goat anti sin3a Search Results


anti rabbit igg antibody  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology anti rabbit igg antibody
The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
Anti Rabbit Igg Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+sin3a/goat+anti-rabbit+IgG-B/pmc03979996-84-32-15
Average 96 stars, based on 1 article reviews
anti rabbit igg antibody - by Bioz Stars, 2026-11
96/100 stars
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goat anti sin3a  (R&D Systems)
92
R&D Systems goat anti sin3a
The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
Goat Anti Sin3a, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+sin3a/Human%2FMouse+SIN3A+Antibody/pmc11350972-133-68-71
Average 92 stars, based on 1 article reviews
goat anti sin3a - by Bioz Stars, 2026-11
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sin3a  (Cell Signaling Technology Inc)
93
Cell Signaling Technology Inc sin3a
Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the <t>Sin3A</t> complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.
Sin3a, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+sin3a/SIN3A+Rabbit+mAb/pmc12300445-101-48-50
Average 93 stars, based on 1 article reviews
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anti sin3a  (Bethyl)
91
Bethyl anti sin3a
Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the <t>Sin3A</t> complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.
Anti Sin3a, supplied by Bethyl, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+sin3a/Sin3A+Antibody/pmc06728282-141-46-34
Average 91 stars, based on 1 article reviews
anti sin3a - by Bioz Stars, 2026-11
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goat-anti-mouse hrp-conjugated antibodies  (Promega)
90
Promega goat-anti-mouse hrp-conjugated antibodies
Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the <t>Sin3A</t> complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.
Goat Anti Mouse Hrp Conjugated Antibodies, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+sin3a/hrp+conjugated+secondary+antibodies/pmc07713351-189-28-37
Average 90 stars, based on 1 article reviews
goat-anti-mouse hrp-conjugated antibodies - by Bioz Stars, 2026-11
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goat anti-egfr antibody  (GeneTex)
90
GeneTex goat anti-egfr antibody
Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the <t>Sin3A</t> complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.
Goat Anti Egfr Antibody, supplied by GeneTex, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+sin3a/anti+egfr+antibody/pm39192337-148-60-64
Average 90 stars, based on 1 article reviews
goat anti-egfr antibody - by Bioz Stars, 2026-11
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odyssey imaging system  (LI-COR)
99
LI-COR odyssey imaging system
Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the <t>Sin3A</t> complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.
Odyssey Imaging System, supplied by LI-COR, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+sin3a/Odyssey+Imaging+System/custom%40odyssey-imaging-system%4010%2E1074%2Fmcp%2Era120%2E002078
Average 99 stars, based on 1 article reviews
odyssey imaging system - by Bioz Stars, 2026-11
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goat anti somatostatin  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology goat anti somatostatin
Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the <t>Sin3A</t> complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.
Goat Anti Somatostatin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+sin3a/Somatostatin/pmc07243292-118-77-80
Average 96 stars, based on 1 article reviews
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odyssey  (LI-COR)
99
LI-COR odyssey
Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the <t>Sin3A</t> complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.
Odyssey, supplied by LI-COR, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+sin3a/Odyssey/custom%40Odyssey%4010%2E1074%2Fmcp%2Era120%2E002078
Average 99 stars, based on 1 article reviews
odyssey - by Bioz Stars, 2026-11
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goatarabbit irdye 800cw  (LI-COR)
99
LI-COR goatarabbit irdye 800cw
Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the <t>Sin3A</t> complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.
Goatarabbit Irdye 800cw, supplied by LI-COR, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+sin3a/GOATaRABBIT+IRDye+800CW/custom%40926-32211%4010%2E1074%2Fmcp%2Era120%2E002078
Average 99 stars, based on 1 article reviews
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goat anti mouse  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc goat anti mouse
Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the <t>Sin3A</t> complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.
Goat Anti Mouse, 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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Average 96 stars, based on 1 article reviews
goat anti mouse - by Bioz Stars, 2026-11
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goat anti mouse igg  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology goat anti mouse igg
Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the <t>Sin3A</t> complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.
Goat Anti Mouse Igg, supplied by Santa Cruz Biotechnology, 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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Average 96 stars, based on 1 article reviews
goat anti mouse igg - by Bioz Stars, 2026-11
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Image Search Results


The Sin3A co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect Sin3A. β-actin was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.

Journal: International Journal of Biological Sciences

Article Title: ELK3 Suppresses Angiogenesis by Inhibiting the Transcriptional Activity of ETS-1 on MT1-MMP

doi: 10.7150/ijbs.8095

Figure Lengend Snippet: The Sin3A co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect Sin3A. β-actin was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.

Article Snippet: Next, the membrane was incubated with monoclonal anti-Sin3A (Santa Cruz Biotechnology, sc-994) (1:1000 dilution), anti-ELK3 (Santa Cruz Biotechnology, sc-17860) (1:1000 dilution) or anti-β-actin antibody (1:3000 dilution) overnight at 4°C, then incubated with anti-rabbit IgG antibody (1:2000 dilution, secondary antibody against anti-Sin3A) or anti-goat IgG antibody (1:2000 dilution, secondary antibody against anti-ELK3 and anti-β-actin) for 1 h at room temperature.

Techniques: Activity Assay, Transfection, Plasmid Preparation, Luciferase, Expressing, Isolation, SDS Page, Software, Over Expression, Western Blot

Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the Sin3A complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.

Journal: Viruses

Article Title: IFI16 Mediates Deacetylation of KSHV Chromatin via Interaction with NuRD and Sin3A Co-Repressor Complexes

doi: 10.3390/v17070921

Figure Lengend Snippet: Immunoprecipitation (IP) of IFI16 followed by label-free quantitative mass spectrometry (IP-LFQ-MS) analysis. Whole-cell lysates of latently infected BCBL-1 cells were immunoprecipitated with two separate anti-IFI16 antibodies: anti-IFI16 mouse monoclonal (Ms), anti-IFI16 rabbit polyclonal (Rb), or IgG (Rb), followed by purification of the co-precipitated proteins using Protein A/G Dynabeads (two biological replicates, each). Subsequently, on-bead trypsin digestion and LC-MS/MS were performed to identify the co-precipitated proteins. ( A ) Venn diagram of proteins enriched (Log2 fold change ≥ 0.6) in the two IPs using mouse and rabbit antibodies against IFI16, compared to IgG controls. Proteins common to both the IPs are represented in orange, while those exclusive to the Ms antibody are represented in pink, and those exclusive to the Rb antibody are represented in green. ( B , C ) Volcano plot of proteins enriched in IFI16 IP using the Rb antibody ( B ), and the Ms antibody ( C ) compared to IgG controls. Proteins identified by LC-MS/MS were analyzed for differential abundance between IP conditions, and log2 fold change and −log10 p -values were calculated for each protein. Highlighted proteins (colored dots) indicate the proteins of interest: Red: core subunit proteins common to both the NuRD complex and the Sin3A complex (HDAC1, HDAC2, RbAp46, and RbAp48). Orange: proteins of the NuRD complex, other than the core subunit (CHD4, MTA1, MTA2, and MBD2/3). Pink: proteins of the Sin3A complex, other than the core subunit (Sin3A and SAP18). Green: IFI16 itself (bait). The dashed lines indicate the Log2FC ≥ 0.6 threshold. ( D ) Heatmap showing the Log2 fold change values for the highlighted proteins of interest, comparing the two IFI16 IPs, Ms and Rb antibodies versus IgG controls. Fold changes were calculated from LFQ intensities using duplicate replicates per condition. Proteins consistently enriched across both antibody conditions support their role as robust interactors of IFI16. ( E ) The label-free quantitation intensities (LFQ) and sequence coverage (SC%) of the proteins of interest.

Article Snippet: The antibodies used for this study are: IFI16, anti-mouse (Santa Cruz Biotechnology, Dallas, TX, USA, SC-8023); IFI16, anti-rabbit (Millipore Sigma, HPA073514); KSHV LANA, anti-rabbit (In-house); HDAC1, anti-rabbit (Proteintech, Rosemont, IL, USA, 10197-1-AP); HDAC1, anti-goat (Origene, Rockville, MD, USA, TA348968); HDAC2, anti-rabbit (Proteintech, 12922-3-AP); CHD4, anti-rabbit (Cell Signaling, 12011); SIN3A, anti-rabbit (Cell Signaling, 8056); CoREST anti-rabbit (Cell Signaling, 14567); Histone H2A anti-rabbit (Cell Signaling, 12349); Acetyl-Histone H2A anti-rabbit (Cell Signaling, 2576); Histone H2B anti-rabbit (Cell Signaling 12364); Acetyl-Histone H2B anti-rabbit (Cell Signaling, 12799); Histone H3 anti-rabbit (Cell Signaling, 4499); Acetyl-Histone H3 anti-rabbit (Cell Signaling, 8173); Histone H4 anti-rabbit (Cell Signaling, 13919); Acetyl-Histone H4 anti-rabbit (Cell Signaling, 13534); anti-rabbit control IgG (Proteintech, 30000-0-AP); Anti-rabbit IgG Alexa Fluor 488 (Invitrogen, A-11008); Anti-mouse IgG Alexa Fluor 488 (Invitrogen, A-11001).

Techniques: Immunoprecipitation, Mass Spectrometry, Infection, Purification, Liquid Chromatography with Mass Spectroscopy, Quantitation Assay, Sequencing

Interaction of IFI16 with CHD4 and Sin3A. ( A ) Proximity ligation assay (PLA, red) was performed for CHD4, Sin3A, CoREST, and IgG with IFI16 in BCBL-1 cells. The red channel shows the PLA puncta. Also, IFA (green) for KSHV LANA was conducted in the same experiment. White arrowheads in the enlarged image point to the colocalization (yellow) between the PLA dots and KSHV LANA. ( B ) The quantification of the PLA dots is represented as PLA dots/cell in a swarm plot. Kruskal–Wallis test with Dunn’s multiple comparisons test was performed (BioRender.com). p < 0.05 (*), p < 0.0001 (****).

Journal: Viruses

Article Title: IFI16 Mediates Deacetylation of KSHV Chromatin via Interaction with NuRD and Sin3A Co-Repressor Complexes

doi: 10.3390/v17070921

Figure Lengend Snippet: Interaction of IFI16 with CHD4 and Sin3A. ( A ) Proximity ligation assay (PLA, red) was performed for CHD4, Sin3A, CoREST, and IgG with IFI16 in BCBL-1 cells. The red channel shows the PLA puncta. Also, IFA (green) for KSHV LANA was conducted in the same experiment. White arrowheads in the enlarged image point to the colocalization (yellow) between the PLA dots and KSHV LANA. ( B ) The quantification of the PLA dots is represented as PLA dots/cell in a swarm plot. Kruskal–Wallis test with Dunn’s multiple comparisons test was performed (BioRender.com). p < 0.05 (*), p < 0.0001 (****).

Article Snippet: The antibodies used for this study are: IFI16, anti-mouse (Santa Cruz Biotechnology, Dallas, TX, USA, SC-8023); IFI16, anti-rabbit (Millipore Sigma, HPA073514); KSHV LANA, anti-rabbit (In-house); HDAC1, anti-rabbit (Proteintech, Rosemont, IL, USA, 10197-1-AP); HDAC1, anti-goat (Origene, Rockville, MD, USA, TA348968); HDAC2, anti-rabbit (Proteintech, 12922-3-AP); CHD4, anti-rabbit (Cell Signaling, 12011); SIN3A, anti-rabbit (Cell Signaling, 8056); CoREST anti-rabbit (Cell Signaling, 14567); Histone H2A anti-rabbit (Cell Signaling, 12349); Acetyl-Histone H2A anti-rabbit (Cell Signaling, 2576); Histone H2B anti-rabbit (Cell Signaling 12364); Acetyl-Histone H2B anti-rabbit (Cell Signaling, 12799); Histone H3 anti-rabbit (Cell Signaling, 4499); Acetyl-Histone H3 anti-rabbit (Cell Signaling, 8173); Histone H4 anti-rabbit (Cell Signaling, 13919); Acetyl-Histone H4 anti-rabbit (Cell Signaling, 13534); anti-rabbit control IgG (Proteintech, 30000-0-AP); Anti-rabbit IgG Alexa Fluor 488 (Invitrogen, A-11008); Anti-mouse IgG Alexa Fluor 488 (Invitrogen, A-11001).

Techniques: Proximity Ligation Assay

IFI16’s role in the interaction between HDAC1 and the NuRD and Sin3A complexes. ( A ) IFI16 was knocked down in BCBL-1 using shIFI16 lentiviral transduction. Control (shC) and KD (shIFI16) cells were subjected to PLA (yellow) for CHD4 ( i ) and Sin3A ( ii ) with HDAC1. IFA (green) for IFI16 shows IFI16 KD efficiency. A swarm plot for the corresponding PLA panels represents the number of PLA dots/cell. ( B ) The recruitment of chromatin remodeling complexes, NuRD, Sin3A, and CoREST, to the ORF63 promoter was studied by ChIP using anti-Sin3A, anti-CHD4, and anti-CoREST antibodies, respectively. Error bars represent mean ± standard deviation (SDEV) from three independent biological replicates. Statistical significance was determined by unpaired two-tailed Student’s t -test; p < 0.001 (***), p < 0.0001 (****).

Journal: Viruses

Article Title: IFI16 Mediates Deacetylation of KSHV Chromatin via Interaction with NuRD and Sin3A Co-Repressor Complexes

doi: 10.3390/v17070921

Figure Lengend Snippet: IFI16’s role in the interaction between HDAC1 and the NuRD and Sin3A complexes. ( A ) IFI16 was knocked down in BCBL-1 using shIFI16 lentiviral transduction. Control (shC) and KD (shIFI16) cells were subjected to PLA (yellow) for CHD4 ( i ) and Sin3A ( ii ) with HDAC1. IFA (green) for IFI16 shows IFI16 KD efficiency. A swarm plot for the corresponding PLA panels represents the number of PLA dots/cell. ( B ) The recruitment of chromatin remodeling complexes, NuRD, Sin3A, and CoREST, to the ORF63 promoter was studied by ChIP using anti-Sin3A, anti-CHD4, and anti-CoREST antibodies, respectively. Error bars represent mean ± standard deviation (SDEV) from three independent biological replicates. Statistical significance was determined by unpaired two-tailed Student’s t -test; p < 0.001 (***), p < 0.0001 (****).

Article Snippet: The antibodies used for this study are: IFI16, anti-mouse (Santa Cruz Biotechnology, Dallas, TX, USA, SC-8023); IFI16, anti-rabbit (Millipore Sigma, HPA073514); KSHV LANA, anti-rabbit (In-house); HDAC1, anti-rabbit (Proteintech, Rosemont, IL, USA, 10197-1-AP); HDAC1, anti-goat (Origene, Rockville, MD, USA, TA348968); HDAC2, anti-rabbit (Proteintech, 12922-3-AP); CHD4, anti-rabbit (Cell Signaling, 12011); SIN3A, anti-rabbit (Cell Signaling, 8056); CoREST anti-rabbit (Cell Signaling, 14567); Histone H2A anti-rabbit (Cell Signaling, 12349); Acetyl-Histone H2A anti-rabbit (Cell Signaling, 2576); Histone H2B anti-rabbit (Cell Signaling 12364); Acetyl-Histone H2B anti-rabbit (Cell Signaling, 12799); Histone H3 anti-rabbit (Cell Signaling, 4499); Acetyl-Histone H3 anti-rabbit (Cell Signaling, 8173); Histone H4 anti-rabbit (Cell Signaling, 13919); Acetyl-Histone H4 anti-rabbit (Cell Signaling, 13534); anti-rabbit control IgG (Proteintech, 30000-0-AP); Anti-rabbit IgG Alexa Fluor 488 (Invitrogen, A-11008); Anti-mouse IgG Alexa Fluor 488 (Invitrogen, A-11001).

Techniques: Transduction, Control, Standard Deviation, Two Tailed Test