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anti nf κb p65 antibody  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology anti nf κb p65 antibody
    HDAC5 deacetylates NFκB <t>p65</t> and indirectly regulates NLRP3 expression. (A) BV2 cells were transfected with lentivirus for 48 h and then harvested for Co‐IP assay. (B) Molecular docking analysis predicting the interaction between HDAC5 <t>and</t> <t>NF‐κB</t> p65. The enlarged inset shows the predicted potential binding site. (C) Co‐IP assay showing the interaction between HDAC5 and NF‐κB p65 in BV2 cells. (D) Western blot assay to detect the expression of acetylated proteins after Hdac5 KD. (E) Hdac5 KD in BV2 cells and subsequent Co‐IP assay. (F) Western blot assay to detect NFκB p65 protein expression in cytoplasm and nucleus after Hdac5 KD. (G, H) Quantitative analysis of NFκB p65 protein form (D) ( n = 4). (I) Schematic of the predicted NFκB p65 (Rela) binding site in the promoter of NLRP3. All quantitative data are expressed as mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001 by one‐way ANOVA.
    Anti Nf κb P65 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 14463 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/nf+%CE%BAb+p65/NF%CE%BAB+p65+Antibody/pmc13624526-105-19-22
    Average 96 stars, based on 14463 article reviews
    anti nf κb p65 antibody - by Bioz Stars, 2026-10
    96/100 stars

    Images

    1) Product Images from "Targeting Microglial HDAC5 Suppresses NLRP3 Inflammation via NF ‐ κB Deacetylation to Alleviate Ischemic Brain Injury"

    Article Title: Targeting Microglial HDAC5 Suppresses NLRP3 Inflammation via NF ‐ κB Deacetylation to Alleviate Ischemic Brain Injury

    Journal: CNS Neuroscience & Therapeutics

    doi: 10.1002/cns.71161

    HDAC5 deacetylates NFκB p65 and indirectly regulates NLRP3 expression. (A) BV2 cells were transfected with lentivirus for 48 h and then harvested for Co‐IP assay. (B) Molecular docking analysis predicting the interaction between HDAC5 and NF‐κB p65. The enlarged inset shows the predicted potential binding site. (C) Co‐IP assay showing the interaction between HDAC5 and NF‐κB p65 in BV2 cells. (D) Western blot assay to detect the expression of acetylated proteins after Hdac5 KD. (E) Hdac5 KD in BV2 cells and subsequent Co‐IP assay. (F) Western blot assay to detect NFκB p65 protein expression in cytoplasm and nucleus after Hdac5 KD. (G, H) Quantitative analysis of NFκB p65 protein form (D) ( n = 4). (I) Schematic of the predicted NFκB p65 (Rela) binding site in the promoter of NLRP3. All quantitative data are expressed as mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001 by one‐way ANOVA.
    Figure Legend Snippet: HDAC5 deacetylates NFκB p65 and indirectly regulates NLRP3 expression. (A) BV2 cells were transfected with lentivirus for 48 h and then harvested for Co‐IP assay. (B) Molecular docking analysis predicting the interaction between HDAC5 and NF‐κB p65. The enlarged inset shows the predicted potential binding site. (C) Co‐IP assay showing the interaction between HDAC5 and NF‐κB p65 in BV2 cells. (D) Western blot assay to detect the expression of acetylated proteins after Hdac5 KD. (E) Hdac5 KD in BV2 cells and subsequent Co‐IP assay. (F) Western blot assay to detect NFκB p65 protein expression in cytoplasm and nucleus after Hdac5 KD. (G, H) Quantitative analysis of NFκB p65 protein form (D) ( n = 4). (I) Schematic of the predicted NFκB p65 (Rela) binding site in the promoter of NLRP3. All quantitative data are expressed as mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001 by one‐way ANOVA.

    Techniques Used: Expressing, Transfection, Co-Immunoprecipitation Assay, Docking Assay, Analysis, Binding Assay, Western Blot

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    Incubation:

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    Proteintech p65
    HDAC5 deacetylates NFκB <t>p65</t> and indirectly regulates NLRP3 expression. (A) BV2 cells were transfected with lentivirus for 48 h and then harvested for Co‐IP assay. (B) Molecular docking analysis predicting the interaction between HDAC5 <t>and</t> <t>NF‐κB</t> p65. The enlarged inset shows the predicted potential binding site. (C) Co‐IP assay showing the interaction between HDAC5 and NF‐κB p65 in BV2 cells. (D) Western blot assay to detect the expression of acetylated proteins after Hdac5 KD. (E) Hdac5 KD in BV2 cells and subsequent Co‐IP assay. (F) Western blot assay to detect NFκB p65 protein expression in cytoplasm and nucleus after Hdac5 KD. (G, H) Quantitative analysis of NFκB p65 protein form (D) ( n = 4). (I) Schematic of the predicted NFκB p65 (Rela) binding site in the promoter of NLRP3. All quantitative data are expressed as mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001 by one‐way ANOVA.
    P65, 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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    anti nf κb p65  (Boster Bio)
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    HDAC5 deacetylates NFκB <t>p65</t> and indirectly regulates NLRP3 expression. (A) BV2 cells were transfected with lentivirus for 48 h and then harvested for Co‐IP assay. (B) Molecular docking analysis predicting the interaction between HDAC5 <t>and</t> <t>NF‐κB</t> p65. The enlarged inset shows the predicted potential binding site. (C) Co‐IP assay showing the interaction between HDAC5 and NF‐κB p65 in BV2 cells. (D) Western blot assay to detect the expression of acetylated proteins after Hdac5 KD. (E) Hdac5 KD in BV2 cells and subsequent Co‐IP assay. (F) Western blot assay to detect NFκB p65 protein expression in cytoplasm and nucleus after Hdac5 KD. (G, H) Quantitative analysis of NFκB p65 protein form (D) ( n = 4). (I) Schematic of the predicted NFκB p65 (Rela) binding site in the promoter of NLRP3. All quantitative data are expressed as mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001 by one‐way ANOVA.
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    anti nf κb p65  (Santa Cruz Biotechnology)
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    HDAC5 deacetylates NFκB <t>p65</t> and indirectly regulates NLRP3 expression. (A) BV2 cells were transfected with lentivirus for 48 h and then harvested for Co‐IP assay. (B) Molecular docking analysis predicting the interaction between HDAC5 <t>and</t> <t>NF‐κB</t> p65. The enlarged inset shows the predicted potential binding site. (C) Co‐IP assay showing the interaction between HDAC5 and NF‐κB p65 in BV2 cells. (D) Western blot assay to detect the expression of acetylated proteins after Hdac5 KD. (E) Hdac5 KD in BV2 cells and subsequent Co‐IP assay. (F) Western blot assay to detect NFκB p65 protein expression in cytoplasm and nucleus after Hdac5 KD. (G, H) Quantitative analysis of NFκB p65 protein form (D) ( n = 4). (I) Schematic of the predicted NFκB p65 (Rela) binding site in the promoter of NLRP3. All quantitative data are expressed as mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001 by one‐way ANOVA.
    Anti Nf κb P65, 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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    Image Search Results


    Journal: iScience

    Article Title: M2 type tumor-associated macrophage-derived CCL-18 promotes glioma cell proliferation but does not mediates glioma recurrence after radiotherapy

    doi: 10.1016/j.isci.2026.117695

    Figure Lengend Snippet:

    Article Snippet: Anti-p65 rabbit antibody , Proteintech , 10745-1-AP; RRID: AB_2178878.

    Techniques: Cell-Signaling, Virus, Tissue, Microarray, Recombinant, cDNA Synthesis, Enzyme-linked Immunosorbent Assay, Software, Biomarker Discovery, In Vivo Imaging

    (A) RNA antisense purification–mass spectrometry experimental outline. (B) RT-qPCR analysis of GRAS1, U1 snRNA, and GAPDH mRNA in nuclear and cytoplasmic fractionations of A549 cells (left panel). Immunoblot of Lamin A/C as a marker for nuclear fraction, and GAPDH as a marker for cytoplasmic fraction (right panel); N = 3. (C) Validation of GRAS1 RNA capture and recovery by biotinylated antisense oligonucleotide probes against GRAS1. RT-qPCR analysis of GRAS1 RNA and TUBB control mRNA in three fractions, including input with probes added, unbound sample flowthrough, and elution; N = 3. (D) Total proteins identified in RAP-MS of GRAS1 RNA, U1 snRNA positive control, and luciferase mRNA negative control elution samples. (E) GRAS1 interactome proteins identified by RAP-MS, with at least two unique peptides, after excluding proteins that were also found in U1 and luciferase control captures (left panel). The top 10 GRAS1-interacting proteins and their molecular weights (right panel). (F) GRAS1 RNA enrichment measured by RT-qPCR after immunoprecipitation of NKAP in A549 cells, compared with immunoprecipitation with IgG control antibody; N = 3. (G) Immunoblot of NKAP and p65 in A549 cells treated with control GapmeR compared with GRAS1 GapmeR1 or GRAS1 GapmeR2. (H) Quantification of immunoblot (G). NKAP and p65 expression were calculated after normalization to the GAPDH loading control for each sample; N = 3. (I) RT-qPCR analysis of GCLC, ANGPT1, BDKRB1, and NR3C1 expression levels in A549 cells treated with control GapmeR compared with GRAS1 GapmeR1 or GRAS1 GapmeR2, normalized to GAPDH control mRNA; N = 3. (J) RT-qPCR analysis of NKAP mRNA expression in A549 cells treated with control GapmeR compared with GRAS1 GapmeR1 or GRAS1 GapmeR2, normalized to GAPDH control mRNA; N = 3. (K) Immunoblot of NKAP and p65 in A549 cells treated with control GapmeR compared with GRAS1 GapmeR1 or GRAS1 GapmeR2, with 5 μM MG-132 treatment. (L) Quantification of immunoblot (K). NKAP and p65 expression were calculated after normalization to GAPDH loading control for each sample; N = 6. Error bars represent SD in all panels; (ns) P > 0.05; (***) P < 0.001 by two-tailed t test.

    Journal: Life Science Alliance

    Article Title: The noncoding RNA GRAS1 interacts with NKAP and protects against DNA damage and cell death

    doi: 10.26508/lsa.202403105

    Figure Lengend Snippet: (A) RNA antisense purification–mass spectrometry experimental outline. (B) RT-qPCR analysis of GRAS1, U1 snRNA, and GAPDH mRNA in nuclear and cytoplasmic fractionations of A549 cells (left panel). Immunoblot of Lamin A/C as a marker for nuclear fraction, and GAPDH as a marker for cytoplasmic fraction (right panel); N = 3. (C) Validation of GRAS1 RNA capture and recovery by biotinylated antisense oligonucleotide probes against GRAS1. RT-qPCR analysis of GRAS1 RNA and TUBB control mRNA in three fractions, including input with probes added, unbound sample flowthrough, and elution; N = 3. (D) Total proteins identified in RAP-MS of GRAS1 RNA, U1 snRNA positive control, and luciferase mRNA negative control elution samples. (E) GRAS1 interactome proteins identified by RAP-MS, with at least two unique peptides, after excluding proteins that were also found in U1 and luciferase control captures (left panel). The top 10 GRAS1-interacting proteins and their molecular weights (right panel). (F) GRAS1 RNA enrichment measured by RT-qPCR after immunoprecipitation of NKAP in A549 cells, compared with immunoprecipitation with IgG control antibody; N = 3. (G) Immunoblot of NKAP and p65 in A549 cells treated with control GapmeR compared with GRAS1 GapmeR1 or GRAS1 GapmeR2. (H) Quantification of immunoblot (G). NKAP and p65 expression were calculated after normalization to the GAPDH loading control for each sample; N = 3. (I) RT-qPCR analysis of GCLC, ANGPT1, BDKRB1, and NR3C1 expression levels in A549 cells treated with control GapmeR compared with GRAS1 GapmeR1 or GRAS1 GapmeR2, normalized to GAPDH control mRNA; N = 3. (J) RT-qPCR analysis of NKAP mRNA expression in A549 cells treated with control GapmeR compared with GRAS1 GapmeR1 or GRAS1 GapmeR2, normalized to GAPDH control mRNA; N = 3. (K) Immunoblot of NKAP and p65 in A549 cells treated with control GapmeR compared with GRAS1 GapmeR1 or GRAS1 GapmeR2, with 5 μM MG-132 treatment. (L) Quantification of immunoblot (K). NKAP and p65 expression were calculated after normalization to GAPDH loading control for each sample; N = 6. Error bars represent SD in all panels; (ns) P > 0.05; (***) P < 0.001 by two-tailed t test.

    Article Snippet: The following primary antibodies were used: NKAP polyclonal antibody (ab229096; Abcam, 1:1,000 dilution), phospho-histone (γ) H2A.X Ser139 20E3 (60566SF; Cell Signaling Technology, 1:1,000 dilution), p53 (10442-1-AP; Proteintech, 1:1,000 dilution), GAPDH (60004-1-Ig; Proteintech, 1:3,000 dilution), Lamin A/C (10298-1-AP; Proteintech, 1:1,000 dilution), NF-κB p65 (10745-1-AP; Proteintech, 1:1,000 dilution), and TIGA1 (MBS9610109; MyBioSource, 1:1,000 dilution).

    Techniques: Purification, Mass Spectrometry, Quantitative RT-PCR, Analysis, Western Blot, Marker, Biomarker Discovery, Control, Positive Control, Luciferase, Negative Control, Immunoprecipitation, Expressing, Two Tailed Test

    HDAC5 deacetylates NFκB p65 and indirectly regulates NLRP3 expression. (A) BV2 cells were transfected with lentivirus for 48 h and then harvested for Co‐IP assay. (B) Molecular docking analysis predicting the interaction between HDAC5 and NF‐κB p65. The enlarged inset shows the predicted potential binding site. (C) Co‐IP assay showing the interaction between HDAC5 and NF‐κB p65 in BV2 cells. (D) Western blot assay to detect the expression of acetylated proteins after Hdac5 KD. (E) Hdac5 KD in BV2 cells and subsequent Co‐IP assay. (F) Western blot assay to detect NFκB p65 protein expression in cytoplasm and nucleus after Hdac5 KD. (G, H) Quantitative analysis of NFκB p65 protein form (D) ( n = 4). (I) Schematic of the predicted NFκB p65 (Rela) binding site in the promoter of NLRP3. All quantitative data are expressed as mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001 by one‐way ANOVA.

    Journal: CNS Neuroscience & Therapeutics

    Article Title: Targeting Microglial HDAC5 Suppresses NLRP3 Inflammation via NF ‐ κB Deacetylation to Alleviate Ischemic Brain Injury

    doi: 10.1002/cns.71161

    Figure Lengend Snippet: HDAC5 deacetylates NFκB p65 and indirectly regulates NLRP3 expression. (A) BV2 cells were transfected with lentivirus for 48 h and then harvested for Co‐IP assay. (B) Molecular docking analysis predicting the interaction between HDAC5 and NF‐κB p65. The enlarged inset shows the predicted potential binding site. (C) Co‐IP assay showing the interaction between HDAC5 and NF‐κB p65 in BV2 cells. (D) Western blot assay to detect the expression of acetylated proteins after Hdac5 KD. (E) Hdac5 KD in BV2 cells and subsequent Co‐IP assay. (F) Western blot assay to detect NFκB p65 protein expression in cytoplasm and nucleus after Hdac5 KD. (G, H) Quantitative analysis of NFκB p65 protein form (D) ( n = 4). (I) Schematic of the predicted NFκB p65 (Rela) binding site in the promoter of NLRP3. All quantitative data are expressed as mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001 by one‐way ANOVA.

    Article Snippet: Equal amounts of protein were incubated overnight at 4°C with anti‐HDAC5 antibody (Santa Cruz), anti‐acetylated‐lysine antibody (Cell Signaling Technology), anti‐NF‐κB p65 antibody (Santa Cruz), or the corresponding species‐matched IgG as a negative control.

    Techniques: Expressing, Transfection, Co-Immunoprecipitation Assay, Docking Assay, Analysis, Binding Assay, Western Blot