintech, 19744-1-AP), PRPF8 (Proteintech, 11171-1-AP), PARP1 (Proteintech, 66520-1-Ig), GAPDH (Proteintech, 60004-1-Ig), Goat anti-Mouse IgG (H + L) (Thermo Fisher Scientific, A-11001), and Goat anti-Rabbit IgG (H + L) (Thermo Fisher Scientific, A-11012).

Techniques: Mutagenesis, RNA Sequencing, Derivative Assay, Western Blot, Marker, Staining, Single Cell Gel Electrophoresis, Electrophoresis

A Localization of NLRP7, RAD51, and DNA damage marker γH2A.X under different conditions. Scale bar, 50 μm. BOX, Scale bar, 10 μm. B Representative image of silver staining for proteins immunoprecipitated with NLRP7 using an anti-Flag antibody. The Flag-NLRP7 band is indicated with a black triangle. C KEGG analysis for proteins interacting with NLRP7 showed enriched Microbial infection and spliceosome-associated terms. D GO analysis for proteins interacting with NLRP7 showed enriched RNA processing-associated terms. E Left: Venn diagram showed overlap between the proteins that interacted with NLRP7 from this study and another independent study . Right: List of proteins in common is given. F GO analysis for proteins in common showed enriched RNA processing and RNA splicing associated terms. G–K Co-IP revealed the interaction of NLRP7 with factors related to AS and DDR, including DDX39B, PRPF8, THRAP3, and PARP1.

Journal: Communications Biology

Article Title: NLRP7 maintains the genomic stability during early human embryogenesis via mediating alternative splicing

doi: 10.1038/s42003-025-07571-5

Figure Lengend Snippet: A Localization of NLRP7, RAD51, and DNA damage marker γH2A.X under different conditions. Scale bar, 50 μm. BOX, Scale bar, 10 μm. B Representative image of silver staining for proteins immunoprecipitated with NLRP7 using an anti-Flag antibody. The Flag-NLRP7 band is indicated with a black triangle. C KEGG analysis for proteins interacting with NLRP7 showed enriched Microbial infection and spliceosome-associated terms. D GO analysis for proteins interacting with NLRP7 showed enriched RNA processing-associated terms. E Left: Venn diagram showed overlap between the proteins that interacted with NLRP7 from this study and another independent study . Right: List of proteins in common is given. F GO analysis for proteins in common showed enriched RNA processing and RNA splicing associated terms. G–K Co-IP revealed the interaction of NLRP7 with factors related to AS and DDR, including DDX39B, PRPF8, THRAP3, and PARP1.

Article Snippet: The primary antibodies and appropriate fluorohore-conjugated secondary antibodies used in this study are as follows: OCT4 (Santa Cruz, sc-5279), NANOG (Thermo Fisher Scientific, PA1-097X), NLRP7 (Abcam, ab105405), KLF17 (ATLAS ANTIBODIES, HPA024629), CDX2 (Abcam, ab76541), GATA3 (Abcam, ab199428), KRT7 (Abcam, ab68459), HLA-G (Santa Cruz, sc-21799), BrdU (BD Biosciences, 347580), γH2A.X (Cell Signaling Technology, 9718S), γH2A.X (abmart, M63324), Active-Caspase 3 (Cell Signaling Technology, 9661S), Rad51 (Abcam, ab133534), Flag (Proteintech, 66008-4-Ig), Flag (abmart, M20008S), DDX39B (Proteintech, 14798-1-AP), THRAP3 (Proteintech, 19744-1-AP), PRPF8 (Proteintech, 11171-1-AP), PARP1 (Proteintech, 66520-1-Ig), GAPDH (Proteintech, 60004-1-Ig), Goat anti-Mouse IgG (H + L) (Thermo Fisher Scientific, A-11001), and Goat anti-Rabbit IgG (H + L) (Thermo Fisher Scientific, A-11012).

Techniques: Marker, Silver Staining, Immunoprecipitation, Infection, Co-Immunoprecipitation Assay

(A) Top hits from dsRNA immunoprecipitation-mass spectrometry (IP-MS) of TC83 and TC83/E1 IDsyn in Raw264.7. Raw264.7 cells were infected with TC83 or TC83/E1 IDsyn at an MOI of 0.1, and viral dsRNA isolated from lysates at 24 hpi using J2 dsRNA antibody or IgG isotype control. RNA-bound proteins were identified by MS, and fold-enrichment of spectral counts relative to IgG controls was calculated. Prioritized hits were chosen based on fold enrichment scores, total spectral counts, and whether targets are known RNA binding proteins (RBPbase hits). (B) Hits equally enriched in TC83 and TC83/E1 IDsyn . (C) STRING network analysis of top proteomics hits. Candidates meeting the cutoff criteria (A) were subjected to Protein-Protein Interaction Networks Functional Enrichment Analysis. Candidate proteins identified in the screen are highlighted in red and interacting proteins in blue. (D) Enriched biological process GO terms that with a p-value >0.001, along with the observed gene count present in the STRING network (E-H) Raw264.7 were transfected with control (NSC) or pooled (3 siRNA) gene specific siRNAs targeting (E) Thrap3, (F) Fbl, (G) Ubap2l, or (H) Dhx38 for 24 hours. Cells were infected TC83 or TC83/E1 ID-syn at an MOI of 0.1, cell culture supernatants collected at 24hpi, and infectious virus titered by FFA. All siRNAs were assayed simultaneously but for visual clarity, data for each gene is shown separately along with the shared control siRNA samples. Each experiment was performed in triplicate three times independently and the mean and SD are graphed. Statistical analysis was performed using unpaired t-test. ** >0.001, ***>0.0001. Fold change and p-values are indicated on each graph.

Journal: PLOS Pathogens

Article Title: RNA structures within Venezuelan equine encephalitis virus E1 alter macrophage replication fitness and contribute to viral emergence

doi: 10.1371/journal.ppat.1012179

Figure Lengend Snippet: (A) Top hits from dsRNA immunoprecipitation-mass spectrometry (IP-MS) of TC83 and TC83/E1 IDsyn in Raw264.7. Raw264.7 cells were infected with TC83 or TC83/E1 IDsyn at an MOI of 0.1, and viral dsRNA isolated from lysates at 24 hpi using J2 dsRNA antibody or IgG isotype control. RNA-bound proteins were identified by MS, and fold-enrichment of spectral counts relative to IgG controls was calculated. Prioritized hits were chosen based on fold enrichment scores, total spectral counts, and whether targets are known RNA binding proteins (RBPbase hits). (B) Hits equally enriched in TC83 and TC83/E1 IDsyn . (C) STRING network analysis of top proteomics hits. Candidates meeting the cutoff criteria (A) were subjected to Protein-Protein Interaction Networks Functional Enrichment Analysis. Candidate proteins identified in the screen are highlighted in red and interacting proteins in blue. (D) Enriched biological process GO terms that with a p-value >0.001, along with the observed gene count present in the STRING network (E-H) Raw264.7 were transfected with control (NSC) or pooled (3 siRNA) gene specific siRNAs targeting (E) Thrap3, (F) Fbl, (G) Ubap2l, or (H) Dhx38 for 24 hours. Cells were infected TC83 or TC83/E1 ID-syn at an MOI of 0.1, cell culture supernatants collected at 24hpi, and infectious virus titered by FFA. All siRNAs were assayed simultaneously but for visual clarity, data for each gene is shown separately along with the shared control siRNA samples. Each experiment was performed in triplicate three times independently and the mean and SD are graphed. Statistical analysis was performed using unpaired t-test. ** >0.001, ***>0.0001. Fold change and p-values are indicated on each graph.

Article Snippet: The following antibodies were used: beta-Actin Mouse mAb (Cell signaling, 8H10D10), beta-Actin Rabbit mAb (Cell signaling, 13E5), Rig-I mAb (Cell signaling, D1466), MDA-5 Rabbit mAb (Cell signaling, D74E4), Fibrillarin/U3 RNP Rabbit pAb (ABclonal, A1136), Dhx38 (ABclonal A4341), Thrap3 Rabbit pAb (ABclonal, A9396), UBAP2L (E5X4E) Rabbit mAb (Cell Signaling Technology, 40199), Goat-anti-Rabbit IRDye 800 (Licor, 926–32211), Goat-anti-mouse IRDye 680 (Licor, 926–68070).

Techniques: Immunoprecipitation, Mass Spectrometry, Protein-Protein interactions, Infection, Isolation, Control, RNA Binding Assay, Functional Assay, Transfection, Cell Culture, Virus

(A) Schematic of translation reporter and replicon RNAs used. (B) 4μg of translation reporter RNA containing the E1 sequence from either TC83 or TC83/E1 ID-syn were nucleofected into Raw264.7 macrophages. Cell lysates were collected at indicated times post nucleofection and luciferase activity measured. Data depicted as fold change over the TC83 samples for all time points. (C) 4μg nano/firefly replicon reporter RNAs was nucleofected into Raw264.7 macrophages and cell lysates were harvested and dual-luciferase activity measured for indicated time-points. Nano-luciferase activity is displayed as fold change RLU/μg over TC83. (D-F) Raw264.7 were infected (MOI 1) with TC83 or TC83/E1 ID-syn and lysates were harvested at 1, 3, 6 and 12hpi. RT-qPCR was performed using probes specific for genomic and sub-genomic RNA species. (D) the fold change between genomic and sub-genomic RNA per time point is displayed, (E-F) viral RNA ffu equivalence was calculated using a standard from RNA derived from a known concentration virus stock. (G-H) Raw264.7 were transfected with a non-silencing control (NSC) or Thrap3 siRNA and after 24hs cells were nucleofected with 4μg of translation reporter RNA constructs. Cell lysates were collected at indicated times post nucleofection and luciferase activity measured. The fold-change in RLU/μg is displayed for each time point. Each experiment was performed in duplicate or triplicate, three times independently and the mean and SD graphed. Statistical analysis was performed using an unpaired T-test.

Journal: PLOS Pathogens

Article Title: RNA structures within Venezuelan equine encephalitis virus E1 alter macrophage replication fitness and contribute to viral emergence

doi: 10.1371/journal.ppat.1012179

Figure Lengend Snippet: (A) Schematic of translation reporter and replicon RNAs used. (B) 4μg of translation reporter RNA containing the E1 sequence from either TC83 or TC83/E1 ID-syn were nucleofected into Raw264.7 macrophages. Cell lysates were collected at indicated times post nucleofection and luciferase activity measured. Data depicted as fold change over the TC83 samples for all time points. (C) 4μg nano/firefly replicon reporter RNAs was nucleofected into Raw264.7 macrophages and cell lysates were harvested and dual-luciferase activity measured for indicated time-points. Nano-luciferase activity is displayed as fold change RLU/μg over TC83. (D-F) Raw264.7 were infected (MOI 1) with TC83 or TC83/E1 ID-syn and lysates were harvested at 1, 3, 6 and 12hpi. RT-qPCR was performed using probes specific for genomic and sub-genomic RNA species. (D) the fold change between genomic and sub-genomic RNA per time point is displayed, (E-F) viral RNA ffu equivalence was calculated using a standard from RNA derived from a known concentration virus stock. (G-H) Raw264.7 were transfected with a non-silencing control (NSC) or Thrap3 siRNA and after 24hs cells were nucleofected with 4μg of translation reporter RNA constructs. Cell lysates were collected at indicated times post nucleofection and luciferase activity measured. The fold-change in RLU/μg is displayed for each time point. Each experiment was performed in duplicate or triplicate, three times independently and the mean and SD graphed. Statistical analysis was performed using an unpaired T-test.

Article Snippet: The following antibodies were used: beta-Actin Mouse mAb (Cell signaling, 8H10D10), beta-Actin Rabbit mAb (Cell signaling, 13E5), Rig-I mAb (Cell signaling, D1466), MDA-5 Rabbit mAb (Cell signaling, D74E4), Fibrillarin/U3 RNP Rabbit pAb (ABclonal, A1136), Dhx38 (ABclonal A4341), Thrap3 Rabbit pAb (ABclonal, A9396), UBAP2L (E5X4E) Rabbit mAb (Cell Signaling Technology, 40199), Goat-anti-Rabbit IRDye 800 (Licor, 926–32211), Goat-anti-mouse IRDye 680 (Licor, 926–68070).

Techniques: Sequencing, Luciferase, Activity Assay, Infection, Quantitative RT-PCR, Derivative Assay, Concentration Assay, Virus, Transfection, Control, Construct