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p p65 rabbit ab  (Bioss)


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    Structured Review

    Bioss p p65 rabbit ab
    The mRNA expression of ITGAV, FAK, PLC, PKC, <t>p65,</t> ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.
    P P65 Rabbit Ab, supplied by Bioss, used in various techniques. Bioz Stars score: 95/100, based on 144 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+antibody+p+p65/pmc13125192-134-0-4?v=Bioss
    Average 95 stars, based on 144 article reviews
    p p65 rabbit ab - by Bioz Stars, 2026-08
    95/100 stars

    Images

    1) Product Images from "Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor"

    Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

    Journal: Poultry Science

    doi: 10.1016/j.psj.2026.106922

    The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.
    Figure Legend Snippet: The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.

    Techniques Used: Expressing

    The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.
    Figure Legend Snippet: The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.

    Techniques Used: Activity Assay



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    CSF3 enhances the immune response to ALV-J via the NFκB signaling pathway. (A) Western blot analysis of p52, p100, phosphorylated <t>p65</t> (p-p65), IκBα, and phosphorylated IκBα (p-IκBα) protein following CSF3 overexpression in DF-1 cells. (B) Quantification of protein levels in (A) based on relative grayscale values. (C) Western blot analysis of p52, p100, phosphorylated p65 (p-p65), IκBα, and phosphorylated IκBα (p-IκBα) protein following CSF3 knockdown in DF-1 cells. (D) Quantification of protein levels in (C) based on relative grayscale values. (D, E) RT-qPCR analysis of TNF-α, IL-1β , and IL-6 mRNA expression following CSF3 overexpression (D) or knockdown (E) in DF-1 cells. (F, G) ELISA measurement of TNF-α, IL-1β, and IL-6 protein levels following CSF3 overexpression (F) or knockdown (G) in DF-1 cells. (H, I) RT-qPCR analysis of TNF-α, IL-1β , and IL-6 mRNA expression following CSF3 overexpression (H) or knockdown (I) in CEF cells. (J, K) ELISA measurement of TNF-α, IL-1β, and IL-6 protein levels following CSF3 overexpression (J) or knockdown (K) in CEF cells. (L) Western blot analysis of STAT3, phosphorylated STAT3 (p-STAT3), env, β-actin, IκBα, p-IκBα, p-p65, p52, and p100 after STAT3 phosphorylation inhibition in CSF3-overexpressing DF-1 cells. (M) Quantification of protein levels in (L) based on relative grayscale values. Statistical significance was determined using a two-tailed unpaired Student’s t-test ( p < 0.05). * p < 0.05, **p < 0.01, *** p < 0.001.
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    Figure 7. Rictor inhibited NLRP3 transcription through increasing the K48-linked ubiquitination of <t>p65</t> by E3 ubiquitin ligase SOCS1. a) Western blotting analysis of total and phosphorylated p65 in WT or Rictor-/-BMDMs treated with LPS (200 ng mL−1) for indicated time. b) Western blotting analysis of indicated proteins in WT or Rictor-/-BMDMs priming with LPS (200 ng mL−1) and JSH-23 (20 μm) for 4 h. c) qRT-PCR analysis showing the mRNA level of p65 in WT or Rictor-/- BMDMs treated with LPS (200 ng mL−1) for 4 h (n = 5). d) Luciferase activity in negative control (NC) or Rictor overexpression (OE) HEK293T cells transfected with plasmids encoding an NF-𝜅B luciferase reporter and TK-Renilla reporter, together with indicated plasmids, was measured
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    Figure 7. Rictor inhibited NLRP3 transcription through increasing the K48-linked ubiquitination of <t>p65</t> by E3 ubiquitin ligase SOCS1. a) Western blotting analysis of total and phosphorylated p65 in WT or Rictor-/-BMDMs treated with LPS (200 ng mL−1) for indicated time. b) Western blotting analysis of indicated proteins in WT or Rictor-/-BMDMs priming with LPS (200 ng mL−1) and JSH-23 (20 μm) for 4 h. c) qRT-PCR analysis showing the mRNA level of p65 in WT or Rictor-/- BMDMs treated with LPS (200 ng mL−1) for 4 h (n = 5). d) Luciferase activity in negative control (NC) or Rictor overexpression (OE) HEK293T cells transfected with plasmids encoding an NF-𝜅B luciferase reporter and TK-Renilla reporter, together with indicated plasmids, was measured
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    Image Search Results


    The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.

    Journal: Poultry Science

    Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

    doi: 10.1016/j.psj.2026.106922

    Figure Lengend Snippet: The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.

    Article Snippet: p-p65 Rabbit Ab , Bioss , bs-0982R , 1: 1500.

    Techniques: Expressing

    The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.

    Journal: Poultry Science

    Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

    doi: 10.1016/j.psj.2026.106922

    Figure Lengend Snippet: The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.

    Article Snippet: p-p65 Rabbit Ab , Bioss , bs-0982R , 1: 1500.

    Techniques: Activity Assay

    RNA-seq of HMEC-1. (A) Volcano plots of DEGs (n = 5). (B) KEGG enrichment bubble plots of DEGs (n = 5). (C) DEGs related to vascular endothelial injury. (D) The relative mRNA expression levels of vascular endothelial injury-related genes verified by RT-qPCR (n = 3). (E) The relative mRNA expression levels of TLR4, TRIF and p65 were detected by RT-qPCR (n = 3). (F) The expression protein levels of TLR4, TRIF and p-p65/p65 were detected by Western blot (n = 3). Values are expressed as mean ± SD. * p < 0.05, ** p < 0.01. The screening criteria for DEGs were defined as FC ≥ 2 or ≤0.5, FDR < 0.05 and p -value <0.05.

    Journal: Frontiers in Pharmacology

    Article Title: Naoxintong capsule decreases circulating exosomes of miR-382-5p to protect LPS-induced vascular endothelial cell injury by targeting STC1 in vitro

    doi: 10.3389/fphar.2026.1655883

    Figure Lengend Snippet: RNA-seq of HMEC-1. (A) Volcano plots of DEGs (n = 5). (B) KEGG enrichment bubble plots of DEGs (n = 5). (C) DEGs related to vascular endothelial injury. (D) The relative mRNA expression levels of vascular endothelial injury-related genes verified by RT-qPCR (n = 3). (E) The relative mRNA expression levels of TLR4, TRIF and p65 were detected by RT-qPCR (n = 3). (F) The expression protein levels of TLR4, TRIF and p-p65/p65 were detected by Western blot (n = 3). Values are expressed as mean ± SD. * p < 0.05, ** p < 0.01. The screening criteria for DEGs were defined as FC ≥ 2 or ≤0.5, FDR < 0.05 and p -value <0.05.

    Article Snippet: After transfer, the membranes were blocked with sealing liquid and incubated for 2 h. Following blocking, membranes were incubated with primary antibodies against β-actin (dilution 1:1,000, ab8227, Abcam), ALIX (dilution 1:1,000, ab275377, Abcam), TSG101 (dilution 1:1,000, ab125011, Abcam), CD9 (dilution 1:1,000, ab236630, Abcam), Bax (dilution 1:1,000, ab32503, Abcam), Bcl-2 (dilution 1:1,000, ab32124, Abcam), Cleaved caspase 3 (dilution 1:500, ab32042, Abcam), TLR4 (dilution 1:1,000, TA382568, OriGene), TRIF (dilution 1:1,000, TA382523, OriGene), NF-κB p65 (dilution 1:1,000, TA385159, OriGene), Phospho-NF-κB p-p65 (dilution 1:1,000, TA380848, OriGene), STC1 (dilution 1:5000, ab229477, Abcam) at 4 °C overnight.

    Techniques: RNA Sequencing, Expressing, Quantitative RT-PCR, Western Blot

    CSF3 enhances the immune response to ALV-J via the NFκB signaling pathway. (A) Western blot analysis of p52, p100, phosphorylated p65 (p-p65), IκBα, and phosphorylated IκBα (p-IκBα) protein following CSF3 overexpression in DF-1 cells. (B) Quantification of protein levels in (A) based on relative grayscale values. (C) Western blot analysis of p52, p100, phosphorylated p65 (p-p65), IκBα, and phosphorylated IκBα (p-IκBα) protein following CSF3 knockdown in DF-1 cells. (D) Quantification of protein levels in (C) based on relative grayscale values. (D, E) RT-qPCR analysis of TNF-α, IL-1β , and IL-6 mRNA expression following CSF3 overexpression (D) or knockdown (E) in DF-1 cells. (F, G) ELISA measurement of TNF-α, IL-1β, and IL-6 protein levels following CSF3 overexpression (F) or knockdown (G) in DF-1 cells. (H, I) RT-qPCR analysis of TNF-α, IL-1β , and IL-6 mRNA expression following CSF3 overexpression (H) or knockdown (I) in CEF cells. (J, K) ELISA measurement of TNF-α, IL-1β, and IL-6 protein levels following CSF3 overexpression (J) or knockdown (K) in CEF cells. (L) Western blot analysis of STAT3, phosphorylated STAT3 (p-STAT3), env, β-actin, IκBα, p-IκBα, p-p65, p52, and p100 after STAT3 phosphorylation inhibition in CSF3-overexpressing DF-1 cells. (M) Quantification of protein levels in (L) based on relative grayscale values. Statistical significance was determined using a two-tailed unpaired Student’s t-test ( p < 0.05). * p < 0.05, **p < 0.01, *** p < 0.001.

    Journal: Poultry Science

    Article Title: CSF3 enhances the innate immune responses to ALV-J infections via NF-κB and interferon pathways

    doi: 10.1016/j.psj.2025.105648

    Figure Lengend Snippet: CSF3 enhances the immune response to ALV-J via the NFκB signaling pathway. (A) Western blot analysis of p52, p100, phosphorylated p65 (p-p65), IκBα, and phosphorylated IκBα (p-IκBα) protein following CSF3 overexpression in DF-1 cells. (B) Quantification of protein levels in (A) based on relative grayscale values. (C) Western blot analysis of p52, p100, phosphorylated p65 (p-p65), IκBα, and phosphorylated IκBα (p-IκBα) protein following CSF3 knockdown in DF-1 cells. (D) Quantification of protein levels in (C) based on relative grayscale values. (D, E) RT-qPCR analysis of TNF-α, IL-1β , and IL-6 mRNA expression following CSF3 overexpression (D) or knockdown (E) in DF-1 cells. (F, G) ELISA measurement of TNF-α, IL-1β, and IL-6 protein levels following CSF3 overexpression (F) or knockdown (G) in DF-1 cells. (H, I) RT-qPCR analysis of TNF-α, IL-1β , and IL-6 mRNA expression following CSF3 overexpression (H) or knockdown (I) in CEF cells. (J, K) ELISA measurement of TNF-α, IL-1β, and IL-6 protein levels following CSF3 overexpression (J) or knockdown (K) in CEF cells. (L) Western blot analysis of STAT3, phosphorylated STAT3 (p-STAT3), env, β-actin, IκBα, p-IκBα, p-p65, p52, and p100 after STAT3 phosphorylation inhibition in CSF3-overexpressing DF-1 cells. (M) Quantification of protein levels in (L) based on relative grayscale values. Statistical significance was determined using a two-tailed unpaired Student’s t-test ( p < 0.05). * p < 0.05, **p < 0.01, *** p < 0.001.

    Article Snippet: Mouse Anti-ALV-J envelope protein JE9 (kindly provided by Prof. Aijian Qin, Yangzhou University, Yangzhou, China), Rabbit Anti-STAT3 antibody (bs-1141R; Boss, China; 1:1000), Rabbit Anti-phospho-STAT3 (Ser727) antibody (bs-3429R; Boss, China; 1:1000), Rabbit Anti-NFκB2 antibody (10037P, Boss, China; 1:1000), Rabbit Anti-NFκB p-p65 (bs-0982R, Boss, China; 1:1000), Rabbit Anti-IKBα Rabbit (10268-1-AP, Proteintech, USA; 1:1000), Anti-p-IKBα (bs-2513R, Boss, China; 1:1000), and goat anti-rabbit IgG/HRP (bs13278), goat anti-mouse IgG/HRP (bs12478), goat Anti-Mouse IgG ( H + L ) FITC (bs10950) secondary antibody were purchased from Bioss (Beijing, China).

    Techniques: Western Blot, Over Expression, Knockdown, Quantitative RT-PCR, Expressing, Enzyme-linked Immunosorbent Assay, Phospho-proteomics, Inhibition, Two Tailed Test

    Figure 7. Rictor inhibited NLRP3 transcription through increasing the K48-linked ubiquitination of p65 by E3 ubiquitin ligase SOCS1. a) Western blotting analysis of total and phosphorylated p65 in WT or Rictor-/-BMDMs treated with LPS (200 ng mL−1) for indicated time. b) Western blotting analysis of indicated proteins in WT or Rictor-/-BMDMs priming with LPS (200 ng mL−1) and JSH-23 (20 μm) for 4 h. c) qRT-PCR analysis showing the mRNA level of p65 in WT or Rictor-/- BMDMs treated with LPS (200 ng mL−1) for 4 h (n = 5). d) Luciferase activity in negative control (NC) or Rictor overexpression (OE) HEK293T cells transfected with plasmids encoding an NF-𝜅B luciferase reporter and TK-Renilla reporter, together with indicated plasmids, was measured

    Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

    Article Title: Rictor Ameliorates Acute Antibody-Mediated Rejection Following Kidney Transplantation by Suppressing Macrophage M1 Polarization Through p65-NLRP3 Axis.

    doi: 10.1002/advs.202417119

    Figure Lengend Snippet: Figure 7. Rictor inhibited NLRP3 transcription through increasing the K48-linked ubiquitination of p65 by E3 ubiquitin ligase SOCS1. a) Western blotting analysis of total and phosphorylated p65 in WT or Rictor-/-BMDMs treated with LPS (200 ng mL−1) for indicated time. b) Western blotting analysis of indicated proteins in WT or Rictor-/-BMDMs priming with LPS (200 ng mL−1) and JSH-23 (20 μm) for 4 h. c) qRT-PCR analysis showing the mRNA level of p65 in WT or Rictor-/- BMDMs treated with LPS (200 ng mL−1) for 4 h (n = 5). d) Luciferase activity in negative control (NC) or Rictor overexpression (OE) HEK293T cells transfected with plasmids encoding an NF-𝜅B luciferase reporter and TK-Renilla reporter, together with indicated plasmids, was measured

    Article Snippet: The incubation was performed at 4 °C overnight with the primary antibodies against Rictor (1:1000, #2114, CST), Raptor (1:1000, #2280, CST), Akt (1:2000, #10176-2-AP, Proteintech), p-Akt(Ser473) (1:1000, #66444-1-Ig, Proteintech), pAkt(Thr308) (1:1000, #9275, CST), mTOR (1:1000, #2983, CST), p-mTOR (1:1000, #5536, CST), NLRP3 (1:1000, #15101, CST), IL-1β (1:1000, #31202, CST), Caspase-1 (1:1000, #24232, CST), cleaved-IL1β (1:1000, #63124, CST), cleaved-Caspase-1 (1:1000, #AG-20B-0042, AdigoGen), ASC (1:1000, #67824, CST), AIM2 (1:1000, #63660, CST), SOCS1 (1:1000, #55313, CST), p65 (1:1000, #8242, CST), p-p65 (1:1000, #TA325803, Origene), ubiquitin (#sc-8017, Santa Cruz), Flag (#14793, CST), HA (#51064-2-AP, Proteintech), Myc (#sc-40, Santa Cruz), GAPDH (1:10000, #60004-1-Ig, Proteintech) and β-actin (1:10000, #66009-1-Ig, Proteintech).

    Techniques: Ubiquitin Proteomics, Western Blot, Quantitative RT-PCR, Luciferase, Activity Assay, Negative Control, Over Expression, Transfection