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goat anti mouse immunoglobulin g igg  (Santa Cruz Biotechnology)


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    Structured Review

    Santa Cruz Biotechnology goat anti mouse immunoglobulin g igg
    Goat Anti Mouse Immunoglobulin G Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 487 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/normal+immunoglobulin+g/normal+mouse+IgG-HRP/pmc12929413-50-4-20
    Average 96 stars, based on 487 article reviews
    goat anti mouse immunoglobulin g igg - by Bioz Stars, 2026-09
    96/100 stars

    Images

    Related Articles

    Immunoprecipitation:

    Article Title: Telomere elongation by a mutant tankyrase 1 without TRF1 poly(ADP-ribosyl)ation.
    Article Snippet: Yukiko Muramatsu, Hidetoshi Tahara, Taeko Ono, Takashi Tsuruo, Hiroyuki Seimiya⁎ Division of Molecular Biotherapy, Cancer Chemotherapy Center, Japanese Foundation for Cancer Research, Tokyo 135-8550, Japan Department of Cellular and Molecular Biology, Division of Integrated Medical Science, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima 734-8551, Japan Director's Room, Cancer Chemotherapy Center, Japanese Foundation for Cancer Research, Tokyo 135-8550, Japan

    Article Title: Epigenetic therapy combination of UNC0638 and CI-994 suppresses breast cancer via epigenetic remodeling of BIRC5 and GADD45A.
    Article Snippet: Briefly, UNC0638 (4 μM) and CI-994 (10 μM)-treated cells were fixed (1% formaldehyde, 10 min), neutralized (1× glycine, 5 min), and then sonicated using Q700 sonicator (Qsonica, Newtown, CT, USA). .. Immunoprecipitation was carried out using anti-RNA polymerase II antibody (sc-899X, Santa Cruz, Santa Cruz, CA, USA), H3ac (06–599, Millipore), H3K4me3 (07–442, Millipore), or normal immunoglobulin G (sc-2025, Santa Cruz, negative control) together with fragmented chromatin (5 μg) at 4 ◦C, overnight, and then the immunoprecipitated DNA was purified for qPCR. ..

    Negative Control:

    Article Title: Epigenetic therapy combination of UNC0638 and CI-994 suppresses breast cancer via epigenetic remodeling of BIRC5 and GADD45A.
    Article Snippet: Briefly, UNC0638 (4 μM) and CI-994 (10 μM)-treated cells were fixed (1% formaldehyde, 10 min), neutralized (1× glycine, 5 min), and then sonicated using Q700 sonicator (Qsonica, Newtown, CT, USA). .. Immunoprecipitation was carried out using anti-RNA polymerase II antibody (sc-899X, Santa Cruz, Santa Cruz, CA, USA), H3ac (06–599, Millipore), H3K4me3 (07–442, Millipore), or normal immunoglobulin G (sc-2025, Santa Cruz, negative control) together with fragmented chromatin (5 μg) at 4 ◦C, overnight, and then the immunoprecipitated DNA was purified for qPCR. ..

    Article Title: MicroRNA-26b functions as a proapoptotic factor in porcine follicular Granulosa cells by targeting Sma-and Mad-related protein 4.
    Article Snippet: The nuclei were counterstained with hematoxylin (Sigma). .. Staining with normal immunoglobulin G (Santa Cruz) was performed as negative control (NC). ..

    Purification:

    Article Title: Epigenetic therapy combination of UNC0638 and CI-994 suppresses breast cancer via epigenetic remodeling of BIRC5 and GADD45A.
    Article Snippet: Briefly, UNC0638 (4 μM) and CI-994 (10 μM)-treated cells were fixed (1% formaldehyde, 10 min), neutralized (1× glycine, 5 min), and then sonicated using Q700 sonicator (Qsonica, Newtown, CT, USA). .. Immunoprecipitation was carried out using anti-RNA polymerase II antibody (sc-899X, Santa Cruz, Santa Cruz, CA, USA), H3ac (06–599, Millipore), H3K4me3 (07–442, Millipore), or normal immunoglobulin G (sc-2025, Santa Cruz, negative control) together with fragmented chromatin (5 μg) at 4 ◦C, overnight, and then the immunoprecipitated DNA was purified for qPCR. ..

    Real-time Polymerase Chain Reaction:

    Article Title: Epigenetic therapy combination of UNC0638 and CI-994 suppresses breast cancer via epigenetic remodeling of BIRC5 and GADD45A.
    Article Snippet: Briefly, UNC0638 (4 μM) and CI-994 (10 μM)-treated cells were fixed (1% formaldehyde, 10 min), neutralized (1× glycine, 5 min), and then sonicated using Q700 sonicator (Qsonica, Newtown, CT, USA). .. Immunoprecipitation was carried out using anti-RNA polymerase II antibody (sc-899X, Santa Cruz, Santa Cruz, CA, USA), H3ac (06–599, Millipore), H3K4me3 (07–442, Millipore), or normal immunoglobulin G (sc-2025, Santa Cruz, negative control) together with fragmented chromatin (5 μg) at 4 ◦C, overnight, and then the immunoprecipitated DNA was purified for qPCR. ..

    Staining:

    Article Title: MicroRNA-26b functions as a proapoptotic factor in porcine follicular Granulosa cells by targeting Sma-and Mad-related protein 4.
    Article Snippet: The nuclei were counterstained with hematoxylin (Sigma). .. Staining with normal immunoglobulin G (Santa Cruz) was performed as negative control (NC). ..

    Chromatin Immunoprecipitation:

    Article Title: A stem cell differentiation model reveals two alternative fates in CBFA2T3::GLIS2-driven acute megakaryoblastic leukemia initiation
    Article Snippet: CD34 – Allophycocyanin , Mouse , BD Biosciences , 345804 , IF: 1:500 FC 1:500 , AB2686894. .. normal immunoglobulin G , Mouse , Santa Cruz Biotech , sc-2025 , ChIP , AB737182. .. CBFA2T3 , Rabbit , Abclonal , A14712 , ChIP; WB 1:1000 , AB2761588.



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    ( A ) Western blot analysis and Co-IP assay showing the Drp1 and Filamin/Kinesin binding ability of the myocardial tissue after CLP; n = 8 per group. ( B ) Functional pattern of the full-length domain of Drp1 protein. ( C and D ) Schematic diagram of the docking of Filamin and Kinesin with Drp1. ( E ) Immunofluorescence images showing the expression and distribution of Drp1 (green) and Filamin/Kinesin (red) in cardiomyocytes cocultured with endothelial cells from control and LPS-treated groups; n = 3 per group. Scale bars, 25 μm. ( F ) Immunofluorescence images showing the expression of Filamin/Kinesin (red) in cardiomyocytes cocultured with fibroblasts or macrophages; n = 3 per group. Scale bars, 25 μm. ( G and H ) Time-lapse recordings of mitochondrial transfer via TNT between WT and Drp1 eCKO primary cardiomyocytes and primary endothelial cells, fibroblasts, and macrophages by HIS-SIM. Mitochondria were labeled with PKmito (yellow); TNTs were labeled with tubulin (green) and actin (cyan); n = 3 per group. Scale bars, 10 μm. IgG, immunoglobulin G; GTPase, guanosine triphosphatase; aa, amino acids.
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    Identification of GATA2 binding sites in gene promoters through chromatin immunoprecipitation sequencing and prediction of its regulatory functions. A: Scatter plot showing the correlation between biological replicates; B: Histogram depicting the distribution of peak lengths; C: Distribution of peaks across chromosomes (X-axis: Chromosome length; left Y-axis: Peak intensity; right Y-axis: Chromosome numbers); D: Read distribution surrounding transcription start sites (TSS) of peak-associated genes (top: Line chart of average sequencing depth around TSS; bottom: Heatmap of sequencing depth around TSS for peak-associated genes, ranked by average depth); E: Gene Ontology functional enrichment analysis of peak-associated genes; F: Kyoto Encyclopedia of Genes and Genomes pathway enrichment analysis of peak-associated genes; G: Fold enrichment of selected genes associated with partial regeneration, molecular chaperones, antioxidant response, and fatty acid β-oxidation as determined by chromatin immunoprecipitation sequencing; H: Validation of GATA2 binding to the promoters of heat shock protein family D member 1, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha by chromatin immunoprecipitation real-time quantitative polymerase chain reaction. Data are presented as fold enrichment relative to immunoglobulin G; I: Western blot analysis of GATA2, heat shock protein 60, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha protein expression following transfection with the Gata2 construct. b P < 0.01 vs <t>immunoglobulin</t> <t>G</t> or control group. ChIP-seq: Chromatin immunoprecipitation sequencing; IgG: Immunoglobulin G; PCNA: Proliferating cell nuclear antigen; HSPD1: Heat shock protein family D member 1; GPX4: Glutathione peroxidase 4; UCP2: Uncoupling protein 2; PPARA: Peroxisome proliferator-activated receptor alpha.
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    Identification of GATA2 binding sites in gene promoters through chromatin immunoprecipitation sequencing and prediction of its regulatory functions. A: Scatter plot showing the correlation between biological replicates; B: Histogram depicting the distribution of peak lengths; C: Distribution of peaks across chromosomes (X-axis: Chromosome length; left Y-axis: Peak intensity; right Y-axis: Chromosome numbers); D: Read distribution surrounding transcription start sites (TSS) of peak-associated genes (top: Line chart of average sequencing depth around TSS; bottom: Heatmap of sequencing depth around TSS for peak-associated genes, ranked by average depth); E: Gene Ontology functional enrichment analysis of peak-associated genes; F: Kyoto Encyclopedia of Genes and Genomes pathway enrichment analysis of peak-associated genes; G: Fold enrichment of selected genes associated with partial regeneration, molecular chaperones, antioxidant response, and fatty acid β-oxidation as determined by chromatin immunoprecipitation sequencing; H: Validation of GATA2 binding to the promoters of heat shock protein family D member 1, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha by chromatin immunoprecipitation real-time quantitative polymerase chain reaction. Data are presented as fold enrichment relative to immunoglobulin G; I: Western blot analysis of GATA2, heat shock protein 60, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha protein expression following transfection with the Gata2 construct. b P < 0.01 vs <t>immunoglobulin</t> <t>G</t> or control group. ChIP-seq: Chromatin immunoprecipitation sequencing; IgG: Immunoglobulin G; PCNA: Proliferating cell nuclear antigen; HSPD1: Heat shock protein family D member 1; GPX4: Glutathione peroxidase 4; UCP2: Uncoupling protein 2; PPARA: Peroxisome proliferator-activated receptor alpha.
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    Identification of GATA2 binding sites in gene promoters through chromatin immunoprecipitation sequencing and prediction of its regulatory functions. A: Scatter plot showing the correlation between biological replicates; B: Histogram depicting the distribution of peak lengths; C: Distribution of peaks across chromosomes (X-axis: Chromosome length; left Y-axis: Peak intensity; right Y-axis: Chromosome numbers); D: Read distribution surrounding transcription start sites (TSS) of peak-associated genes (top: Line chart of average sequencing depth around TSS; bottom: Heatmap of sequencing depth around TSS for peak-associated genes, ranked by average depth); E: Gene Ontology functional enrichment analysis of peak-associated genes; F: Kyoto Encyclopedia of Genes and Genomes pathway enrichment analysis of peak-associated genes; G: Fold enrichment of selected genes associated with partial regeneration, molecular chaperones, antioxidant response, and fatty acid β-oxidation as determined by chromatin immunoprecipitation sequencing; H: Validation of GATA2 binding to the promoters of heat shock protein family D member 1, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha by chromatin immunoprecipitation real-time quantitative polymerase chain reaction. Data are presented as fold enrichment relative to immunoglobulin G; I: Western blot analysis of GATA2, heat shock protein 60, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha protein expression following transfection with the Gata2 construct. b P < 0.01 vs <t>immunoglobulin</t> <t>G</t> or control group. ChIP-seq: Chromatin immunoprecipitation sequencing; IgG: Immunoglobulin G; PCNA: Proliferating cell nuclear antigen; HSPD1: Heat shock protein family D member 1; GPX4: Glutathione peroxidase 4; UCP2: Uncoupling protein 2; PPARA: Peroxisome proliferator-activated receptor alpha.
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    Identification of GATA2 binding sites in gene promoters through chromatin immunoprecipitation sequencing and prediction of its regulatory functions. A: Scatter plot showing the correlation between biological replicates; B: Histogram depicting the distribution of peak lengths; C: Distribution of peaks across chromosomes (X-axis: Chromosome length; left Y-axis: Peak intensity; right Y-axis: Chromosome numbers); D: Read distribution surrounding transcription start sites (TSS) of peak-associated genes (top: Line chart of average sequencing depth around TSS; bottom: Heatmap of sequencing depth around TSS for peak-associated genes, ranked by average depth); E: Gene Ontology functional enrichment analysis of peak-associated genes; F: Kyoto Encyclopedia of Genes and Genomes pathway enrichment analysis of peak-associated genes; G: Fold enrichment of selected genes associated with partial regeneration, molecular chaperones, antioxidant response, and fatty acid β-oxidation as determined by chromatin immunoprecipitation sequencing; H: Validation of GATA2 binding to the promoters of heat shock protein family D member 1, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha by chromatin immunoprecipitation real-time quantitative polymerase chain reaction. Data are presented as fold enrichment relative to immunoglobulin G; I: Western blot analysis of GATA2, heat shock protein 60, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha protein expression following transfection with the Gata2 construct. b P < 0.01 vs <t>immunoglobulin</t> <t>G</t> or control group. ChIP-seq: Chromatin immunoprecipitation sequencing; IgG: Immunoglobulin G; PCNA: Proliferating cell nuclear antigen; HSPD1: Heat shock protein family D member 1; GPX4: Glutathione peroxidase 4; UCP2: Uncoupling protein 2; PPARA: Peroxisome proliferator-activated receptor alpha.
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    Image Search Results


    ( A ) Western blot analysis and Co-IP assay showing the Drp1 and Filamin/Kinesin binding ability of the myocardial tissue after CLP; n = 8 per group. ( B ) Functional pattern of the full-length domain of Drp1 protein. ( C and D ) Schematic diagram of the docking of Filamin and Kinesin with Drp1. ( E ) Immunofluorescence images showing the expression and distribution of Drp1 (green) and Filamin/Kinesin (red) in cardiomyocytes cocultured with endothelial cells from control and LPS-treated groups; n = 3 per group. Scale bars, 25 μm. ( F ) Immunofluorescence images showing the expression of Filamin/Kinesin (red) in cardiomyocytes cocultured with fibroblasts or macrophages; n = 3 per group. Scale bars, 25 μm. ( G and H ) Time-lapse recordings of mitochondrial transfer via TNT between WT and Drp1 eCKO primary cardiomyocytes and primary endothelial cells, fibroblasts, and macrophages by HIS-SIM. Mitochondria were labeled with PKmito (yellow); TNTs were labeled with tubulin (green) and actin (cyan); n = 3 per group. Scale bars, 10 μm. IgG, immunoglobulin G; GTPase, guanosine triphosphatase; aa, amino acids.

    Journal: Science Advances

    Article Title: Cytoskeletal remodeling promotes tunneling nanotube formation and drives cardiac resident cell mitochondrial transfer in sepsis

    doi: 10.1126/sciadv.adz3266

    Figure Lengend Snippet: ( A ) Western blot analysis and Co-IP assay showing the Drp1 and Filamin/Kinesin binding ability of the myocardial tissue after CLP; n = 8 per group. ( B ) Functional pattern of the full-length domain of Drp1 protein. ( C and D ) Schematic diagram of the docking of Filamin and Kinesin with Drp1. ( E ) Immunofluorescence images showing the expression and distribution of Drp1 (green) and Filamin/Kinesin (red) in cardiomyocytes cocultured with endothelial cells from control and LPS-treated groups; n = 3 per group. Scale bars, 25 μm. ( F ) Immunofluorescence images showing the expression of Filamin/Kinesin (red) in cardiomyocytes cocultured with fibroblasts or macrophages; n = 3 per group. Scale bars, 25 μm. ( G and H ) Time-lapse recordings of mitochondrial transfer via TNT between WT and Drp1 eCKO primary cardiomyocytes and primary endothelial cells, fibroblasts, and macrophages by HIS-SIM. Mitochondria were labeled with PKmito (yellow); TNTs were labeled with tubulin (green) and actin (cyan); n = 3 per group. Scale bars, 10 μm. IgG, immunoglobulin G; GTPase, guanosine triphosphatase; aa, amino acids.

    Article Snippet: Equal lysate amounts were incubated overnight with Drp1 antibody (1:50; Novus Biologicals, NB110-55288) or immunoglobulin G (1:50; Cell Signaling, #2729) at 4°C, followed by incubation with protein A/G magnetic beads (MedChemExpress, HY-K0202) for 6 hours.

    Techniques: Western Blot, Co-Immunoprecipitation Assay, Binding Assay, Functional Assay, Immunofluorescence, Expressing, Control, Labeling

    Identification of GATA2 binding sites in gene promoters through chromatin immunoprecipitation sequencing and prediction of its regulatory functions. A: Scatter plot showing the correlation between biological replicates; B: Histogram depicting the distribution of peak lengths; C: Distribution of peaks across chromosomes (X-axis: Chromosome length; left Y-axis: Peak intensity; right Y-axis: Chromosome numbers); D: Read distribution surrounding transcription start sites (TSS) of peak-associated genes (top: Line chart of average sequencing depth around TSS; bottom: Heatmap of sequencing depth around TSS for peak-associated genes, ranked by average depth); E: Gene Ontology functional enrichment analysis of peak-associated genes; F: Kyoto Encyclopedia of Genes and Genomes pathway enrichment analysis of peak-associated genes; G: Fold enrichment of selected genes associated with partial regeneration, molecular chaperones, antioxidant response, and fatty acid β-oxidation as determined by chromatin immunoprecipitation sequencing; H: Validation of GATA2 binding to the promoters of heat shock protein family D member 1, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha by chromatin immunoprecipitation real-time quantitative polymerase chain reaction. Data are presented as fold enrichment relative to immunoglobulin G; I: Western blot analysis of GATA2, heat shock protein 60, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha protein expression following transfection with the Gata2 construct. b P < 0.01 vs immunoglobulin G or control group. ChIP-seq: Chromatin immunoprecipitation sequencing; IgG: Immunoglobulin G; PCNA: Proliferating cell nuclear antigen; HSPD1: Heat shock protein family D member 1; GPX4: Glutathione peroxidase 4; UCP2: Uncoupling protein 2; PPARA: Peroxisome proliferator-activated receptor alpha.

    Journal: World Journal of Stem Cells

    Article Title: GATA2 deficiency exacerbates chronic liver injury via disrupting hepatocyte death-regeneration balance: Clinical, histopathological, and molecular evidence

    doi: 10.4252/wjsc.v18.i2.112940

    Figure Lengend Snippet: Identification of GATA2 binding sites in gene promoters through chromatin immunoprecipitation sequencing and prediction of its regulatory functions. A: Scatter plot showing the correlation between biological replicates; B: Histogram depicting the distribution of peak lengths; C: Distribution of peaks across chromosomes (X-axis: Chromosome length; left Y-axis: Peak intensity; right Y-axis: Chromosome numbers); D: Read distribution surrounding transcription start sites (TSS) of peak-associated genes (top: Line chart of average sequencing depth around TSS; bottom: Heatmap of sequencing depth around TSS for peak-associated genes, ranked by average depth); E: Gene Ontology functional enrichment analysis of peak-associated genes; F: Kyoto Encyclopedia of Genes and Genomes pathway enrichment analysis of peak-associated genes; G: Fold enrichment of selected genes associated with partial regeneration, molecular chaperones, antioxidant response, and fatty acid β-oxidation as determined by chromatin immunoprecipitation sequencing; H: Validation of GATA2 binding to the promoters of heat shock protein family D member 1, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha by chromatin immunoprecipitation real-time quantitative polymerase chain reaction. Data are presented as fold enrichment relative to immunoglobulin G; I: Western blot analysis of GATA2, heat shock protein 60, glutathione peroxidase 4, and peroxisome proliferator-activated receptor alpha protein expression following transfection with the Gata2 construct. b P < 0.01 vs immunoglobulin G or control group. ChIP-seq: Chromatin immunoprecipitation sequencing; IgG: Immunoglobulin G; PCNA: Proliferating cell nuclear antigen; HSPD1: Heat shock protein family D member 1; GPX4: Glutathione peroxidase 4; UCP2: Uncoupling protein 2; PPARA: Peroxisome proliferator-activated receptor alpha.

    Article Snippet: An additional 10% was incubated with rabbit immunoglobulin G (IgG) (Cell Signaling Technology, Cat# 2729, Danvers, MA, United States) as a negative control and labeled as “IgG”.

    Techniques: Binding Assay, ChIP-sequencing, Sequencing, Functional Assay, Biomarker Discovery, Chromatin Immunoprecipitation, Real-time Polymerase Chain Reaction, Western Blot, Expressing, Transfection, Construct, Control