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mouse anti human p53 antibody  (Proteintech)


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    Proteintech mouse anti human p53 antibody
    Clusters 0 and 2 were comprised predominantly by wildtype cells. An upregulation of the “HALLMARK_TNFA_SIGNALING_VIA_NFKB” gene set in both Clusters 0 (a) and 2 (b) was observed. In Cluster 0, there was additionally an upregulation of “HALLMARK_ANGIOGENESIS” (c) and “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (d) . In Cluster 2, there was additionally an upregulation of “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (e) , “HALLMARK_KRAS_SIGNALING_UP” (f) , and <t>“HALLMARK_P53_PATHWAY”</t> (g) .
    Mouse Anti Human P53 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 2182 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mouse+anti+human+p53+antibody/P53+Antibody/pmc12527130-160-20-26
    Average 96 stars, based on 2182 article reviews
    mouse anti human p53 antibody - by Bioz Stars, 2026-09
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    Images

    1) Product Images from "STAG2 mutations in the normal colon induce upregulation of oncogenic pathways in neighbouring wildtype cells"

    Article Title: STAG2 mutations in the normal colon induce upregulation of oncogenic pathways in neighbouring wildtype cells

    Journal: PLOS One

    doi: 10.1371/journal.pone.0332499

    Clusters 0 and 2 were comprised predominantly by wildtype cells. An upregulation of the “HALLMARK_TNFA_SIGNALING_VIA_NFKB” gene set in both Clusters 0 (a) and 2 (b) was observed. In Cluster 0, there was additionally an upregulation of “HALLMARK_ANGIOGENESIS” (c) and “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (d) . In Cluster 2, there was additionally an upregulation of “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (e) , “HALLMARK_KRAS_SIGNALING_UP” (f) , and “HALLMARK_P53_PATHWAY” (g) .
    Figure Legend Snippet: Clusters 0 and 2 were comprised predominantly by wildtype cells. An upregulation of the “HALLMARK_TNFA_SIGNALING_VIA_NFKB” gene set in both Clusters 0 (a) and 2 (b) was observed. In Cluster 0, there was additionally an upregulation of “HALLMARK_ANGIOGENESIS” (c) and “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (d) . In Cluster 2, there was additionally an upregulation of “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (e) , “HALLMARK_KRAS_SIGNALING_UP” (f) , and “HALLMARK_P53_PATHWAY” (g) .

    Techniques Used:

    Fluorescent intensity of anti-TNFα antibody (a, b) , anti-KRAS antibody (c, d) and anti-p53 antibody (e, f) was statistically significantly upregulated in co-cultured wildtype organoids relative STAG2 mutant organoids. Scale bars are 50µm. All experiments were performed with N = 3 biological replicates.
    Figure Legend Snippet: Fluorescent intensity of anti-TNFα antibody (a, b) , anti-KRAS antibody (c, d) and anti-p53 antibody (e, f) was statistically significantly upregulated in co-cultured wildtype organoids relative STAG2 mutant organoids. Scale bars are 50µm. All experiments were performed with N = 3 biological replicates.

    Techniques Used: Cell Culture, Mutagenesis

    In co-culture, we observed upregulation of TNFα, KRAS and p53 in wildtype organoids, proposing a cooperative mechanism of early oncogenesis.
    Figure Legend Snippet: In co-culture, we observed upregulation of TNFα, KRAS and p53 in wildtype organoids, proposing a cooperative mechanism of early oncogenesis.

    Techniques Used: Co-Culture Assay

    Related Articles

    Cell Culture:

    Article Title: STAG2 mutations in the normal colon induce upregulation of oncogenic pathways in neighbouring wildtype cells
    Article Snippet: For immunofluorescent experiments in and , unless otherwise stated, steps were similar as above.For immunofluorescent experiments in and , unless otherwise stated, steps were similar as above.. Primary antibodies used included rabbit anti-human STAG2 antibody (1:100, 19837–1-AP, Proteintech, USA), mouse anti-human KI67 antibody (1:500, 66555–6-Ig, Proteintech, USA), mouse anti-human P53 antibody (1:400, 60283–2-Ig, Proteintech, USA), mouse anti-human CCND1 antibody (1:100, 60186–1-Ig, Proteintech, USA), mouse anti-human TERT antibody (1: 100, MA5−16033, Invitrogen, USA), mouse anti-human KRAS antibody (1:250, 415700, Invitrogen, USA), and mouse anti-human TNFα antibody (1:50, MA5−23720, Invitrogen, USA).. Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1 μg/ml, D1306, Invitrogen, USA).Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1..

    Article Title: STAG2 mutations in the normal colon induce upregulation of oncogenic pathways in neighbouring wildtype cells.
    Article Snippet: For immunofluorescent experiments in Figs 4 and 5, unless otherwise stated, steps were similar as above.For immunofluorescent experiments in Figs 4 and 5, unless otherwise stated, steps were similar as above.. Primary antibodies used included rabbit anti-human STAG2 antibody (1:100, 19837–1-AP, Proteintech, USA), mouse anti-human KI67 antibody (1:500, 66555–6-Ig, Proteintech, USA), mouse anti-human P53 antibody (1:400, 60283–2-Ig, Proteintech, USA), mouse anti-human CCND1 antibody (1:100, 60186–1-Ig, Proteintech, USA), mouse anti-human TERT antibody (1: 100, MA5−16033, Invitrogen, USA), mouse anti-human KRAS antibody (1:250, 415700, Invitrogen, USA), and mouse anti-human TNFα antibody (1:50, MA5−23720, Invitrogen, USA).. Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1 μg/ml, D1306, Invitrogen, USA).Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1..

    Mutagenesis:

    Article Title: STAG2 mutations in the normal colon induce upregulation of oncogenic pathways in neighbouring wildtype cells
    Article Snippet: For immunofluorescent experiments in and , unless otherwise stated, steps were similar as above.For immunofluorescent experiments in and , unless otherwise stated, steps were similar as above.. Primary antibodies used included rabbit anti-human STAG2 antibody (1:100, 19837–1-AP, Proteintech, USA), mouse anti-human KI67 antibody (1:500, 66555–6-Ig, Proteintech, USA), mouse anti-human P53 antibody (1:400, 60283–2-Ig, Proteintech, USA), mouse anti-human CCND1 antibody (1:100, 60186–1-Ig, Proteintech, USA), mouse anti-human TERT antibody (1: 100, MA5−16033, Invitrogen, USA), mouse anti-human KRAS antibody (1:250, 415700, Invitrogen, USA), and mouse anti-human TNFα antibody (1:50, MA5−23720, Invitrogen, USA).. Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1 μg/ml, D1306, Invitrogen, USA).Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1..

    Article Title: STAG2 mutations in the normal colon induce upregulation of oncogenic pathways in neighbouring wildtype cells.
    Article Snippet: For immunofluorescent experiments in Figs 4 and 5, unless otherwise stated, steps were similar as above.For immunofluorescent experiments in Figs 4 and 5, unless otherwise stated, steps were similar as above.. Primary antibodies used included rabbit anti-human STAG2 antibody (1:100, 19837–1-AP, Proteintech, USA), mouse anti-human KI67 antibody (1:500, 66555–6-Ig, Proteintech, USA), mouse anti-human P53 antibody (1:400, 60283–2-Ig, Proteintech, USA), mouse anti-human CCND1 antibody (1:100, 60186–1-Ig, Proteintech, USA), mouse anti-human TERT antibody (1: 100, MA5−16033, Invitrogen, USA), mouse anti-human KRAS antibody (1:250, 415700, Invitrogen, USA), and mouse anti-human TNFα antibody (1:50, MA5−23720, Invitrogen, USA).. Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1 μg/ml, D1306, Invitrogen, USA).Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1..

    Co-Culture Assay:

    Article Title: STAG2 mutations in the normal colon induce upregulation of oncogenic pathways in neighbouring wildtype cells
    Article Snippet: For immunofluorescent experiments in and , unless otherwise stated, steps were similar as above.For immunofluorescent experiments in and , unless otherwise stated, steps were similar as above.. Primary antibodies used included rabbit anti-human STAG2 antibody (1:100, 19837–1-AP, Proteintech, USA), mouse anti-human KI67 antibody (1:500, 66555–6-Ig, Proteintech, USA), mouse anti-human P53 antibody (1:400, 60283–2-Ig, Proteintech, USA), mouse anti-human CCND1 antibody (1:100, 60186–1-Ig, Proteintech, USA), mouse anti-human TERT antibody (1: 100, MA5−16033, Invitrogen, USA), mouse anti-human KRAS antibody (1:250, 415700, Invitrogen, USA), and mouse anti-human TNFα antibody (1:50, MA5−23720, Invitrogen, USA).. Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1 μg/ml, D1306, Invitrogen, USA).Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1..

    Article Title: STAG2 mutations in the normal colon induce upregulation of oncogenic pathways in neighbouring wildtype cells.
    Article Snippet: For immunofluorescent experiments in Figs 4 and 5, unless otherwise stated, steps were similar as above.For immunofluorescent experiments in Figs 4 and 5, unless otherwise stated, steps were similar as above.. Primary antibodies used included rabbit anti-human STAG2 antibody (1:100, 19837–1-AP, Proteintech, USA), mouse anti-human KI67 antibody (1:500, 66555–6-Ig, Proteintech, USA), mouse anti-human P53 antibody (1:400, 60283–2-Ig, Proteintech, USA), mouse anti-human CCND1 antibody (1:100, 60186–1-Ig, Proteintech, USA), mouse anti-human TERT antibody (1: 100, MA5−16033, Invitrogen, USA), mouse anti-human KRAS antibody (1:250, 415700, Invitrogen, USA), and mouse anti-human TNFα antibody (1:50, MA5−23720, Invitrogen, USA).. Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1 μg/ml, D1306, Invitrogen, USA).Slides were then washed in PBS, before the addition of CoraLite488-conjugated Goat Anti-Rabbit antibody (1:500, SA00013−2, Proteintech, USA), Multi-rAbTM CoraLite® Plus 647-Goat Anti-Mouse antibody (1:500, RGAM005, Proteintech, USA), and DAPI(0.1..



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    Clusters 0 and 2 were comprised predominantly by wildtype cells. An upregulation of the “HALLMARK_TNFA_SIGNALING_VIA_NFKB” gene set in both Clusters 0 (a) and 2 (b) was observed. In Cluster 0, there was additionally an upregulation of “HALLMARK_ANGIOGENESIS” (c) and “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (d) . In Cluster 2, there was additionally an upregulation of “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (e) , “HALLMARK_KRAS_SIGNALING_UP” (f) , and <t>“HALLMARK_P53_PATHWAY”</t> (g) .
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    Moderate regulation of alternatively spliced p53β mRNA by UPF1. A Alternative splicing (AS) and nonsense-mediated decay (NMD) involving exon 9b (E9b) within p53 intron 9. Inclusion or skipping of E9b (dark gray box) generates p53β or p53α mRNA, respectively. E9b is expected to recruit UPF1 and can be degraded. B UV-crosslinking RNA immunoprecipitation (UV-RIP) assays. HeLa cells were cotransfected with Flag-UPF1 and Dup-p53 minigenes. Lysates were immunoprecipitated using anti-Flag M2 agarose beads. Enrichment of the E9b-included isoform (Dup-β) was assessed using primers spanning the E9b–β-globin exon 2 junction of p53. Data are represented as mean ± SEM (n ≥ 3). * p < 0.05. C Splicing analysis of Dup-p53 minigene-transfected HeLa cells. STOP and GO reporters were used for NMD analysis with or without a premature termination codon (PTC). Primers targeting β-globin exon 1 (forward) and exon 2 (reverse) were used. The upper band corresponds to the E9b-included isoform (β), and the lower band to the E9b-skipped isoform (α). β-actin serves as a loading control. D Splicing analysis from Dup-p53 (STOP) minigene in siUPF1-transfected HeLa cells compared with siGFP-transfected control cells. The upper band corresponds to the E9b-included isoform (β), and the lower band to the E9b-skipped isoform (α). RT-PCR was performed employing β-globin exon 1 (forward) and exon 2 (reverse) primers. UPF1 knockdown was confirmed by Western blot assays (bottom). β-actin was used as a loading control. E RT-qPCR analysis for endogenous p53 mRNA isoforms—p53α and p53β—in UPF1-depleted HeLa cells. F RT-qPCR analysis for exon 1 of endogenous p53 in UPF1-depleted HeLa cells, corresponding to the 5′ UTR. (G, H) Decay rates of p53α mRNA G and p53β mRNA H in siUPF1- and siGFP-transfected cells following transcription inhibition using actinomycin D (ActD). The mean half-lives of p53α or p53β mRNAs are indicated by a dashed line. Data are represented as mean ± SEM (n ≥ 3)

    Journal: Cell & Bioscience

    Article Title: Regulation of oncogenic C-terminal truncated p53β protein isoform expression by SRSF3–UPF1 splicing and surveillance axis

    doi: 10.1186/s13578-026-01556-5

    Figure Lengend Snippet: Moderate regulation of alternatively spliced p53β mRNA by UPF1. A Alternative splicing (AS) and nonsense-mediated decay (NMD) involving exon 9b (E9b) within p53 intron 9. Inclusion or skipping of E9b (dark gray box) generates p53β or p53α mRNA, respectively. E9b is expected to recruit UPF1 and can be degraded. B UV-crosslinking RNA immunoprecipitation (UV-RIP) assays. HeLa cells were cotransfected with Flag-UPF1 and Dup-p53 minigenes. Lysates were immunoprecipitated using anti-Flag M2 agarose beads. Enrichment of the E9b-included isoform (Dup-β) was assessed using primers spanning the E9b–β-globin exon 2 junction of p53. Data are represented as mean ± SEM (n ≥ 3). * p < 0.05. C Splicing analysis of Dup-p53 minigene-transfected HeLa cells. STOP and GO reporters were used for NMD analysis with or without a premature termination codon (PTC). Primers targeting β-globin exon 1 (forward) and exon 2 (reverse) were used. The upper band corresponds to the E9b-included isoform (β), and the lower band to the E9b-skipped isoform (α). β-actin serves as a loading control. D Splicing analysis from Dup-p53 (STOP) minigene in siUPF1-transfected HeLa cells compared with siGFP-transfected control cells. The upper band corresponds to the E9b-included isoform (β), and the lower band to the E9b-skipped isoform (α). RT-PCR was performed employing β-globin exon 1 (forward) and exon 2 (reverse) primers. UPF1 knockdown was confirmed by Western blot assays (bottom). β-actin was used as a loading control. E RT-qPCR analysis for endogenous p53 mRNA isoforms—p53α and p53β—in UPF1-depleted HeLa cells. F RT-qPCR analysis for exon 1 of endogenous p53 in UPF1-depleted HeLa cells, corresponding to the 5′ UTR. (G, H) Decay rates of p53α mRNA G and p53β mRNA H in siUPF1- and siGFP-transfected cells following transcription inhibition using actinomycin D (ActD). The mean half-lives of p53α or p53β mRNAs are indicated by a dashed line. Data are represented as mean ± SEM (n ≥ 3)

    Article Snippet: The antibodies used were as follows- anti-UPF1 (Cell Signaling, #12,040), anti-SRSF3 (Invitrogen, #33–4200), anti-FLAG-M2 (Sigma, #F3165), anti-SRSF1 (Thermo Fisher, #32–4500), anti-Histone H3 (Abcam, #ab1791), anti-α-tubulin (Santa Cruz, #sc-8035), anti-β-actin (Abcam, #ab6276), anti-Myc (Sigma, #05-724MG), anti-p53 (Santa Cruz, DO-1 #sc-126; Pab1801 #sc-98; BIORAD, DO-11 #MCA1704), and E-cadherin (Biosciences, #610,181).

    Techniques: Alternative Splicing, RNA Immunoprecipitation, Immunoprecipitation, Transfection, Control, Reverse Transcription Polymerase Chain Reaction, Knockdown, Western Blot, Quantitative RT-PCR, Inhibition

    Identification and localization of the intron-retained p53 transcript. A Diagram of sequential (seq) or non-sequential (non-seq) splicing of p53 intron 9. I9a and I9b indicate the upstream and downstream introns flanking E9b, respectively. Predicted premature termination codons (PTCs) are shown in red. B RT-qPCR analysis of intron retention in p53 transcripts under basal conditions in HeLa cells. I2, intron2; N.D., not detected. C Decay rates of p53-IR transcript in siUPF1- and siGFP-transfected HeLa cells following transcription inhibition with ActD. The mean half-lives of p53-IR transcript are indicated by a dashed line. Data are represented as mean ± SEM (n ≥ 3). D RT-qPCR-based quantification of p53α, p53β, and p53-IR transcript following cycloheximide (CHX) treatment in HeLa cells. Data are represented as mean ± SEM (n ≥ 3). ** p < 0.01. E , F Ratios of p53α, p53β, and p53-IR transcript levels altered by CHX treatment in the nuclear and cytoplasmic fractions of HeLa cells, compared with DMSO-treated controls. Data are presented as mean ± SEM (n ≥ 3). *** p < 0.001. G Subcellular localization of p53 transcripts in HeLa cells. Cytoplasmic (Cy), Nucleoplasmic (Np), and chromatin-associated (Chr) fractions are indicated. GAPDH pre-mRNA and NEAT1 long noncoding RNA were used as nuclear-retained RNA markers, and 18S ribosomal RNA was used as a cytoplasmic RNA marker

    Journal: Cell & Bioscience

    Article Title: Regulation of oncogenic C-terminal truncated p53β protein isoform expression by SRSF3–UPF1 splicing and surveillance axis

    doi: 10.1186/s13578-026-01556-5

    Figure Lengend Snippet: Identification and localization of the intron-retained p53 transcript. A Diagram of sequential (seq) or non-sequential (non-seq) splicing of p53 intron 9. I9a and I9b indicate the upstream and downstream introns flanking E9b, respectively. Predicted premature termination codons (PTCs) are shown in red. B RT-qPCR analysis of intron retention in p53 transcripts under basal conditions in HeLa cells. I2, intron2; N.D., not detected. C Decay rates of p53-IR transcript in siUPF1- and siGFP-transfected HeLa cells following transcription inhibition with ActD. The mean half-lives of p53-IR transcript are indicated by a dashed line. Data are represented as mean ± SEM (n ≥ 3). D RT-qPCR-based quantification of p53α, p53β, and p53-IR transcript following cycloheximide (CHX) treatment in HeLa cells. Data are represented as mean ± SEM (n ≥ 3). ** p < 0.01. E , F Ratios of p53α, p53β, and p53-IR transcript levels altered by CHX treatment in the nuclear and cytoplasmic fractions of HeLa cells, compared with DMSO-treated controls. Data are presented as mean ± SEM (n ≥ 3). *** p < 0.001. G Subcellular localization of p53 transcripts in HeLa cells. Cytoplasmic (Cy), Nucleoplasmic (Np), and chromatin-associated (Chr) fractions are indicated. GAPDH pre-mRNA and NEAT1 long noncoding RNA were used as nuclear-retained RNA markers, and 18S ribosomal RNA was used as a cytoplasmic RNA marker

    Article Snippet: The antibodies used were as follows- anti-UPF1 (Cell Signaling, #12,040), anti-SRSF3 (Invitrogen, #33–4200), anti-FLAG-M2 (Sigma, #F3165), anti-SRSF1 (Thermo Fisher, #32–4500), anti-Histone H3 (Abcam, #ab1791), anti-α-tubulin (Santa Cruz, #sc-8035), anti-β-actin (Abcam, #ab6276), anti-Myc (Sigma, #05-724MG), anti-p53 (Santa Cruz, DO-1 #sc-126; Pab1801 #sc-98; BIORAD, DO-11 #MCA1704), and E-cadherin (Biosciences, #610,181).

    Techniques: Quantitative RT-PCR, Transfection, Inhibition, Marker

    Chromatin association of SRSF3 and UPF1 at the TP53 gene. A Subcellular localization of SRSF3 and UPF1 in HeLa cells. α-tubulin and Histone H3 are markers for the cytoplasmic and chromatin-associated fractions, respectively. Regarding SRSF1, hyperphosphorylated forms localize to the nucleoplasm, while hyperphosphorylated forms localize to the cytoplasm. B UPF1 and SRSF3 chromatin immunoprecipitation (ChIP) analysis of TP53 genomic regions. UPF1 ChIP was performed using an anti-UPF1 antibody compared with an anti-IgG control in HeLa cells, whereas SRSF3 ChIP was performed using an anti-Flag antibody in Flag-SRSF3-expressing HeLa cells compared with Flag-empty vector (Flag-Vec) control cells. Pro, promoter; I4, intron 4; I9, intron 9; E11, exon 11. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05; ** p < 0.01. C Coimmunoprecipitation (co-IP) showing the interaction between UPF1 and SRSF3. HeLa cells were cotransfected with Myc-UPF1 and Flag-SRSF3, and immunoprecipitation was performed utilizing anti-Flag antibody. D Coimmunofluorescence (co-IF) of UPF1 and SRSF3 after treatment with transcription or translation inhibitors, which are actinomycin D (ActD) and flavopiridol (Flavo), or cycloheximide (CHX), respectively. UPF1 was detected using Cy3-conjugated secondary antibody (red), and SRSF3 was identified employing the Alexa Fluor 488-conjugated one (green). Nuclei were counterstained with DAPI (blue). Scale bars, 5 μm. E Quantification of UPF1 and SRSF3 colocalization by Pearson’s correlation coefficient. Data are presented as mean ± SEM (n ≥ 30). *** p < 0.001. F Representative images of in situ proximity ligation assay (PLA) between UPF1 and SRSF3 in HeLa cells. Each cell was treated with DMSO (control), ActD, Flavo, or CHX. PLA signals are shown as red puncta, and nuclei are counterstained with DAPI (blue). Scale bars, 5 μm. G Quantification of the mean of nuclear PLA signals per nucleus. Data are presented as mean ± SEM (n ≥ 30). Statistical significance was determined by one-way ANOVA. * p < 0.05; *** p < 0.001

    Journal: Cell & Bioscience

    Article Title: Regulation of oncogenic C-terminal truncated p53β protein isoform expression by SRSF3–UPF1 splicing and surveillance axis

    doi: 10.1186/s13578-026-01556-5

    Figure Lengend Snippet: Chromatin association of SRSF3 and UPF1 at the TP53 gene. A Subcellular localization of SRSF3 and UPF1 in HeLa cells. α-tubulin and Histone H3 are markers for the cytoplasmic and chromatin-associated fractions, respectively. Regarding SRSF1, hyperphosphorylated forms localize to the nucleoplasm, while hyperphosphorylated forms localize to the cytoplasm. B UPF1 and SRSF3 chromatin immunoprecipitation (ChIP) analysis of TP53 genomic regions. UPF1 ChIP was performed using an anti-UPF1 antibody compared with an anti-IgG control in HeLa cells, whereas SRSF3 ChIP was performed using an anti-Flag antibody in Flag-SRSF3-expressing HeLa cells compared with Flag-empty vector (Flag-Vec) control cells. Pro, promoter; I4, intron 4; I9, intron 9; E11, exon 11. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05; ** p < 0.01. C Coimmunoprecipitation (co-IP) showing the interaction between UPF1 and SRSF3. HeLa cells were cotransfected with Myc-UPF1 and Flag-SRSF3, and immunoprecipitation was performed utilizing anti-Flag antibody. D Coimmunofluorescence (co-IF) of UPF1 and SRSF3 after treatment with transcription or translation inhibitors, which are actinomycin D (ActD) and flavopiridol (Flavo), or cycloheximide (CHX), respectively. UPF1 was detected using Cy3-conjugated secondary antibody (red), and SRSF3 was identified employing the Alexa Fluor 488-conjugated one (green). Nuclei were counterstained with DAPI (blue). Scale bars, 5 μm. E Quantification of UPF1 and SRSF3 colocalization by Pearson’s correlation coefficient. Data are presented as mean ± SEM (n ≥ 30). *** p < 0.001. F Representative images of in situ proximity ligation assay (PLA) between UPF1 and SRSF3 in HeLa cells. Each cell was treated with DMSO (control), ActD, Flavo, or CHX. PLA signals are shown as red puncta, and nuclei are counterstained with DAPI (blue). Scale bars, 5 μm. G Quantification of the mean of nuclear PLA signals per nucleus. Data are presented as mean ± SEM (n ≥ 30). Statistical significance was determined by one-way ANOVA. * p < 0.05; *** p < 0.001

    Article Snippet: The antibodies used were as follows- anti-UPF1 (Cell Signaling, #12,040), anti-SRSF3 (Invitrogen, #33–4200), anti-FLAG-M2 (Sigma, #F3165), anti-SRSF1 (Thermo Fisher, #32–4500), anti-Histone H3 (Abcam, #ab1791), anti-α-tubulin (Santa Cruz, #sc-8035), anti-β-actin (Abcam, #ab6276), anti-Myc (Sigma, #05-724MG), anti-p53 (Santa Cruz, DO-1 #sc-126; Pab1801 #sc-98; BIORAD, DO-11 #MCA1704), and E-cadherin (Biosciences, #610,181).

    Techniques: Chromatin Immunoprecipitation, Control, Expressing, Plasmid Preparation, Co-Immunoprecipitation Assay, Immunoprecipitation, In Situ, Proximity Ligation Assay

    Binding of SRSF3 at the retained intron of p53 transcript. A UV-RNA immunoprecipitation (UV-RIP) analysis of endogenous p53 (pre-)mRNA. Flag-SRSF3-expressing and Flag-Vec control cells were subjected to immunoprecipitation using an anti-Flag antibody. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05; ** p < 0.01. B Schematic diagram of Dup-p53 minigene reporters harboring mutations in SRSF3-binding motifs, indicated by black circles, and mutated motifs by white circles. The WT contains all intact SRSF3-binding motifs. Mutant reporters (Mut1–Mut4) contain individual or combinations of mutated SRSF3-binding motifs, as indicated. C UV-RIP analysis of Dup-p53 minigene reporters. Flag-SRSF3-expressing cells and Flag-Vec control cells were subjected to immunoprecipitation using an anti-Flag antibody. Data are presented as mean ± SEM (n ≥ 3). ** p < 0.01. D Splicing analysis of Dup-p53 minigene reporters in transfected HeLa cells. Relative Dup-β transcript level was measured by RT-qPCR. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05. E SRSF3 tethering analysis in combination with UPF1 knockdown. MS2 RNA hairpins were inserted into I9a of the Dup-p53 minigene, and MS2-binding protein (MBP)-fused SRSF3 was co-transfected to tether SRSF3 to the MS2 RNA. RT-qPCR was used to quantify Dup-α and Dup-β isoforms. Data are presented as mean ± SEM (n ≥ 3). ** p < 0.01. F Proposed model illustrating the splicing-linked RNA surveillance mechanism. p53-IR transcript interacts with SRSF3, which subsequently recruits UPF1. Formation of p53-IR–SRSF3–UPF1 ternary complex suppresses E9b inclusion, thereby preventing production of the p53β mRNA

    Journal: Cell & Bioscience

    Article Title: Regulation of oncogenic C-terminal truncated p53β protein isoform expression by SRSF3–UPF1 splicing and surveillance axis

    doi: 10.1186/s13578-026-01556-5

    Figure Lengend Snippet: Binding of SRSF3 at the retained intron of p53 transcript. A UV-RNA immunoprecipitation (UV-RIP) analysis of endogenous p53 (pre-)mRNA. Flag-SRSF3-expressing and Flag-Vec control cells were subjected to immunoprecipitation using an anti-Flag antibody. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05; ** p < 0.01. B Schematic diagram of Dup-p53 minigene reporters harboring mutations in SRSF3-binding motifs, indicated by black circles, and mutated motifs by white circles. The WT contains all intact SRSF3-binding motifs. Mutant reporters (Mut1–Mut4) contain individual or combinations of mutated SRSF3-binding motifs, as indicated. C UV-RIP analysis of Dup-p53 minigene reporters. Flag-SRSF3-expressing cells and Flag-Vec control cells were subjected to immunoprecipitation using an anti-Flag antibody. Data are presented as mean ± SEM (n ≥ 3). ** p < 0.01. D Splicing analysis of Dup-p53 minigene reporters in transfected HeLa cells. Relative Dup-β transcript level was measured by RT-qPCR. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05. E SRSF3 tethering analysis in combination with UPF1 knockdown. MS2 RNA hairpins were inserted into I9a of the Dup-p53 minigene, and MS2-binding protein (MBP)-fused SRSF3 was co-transfected to tether SRSF3 to the MS2 RNA. RT-qPCR was used to quantify Dup-α and Dup-β isoforms. Data are presented as mean ± SEM (n ≥ 3). ** p < 0.01. F Proposed model illustrating the splicing-linked RNA surveillance mechanism. p53-IR transcript interacts with SRSF3, which subsequently recruits UPF1. Formation of p53-IR–SRSF3–UPF1 ternary complex suppresses E9b inclusion, thereby preventing production of the p53β mRNA

    Article Snippet: The antibodies used were as follows- anti-UPF1 (Cell Signaling, #12,040), anti-SRSF3 (Invitrogen, #33–4200), anti-FLAG-M2 (Sigma, #F3165), anti-SRSF1 (Thermo Fisher, #32–4500), anti-Histone H3 (Abcam, #ab1791), anti-α-tubulin (Santa Cruz, #sc-8035), anti-β-actin (Abcam, #ab6276), anti-Myc (Sigma, #05-724MG), anti-p53 (Santa Cruz, DO-1 #sc-126; Pab1801 #sc-98; BIORAD, DO-11 #MCA1704), and E-cadherin (Biosciences, #610,181).

    Techniques: Binding Assay, RNA Immunoprecipitation, Expressing, Control, Immunoprecipitation, Mutagenesis, Transfection, Quantitative RT-PCR, Knockdown

    Expression of C-terminal truncated p53 protein upon SRSF3 depletion. A RT-qPCR analysis of p53α and p53β mRNA levels in HEK293, HeLa, HCT116, and SW480 cells transfected with siRNA targeted to SRSF3 (siSRSF3) compared to control siRNA (siGFP). Exon junction-specific primers used for isoform detection are shown (left). Data are presented as mean ± SEM (n ≥ 3). * p < 0.05; ** p < 0.01. B Western blot analysis of p53 protein isoforms in SW480 cells transfected with siRNAs targeting SRSF3 and SRSF1. p53 isoforms were detected using anti-p53 (DO-1) antibody. The upper band corresponds to p53α protein (~ 53 kDa), and the lower band to p53β protein isoform (~ 47 kDa). β-actin serves as a loading control. C Western blot analysis of p53 protein isoforms in SRSF3 knockout (KO) SW480 cells obtained by employing CRISPR/Cas9. Total cell lysates were analyzed using anti-p53 (Pab1801 and DO-11) and a custom anti-p53β-specific antibody. β-actin serves as a loading control. D Western blot analysis of p53 protein isoforms in UPF1-depleted SW480 cells (siUPF1) compared to control cells (siGFP). The anti-p53 (DO-1) antibody used in (B) was also employed to detect p53α and p53β protein isoforms. β-actin serves as a loading control. E Quantification of p53α and p53β protein isoform levels detected by anti-p53 (DO-11) antibody. Data are presented as mean ± SEM (n = 3). ** p < 0.01. F Proposed model explaining the production of the C-terminal truncated p53β protein isoform

    Journal: Cell & Bioscience

    Article Title: Regulation of oncogenic C-terminal truncated p53β protein isoform expression by SRSF3–UPF1 splicing and surveillance axis

    doi: 10.1186/s13578-026-01556-5

    Figure Lengend Snippet: Expression of C-terminal truncated p53 protein upon SRSF3 depletion. A RT-qPCR analysis of p53α and p53β mRNA levels in HEK293, HeLa, HCT116, and SW480 cells transfected with siRNA targeted to SRSF3 (siSRSF3) compared to control siRNA (siGFP). Exon junction-specific primers used for isoform detection are shown (left). Data are presented as mean ± SEM (n ≥ 3). * p < 0.05; ** p < 0.01. B Western blot analysis of p53 protein isoforms in SW480 cells transfected with siRNAs targeting SRSF3 and SRSF1. p53 isoforms were detected using anti-p53 (DO-1) antibody. The upper band corresponds to p53α protein (~ 53 kDa), and the lower band to p53β protein isoform (~ 47 kDa). β-actin serves as a loading control. C Western blot analysis of p53 protein isoforms in SRSF3 knockout (KO) SW480 cells obtained by employing CRISPR/Cas9. Total cell lysates were analyzed using anti-p53 (Pab1801 and DO-11) and a custom anti-p53β-specific antibody. β-actin serves as a loading control. D Western blot analysis of p53 protein isoforms in UPF1-depleted SW480 cells (siUPF1) compared to control cells (siGFP). The anti-p53 (DO-1) antibody used in (B) was also employed to detect p53α and p53β protein isoforms. β-actin serves as a loading control. E Quantification of p53α and p53β protein isoform levels detected by anti-p53 (DO-11) antibody. Data are presented as mean ± SEM (n = 3). ** p < 0.01. F Proposed model explaining the production of the C-terminal truncated p53β protein isoform

    Article Snippet: The antibodies used were as follows- anti-UPF1 (Cell Signaling, #12,040), anti-SRSF3 (Invitrogen, #33–4200), anti-FLAG-M2 (Sigma, #F3165), anti-SRSF1 (Thermo Fisher, #32–4500), anti-Histone H3 (Abcam, #ab1791), anti-α-tubulin (Santa Cruz, #sc-8035), anti-β-actin (Abcam, #ab6276), anti-Myc (Sigma, #05-724MG), anti-p53 (Santa Cruz, DO-1 #sc-126; Pab1801 #sc-98; BIORAD, DO-11 #MCA1704), and E-cadherin (Biosciences, #610,181).

    Techniques: Expressing, Quantitative RT-PCR, Transfection, Control, Western Blot, Knock-Out, CRISPR

    Oncogenic functions of the C-terminal truncated p53β protein isoform. A Cell morphology of colorectal cancer cell lines (HCT116 WT and HCT116 p53−/− , DLD-1) and a lung cancer cell line (A549) upon Flag-p53β overexpression. B RT-qPCR analysis of EMT markers, ZEB1 and TWIST mRNAs, in stably Flag-p53β- expressing HCT116 WT and HCT116 p53−/− , and A549 cells. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05; ** p < 0.01. C , D Wound closure assay in stably Flag-p53β-expressing HCT116 WT and HCT116 p53−/− , and A549 cells. Wound closure was measured 48 h after scratching. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05. E , F Matrigel invasion assay using stably Flag-p53β-expressing HCT116 WT and HCT116. p53−/− , and A549 cells. Cells were seeded in the upper chamber of Matrigel-coated transwells. Invaded cells on the bottom surface were counted after 48 h. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05; *** p < 0.001

    Journal: Cell & Bioscience

    Article Title: Regulation of oncogenic C-terminal truncated p53β protein isoform expression by SRSF3–UPF1 splicing and surveillance axis

    doi: 10.1186/s13578-026-01556-5

    Figure Lengend Snippet: Oncogenic functions of the C-terminal truncated p53β protein isoform. A Cell morphology of colorectal cancer cell lines (HCT116 WT and HCT116 p53−/− , DLD-1) and a lung cancer cell line (A549) upon Flag-p53β overexpression. B RT-qPCR analysis of EMT markers, ZEB1 and TWIST mRNAs, in stably Flag-p53β- expressing HCT116 WT and HCT116 p53−/− , and A549 cells. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05; ** p < 0.01. C , D Wound closure assay in stably Flag-p53β-expressing HCT116 WT and HCT116 p53−/− , and A549 cells. Wound closure was measured 48 h after scratching. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05. E , F Matrigel invasion assay using stably Flag-p53β-expressing HCT116 WT and HCT116. p53−/− , and A549 cells. Cells were seeded in the upper chamber of Matrigel-coated transwells. Invaded cells on the bottom surface were counted after 48 h. Data are presented as mean ± SEM (n ≥ 3). * p < 0.05; *** p < 0.001

    Article Snippet: The antibodies used were as follows- anti-UPF1 (Cell Signaling, #12,040), anti-SRSF3 (Invitrogen, #33–4200), anti-FLAG-M2 (Sigma, #F3165), anti-SRSF1 (Thermo Fisher, #32–4500), anti-Histone H3 (Abcam, #ab1791), anti-α-tubulin (Santa Cruz, #sc-8035), anti-β-actin (Abcam, #ab6276), anti-Myc (Sigma, #05-724MG), anti-p53 (Santa Cruz, DO-1 #sc-126; Pab1801 #sc-98; BIORAD, DO-11 #MCA1704), and E-cadherin (Biosciences, #610,181).

    Techniques: Over Expression, Quantitative RT-PCR, Stable Transfection, Expressing, Wound Closure Assay, Invasion Assay

    Biogenesis of p53 mRNAs and functions of p53 protein isoforms. The scheme represents the role of a newly identified intron-retained p53 transcript (p53-IR transcript) in preventing the generation of the C-terminal truncated and pro-metastatic p53β protein. During transcription elongation, SRSF3 associates with the p53-IR transcript and recruits UPF1 forming a transcript surveillance complex. It specifically monitors p53 pre-mRNA and suppress p53β mRNA expression and C-terminal-truncated p53β protein, which promote epithelial–mesenchymal transition (EMT) and metastasis

    Journal: Cell & Bioscience

    Article Title: Regulation of oncogenic C-terminal truncated p53β protein isoform expression by SRSF3–UPF1 splicing and surveillance axis

    doi: 10.1186/s13578-026-01556-5

    Figure Lengend Snippet: Biogenesis of p53 mRNAs and functions of p53 protein isoforms. The scheme represents the role of a newly identified intron-retained p53 transcript (p53-IR transcript) in preventing the generation of the C-terminal truncated and pro-metastatic p53β protein. During transcription elongation, SRSF3 associates with the p53-IR transcript and recruits UPF1 forming a transcript surveillance complex. It specifically monitors p53 pre-mRNA and suppress p53β mRNA expression and C-terminal-truncated p53β protein, which promote epithelial–mesenchymal transition (EMT) and metastasis

    Article Snippet: The antibodies used were as follows- anti-UPF1 (Cell Signaling, #12,040), anti-SRSF3 (Invitrogen, #33–4200), anti-FLAG-M2 (Sigma, #F3165), anti-SRSF1 (Thermo Fisher, #32–4500), anti-Histone H3 (Abcam, #ab1791), anti-α-tubulin (Santa Cruz, #sc-8035), anti-β-actin (Abcam, #ab6276), anti-Myc (Sigma, #05-724MG), anti-p53 (Santa Cruz, DO-1 #sc-126; Pab1801 #sc-98; BIORAD, DO-11 #MCA1704), and E-cadherin (Biosciences, #610,181).

    Techniques: Expressing

    ( A ) Gene ontology enrichment analysis of epithelial clusters (Epi1–Epi5, EMT) using upregulated genes (Log2(FC) > 0.5, adj. p-value > 0.05). Top: Bubble plots showing significant enriched pathways and biological processes, with color intensity representing q-values and bubble size representing the gene ratio (%). Bottom: Schematic representation of the top expressed genes and associated pathways for each cluster. ( B ) Spatial transcriptomic mapping of representative biological pathways across vascularized spheroid sections, illustrating enrichment of negative ferroptosis regulation, G2/M checkpoint activity, IFN-α response, p53 signaling, and EMT programs. ( C ) Schematic of spheroid cultured for 7 days in 3D within the hydrogel region of the OrganiX TM inserts (left), and representative confocal images of C and CSEM spheroid models showing immunofluorescence validation of p53 expression (green: PANC-1; red: p53; blue: DRAQ7 nuclear stain). Scale bar: 200µm. Schematics created in BioRender.com. ( D ) Spatial visualization of p53 transcriptional signature in the CSEM spheroids. Color scale indicates module score for the mentioned gene set. ( E ) Spatial distribution of gene expression for the most significantly enriched biological process of each epithelial cell cluster in vascularized quadri-culture spheroids. Color scale indicates module score for the mentioned gene set.

    Journal: bioRxiv

    Article Title: Multi-omics and functional analysis of a bioengineered vascularized pancreatic cancer model reveal an immunosuppressive and therapy-resistant niche

    doi: 10.64898/2026.03.05.709702

    Figure Lengend Snippet: ( A ) Gene ontology enrichment analysis of epithelial clusters (Epi1–Epi5, EMT) using upregulated genes (Log2(FC) > 0.5, adj. p-value > 0.05). Top: Bubble plots showing significant enriched pathways and biological processes, with color intensity representing q-values and bubble size representing the gene ratio (%). Bottom: Schematic representation of the top expressed genes and associated pathways for each cluster. ( B ) Spatial transcriptomic mapping of representative biological pathways across vascularized spheroid sections, illustrating enrichment of negative ferroptosis regulation, G2/M checkpoint activity, IFN-α response, p53 signaling, and EMT programs. ( C ) Schematic of spheroid cultured for 7 days in 3D within the hydrogel region of the OrganiX TM inserts (left), and representative confocal images of C and CSEM spheroid models showing immunofluorescence validation of p53 expression (green: PANC-1; red: p53; blue: DRAQ7 nuclear stain). Scale bar: 200µm. Schematics created in BioRender.com. ( D ) Spatial visualization of p53 transcriptional signature in the CSEM spheroids. Color scale indicates module score for the mentioned gene set. ( E ) Spatial distribution of gene expression for the most significantly enriched biological process of each epithelial cell cluster in vascularized quadri-culture spheroids. Color scale indicates module score for the mentioned gene set.

    Article Snippet: Upon washing, overnight incubation with mouse anti-human p53 (DO-1) primary antibody (Santa Cruz Biotechnology, Dallas, TX, USA, Cat. no. SC-126) in 1% BSA PBS was performed at 40C.

    Techniques: Activity Assay, Cell Culture, Immunofluorescence, Biomarker Discovery, Expressing, Staining, Gene Expression

    Western blot analyses of lamin A/C and progerin, full-length p53, Δ133p53α, and p21 Waf1/Cip1 were performed in four 15-week-old Δ133p53α-expressing Group-1 mice ( CAG-133 Tam/+ ; Cre Tg/+ ; Lmna G609G/+ ), along with four each of age-matched, non-expressing control Group-2 ( CAG-133 LSL/+ ; Cre Tg/+ ; Lmna G609G/+ ) and Group-4 mice ( CAG-133 +/+ ; Cre +/+ ; Lmna G609G/+ ), as well as two age-matched wild-type mice ( CAG-133 +/+ ; Cre +/+ ; Lmna +/+ ). Results from skin ( a ), skeletal muscle ( b ), kidney ( c ), spleen ( d ), and lung ( e ) are presented. An inter-blot control (liver from a Group-1 mouse) was included in all blots. F, female; M, male. GAPDH was a loading control and used for normalization of p21 Waf1/Cip1 , progerin, and full-length p53 expression levels. Quantitative data summaries of p21 Waf1/Cip1 , progerin, and full-length p53 in Group-1, -2 and -4 mice are shown as relative values to Group-2 mice (mean ± s.d. from n = 4; open circles indicate two females, and closed circles indicate two males). P values were determined by Welch’s t -test. Two wild-type mice were used only as references and not for statistical comparisons.

    Journal: bioRxiv

    Article Title: Senescence-inhibitory Δ133p53α counteracts accelerated ageing and mortality

    doi: 10.64898/2025.12.31.697195

    Figure Lengend Snippet: Western blot analyses of lamin A/C and progerin, full-length p53, Δ133p53α, and p21 Waf1/Cip1 were performed in four 15-week-old Δ133p53α-expressing Group-1 mice ( CAG-133 Tam/+ ; Cre Tg/+ ; Lmna G609G/+ ), along with four each of age-matched, non-expressing control Group-2 ( CAG-133 LSL/+ ; Cre Tg/+ ; Lmna G609G/+ ) and Group-4 mice ( CAG-133 +/+ ; Cre +/+ ; Lmna G609G/+ ), as well as two age-matched wild-type mice ( CAG-133 +/+ ; Cre +/+ ; Lmna +/+ ). Results from skin ( a ), skeletal muscle ( b ), kidney ( c ), spleen ( d ), and lung ( e ) are presented. An inter-blot control (liver from a Group-1 mouse) was included in all blots. F, female; M, male. GAPDH was a loading control and used for normalization of p21 Waf1/Cip1 , progerin, and full-length p53 expression levels. Quantitative data summaries of p21 Waf1/Cip1 , progerin, and full-length p53 in Group-1, -2 and -4 mice are shown as relative values to Group-2 mice (mean ± s.d. from n = 4; open circles indicate two females, and closed circles indicate two males). P values were determined by Welch’s t -test. Two wild-type mice were used only as references and not for statistical comparisons.

    Article Snippet: Primary antibodies used were as follows: anti-p53 antibodies SAPU (sheep polyclonal) and DO-11 (mouse monoclonal; Bio-Rad, MCA1704) ; anti-p21 Waf1/Cip1 (mouse monoclonal; Santa Cruz Biotechnology, sc-6246, clone F-5); anti-lamin A/C (mouse monoclonal; Santa Cruz Biotechnology, sc-376248); anti-GAPDH (mouse monoclonal; Santa Cruz Biotechnology, sc-166574); and anti-β-actin (mouse monoclonal; Thermo Fisher Scientific, MA1-91399).

    Techniques: Western Blot, Expressing, Control

    a,b , Top Hallmark pathways identified by Gene set enrichment analysis (GSEA). The bulk RNA-seq data were obtained from the heart ( a ) and kidney ( b ) in 9-10-month-old Group-1 and Group-3 mice (n = 5 each). Pathways are ranked by normalized enrichment score. False discovery rate < 0.10. c-g, Enrichment plots illustrate significant downregulation of the p53 pathway ( c,d ) and upregulation of the oxidative phosphorylation ( e,f ) in both heart and kidney, as well as upregulation of the glycolysis in the kidney ( g ). Enrichment plots depict running enrichment scores (ES) and the distribution of genes within each Hallmark gene set. All leading edge genes in each pathway are listed in Extended Data Table 2. h,i, qRT-PCR assays of mRNA expression of genes in the oxidative phosphorylation pathway (Ndufs6, Ndufc2, Uqcrq, Hsd17b10, and Gpx4) and an antioxidant gene Prdx1 in the heart ( h ) and kidney ( i ) of 9-10-month-old Group-1 and Group-3 mice (mean ± s.d. from n = 5, each with technical triplicate; open circles, females; closed circles, males). P values were calculated by Welch’s t -test.

    Journal: bioRxiv

    Article Title: Senescence-inhibitory Δ133p53α counteracts accelerated ageing and mortality

    doi: 10.64898/2025.12.31.697195

    Figure Lengend Snippet: a,b , Top Hallmark pathways identified by Gene set enrichment analysis (GSEA). The bulk RNA-seq data were obtained from the heart ( a ) and kidney ( b ) in 9-10-month-old Group-1 and Group-3 mice (n = 5 each). Pathways are ranked by normalized enrichment score. False discovery rate < 0.10. c-g, Enrichment plots illustrate significant downregulation of the p53 pathway ( c,d ) and upregulation of the oxidative phosphorylation ( e,f ) in both heart and kidney, as well as upregulation of the glycolysis in the kidney ( g ). Enrichment plots depict running enrichment scores (ES) and the distribution of genes within each Hallmark gene set. All leading edge genes in each pathway are listed in Extended Data Table 2. h,i, qRT-PCR assays of mRNA expression of genes in the oxidative phosphorylation pathway (Ndufs6, Ndufc2, Uqcrq, Hsd17b10, and Gpx4) and an antioxidant gene Prdx1 in the heart ( h ) and kidney ( i ) of 9-10-month-old Group-1 and Group-3 mice (mean ± s.d. from n = 5, each with technical triplicate; open circles, females; closed circles, males). P values were calculated by Welch’s t -test.

    Article Snippet: Primary antibodies used were as follows: anti-p53 antibodies SAPU (sheep polyclonal) and DO-11 (mouse monoclonal; Bio-Rad, MCA1704) ; anti-p21 Waf1/Cip1 (mouse monoclonal; Santa Cruz Biotechnology, sc-6246, clone F-5); anti-lamin A/C (mouse monoclonal; Santa Cruz Biotechnology, sc-376248); anti-GAPDH (mouse monoclonal; Santa Cruz Biotechnology, sc-166574); and anti-β-actin (mouse monoclonal; Thermo Fisher Scientific, MA1-91399).

    Techniques: RNA Sequencing, Phospho-proteomics, Quantitative RT-PCR, Expressing

    Expression of p53 protein in colorectal cancer and paracancerous intestinal mucosa tissues (200×magnification). ( A ) Negative p53 expression in paracancerous intestinal mucosa tissue. ( B ) Negative p53 expression in colorectal cancer tissue. ( C ) Low expression of p53 in colorectal cancer tissue. ( D ) High expression of p53 in colorectal cancer tissue.

    Journal: Cancer Management and Research

    Article Title: Expression and Significance of PI3K p85α and p53 Protein in Colorectal Cancer Tissues

    doi: 10.2147/CMAR.S565385

    Figure Lengend Snippet: Expression of p53 protein in colorectal cancer and paracancerous intestinal mucosa tissues (200×magnification). ( A ) Negative p53 expression in paracancerous intestinal mucosa tissue. ( B ) Negative p53 expression in colorectal cancer tissue. ( C ) Low expression of p53 in colorectal cancer tissue. ( D ) High expression of p53 in colorectal cancer tissue.

    Article Snippet: The antibodies used included: concentrated rabbit anti-human PI3K p85α polyclonal antibody (clone N2C1, dilution 1:3200, GeneTex, USA), and concentrated mouse anti-human p53 monoclonal antibody (clone DO-7, dilution 1:100, Zhongshan Golden Bridge Biotechnology, China).

    Techniques: Expressing

    The relationship between clinicopathological parameters, PI3K p85α and p53 protein expression and the survival time of CRC patients. ( A ) The effect of the clinical stage on the survival time. ( B ) The effect of the degree of tumor differentiation on the survival time. ( C ) The effect of lymph node metastasis on the survival time. ( D ) The effect of PI3K p85α protein expression on the survival time. ( E ) The effect of p53 protein expression on the survival time.

    Journal: Cancer Management and Research

    Article Title: Expression and Significance of PI3K p85α and p53 Protein in Colorectal Cancer Tissues

    doi: 10.2147/CMAR.S565385

    Figure Lengend Snippet: The relationship between clinicopathological parameters, PI3K p85α and p53 protein expression and the survival time of CRC patients. ( A ) The effect of the clinical stage on the survival time. ( B ) The effect of the degree of tumor differentiation on the survival time. ( C ) The effect of lymph node metastasis on the survival time. ( D ) The effect of PI3K p85α protein expression on the survival time. ( E ) The effect of p53 protein expression on the survival time.

    Article Snippet: The antibodies used included: concentrated rabbit anti-human PI3K p85α polyclonal antibody (clone N2C1, dilution 1:3200, GeneTex, USA), and concentrated mouse anti-human p53 monoclonal antibody (clone DO-7, dilution 1:100, Zhongshan Golden Bridge Biotechnology, China).

    Techniques: Expressing

    Senescence induction in BC cells following OxxySlab lysate treatment. Cell lines were treated with OxxySlab lysate (75–150 μg/mL) for 48 h. Senescent cells were identified by β-galactosidase staining (β-gal). Representative phase-contrast images of T24 ( A ), 5637 ( E ) and SV-HUC-1 ( I ) β-gal-positive cells (blue staining) are shown. Quantification of senescence was performed by measuring the Mean Gray Value of blue staining intensity using ImageJ software, with data expressed as Inverted Mean Gray Value (255 − MGV), which directly reflects β-gal activity. Data are expressed as mean ± SEM of two independent experiments in triplicate. Western blot analysis of the senescence markers p21, p53 and p16 was performed in untreated (CNTR) and OxxySlab -treated T24 ( B – D ), 5637 ( F – H ), and SV-HUC1 ( J – L ) cells. Protein levels were quantified by densitometry, normalized to GAPDH, and expressed as fold change relative to CNTR of three independent experiments (mean ± SEM). Statistical significance was assessed by one-way ANOVA followed by Tukey post hoc test (* p < 0.05, ** p < 0.01).

    Journal: Antioxidants

    Article Title: Exploring the Anticancer Potential of the Multistrain Probiotic Formulation OxxySlab in Bladder Cancer Cell Lines

    doi: 10.3390/antiox14111282

    Figure Lengend Snippet: Senescence induction in BC cells following OxxySlab lysate treatment. Cell lines were treated with OxxySlab lysate (75–150 μg/mL) for 48 h. Senescent cells were identified by β-galactosidase staining (β-gal). Representative phase-contrast images of T24 ( A ), 5637 ( E ) and SV-HUC-1 ( I ) β-gal-positive cells (blue staining) are shown. Quantification of senescence was performed by measuring the Mean Gray Value of blue staining intensity using ImageJ software, with data expressed as Inverted Mean Gray Value (255 − MGV), which directly reflects β-gal activity. Data are expressed as mean ± SEM of two independent experiments in triplicate. Western blot analysis of the senescence markers p21, p53 and p16 was performed in untreated (CNTR) and OxxySlab -treated T24 ( B – D ), 5637 ( F – H ), and SV-HUC1 ( J – L ) cells. Protein levels were quantified by densitometry, normalized to GAPDH, and expressed as fold change relative to CNTR of three independent experiments (mean ± SEM). Statistical significance was assessed by one-way ANOVA followed by Tukey post hoc test (* p < 0.05, ** p < 0.01).

    Article Snippet: Following incubation with 5% non-fat dry milk in Tris-buffered saline for 1 h at room temperature, the membranes were incubated overnight at 4 °C with primary antibodies: goat anti-human vimentin polyclonal antibody (Chemicon International, Temecula, CA, USA; dilution 1:100), mouse anti-human E-cadherin monoclonal antibody (Cell Signaling Technology; dilution 1:1000), rabbit anti-human β-catenin monoclonal antibody (Cell Signaling Technology; dilution 1:1000), rabbit anti-human p21 polyclonal antibody (Santa Cruz Biotechnology, Dallas, TX, USA dilution 1:1000); rabbit anti-human phospho-Nrf2 monoclonal antibody (S40) (1:2000, Abcam, Cambridge, UK); rabbit anti-human p16 polyclonal antibody (Santa Cruz Biotechnology, dilution 1:200); mouse anti-human p53 monoclonal antibody (Santa Cruz Biotechnology, dilution 1:1000); mouse anti-human GAPDH monoclonal antibody (Immunological Sciences, Rome, Italy; dilution 1:1000).

    Techniques: Staining, Software, Activity Assay, Western Blot

    Clusters 0 and 2 were comprised predominantly by wildtype cells. An upregulation of the “HALLMARK_TNFA_SIGNALING_VIA_NFKB” gene set in both Clusters 0 (a) and 2 (b) was observed. In Cluster 0, there was additionally an upregulation of “HALLMARK_ANGIOGENESIS” (c) and “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (d) . In Cluster 2, there was additionally an upregulation of “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (e) , “HALLMARK_KRAS_SIGNALING_UP” (f) , and “HALLMARK_P53_PATHWAY” (g) .

    Journal: PLOS One

    Article Title: STAG2 mutations in the normal colon induce upregulation of oncogenic pathways in neighbouring wildtype cells

    doi: 10.1371/journal.pone.0332499

    Figure Lengend Snippet: Clusters 0 and 2 were comprised predominantly by wildtype cells. An upregulation of the “HALLMARK_TNFA_SIGNALING_VIA_NFKB” gene set in both Clusters 0 (a) and 2 (b) was observed. In Cluster 0, there was additionally an upregulation of “HALLMARK_ANGIOGENESIS” (c) and “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (d) . In Cluster 2, there was additionally an upregulation of “HALLMARK_EPITHELIAL_MESENCHYMAL_TRANSITION” (e) , “HALLMARK_KRAS_SIGNALING_UP” (f) , and “HALLMARK_P53_PATHWAY” (g) .

    Article Snippet: Primary antibodies used included rabbit anti-human STAG2 antibody (1:100, 19837–1-AP, Proteintech, USA), mouse anti-human KI67 antibody (1:500, 66555–6-Ig, Proteintech, USA), mouse anti-human P53 antibody (1:400, 60283–2-Ig, Proteintech, USA), mouse anti-human CCND1 antibody (1:100, 60186–1-Ig, Proteintech, USA), mouse anti-human TERT antibody (1: 100, MA5−16033, Invitrogen, USA), mouse anti-human KRAS antibody (1:250, 415700, Invitrogen, USA), and mouse anti-human TNFα antibody (1:50, MA5−23720, Invitrogen, USA).

    Techniques:

    Fluorescent intensity of anti-TNFα antibody (a, b) , anti-KRAS antibody (c, d) and anti-p53 antibody (e, f) was statistically significantly upregulated in co-cultured wildtype organoids relative STAG2 mutant organoids. Scale bars are 50µm. All experiments were performed with N = 3 biological replicates.

    Journal: PLOS One

    Article Title: STAG2 mutations in the normal colon induce upregulation of oncogenic pathways in neighbouring wildtype cells

    doi: 10.1371/journal.pone.0332499

    Figure Lengend Snippet: Fluorescent intensity of anti-TNFα antibody (a, b) , anti-KRAS antibody (c, d) and anti-p53 antibody (e, f) was statistically significantly upregulated in co-cultured wildtype organoids relative STAG2 mutant organoids. Scale bars are 50µm. All experiments were performed with N = 3 biological replicates.

    Article Snippet: Primary antibodies used included rabbit anti-human STAG2 antibody (1:100, 19837–1-AP, Proteintech, USA), mouse anti-human KI67 antibody (1:500, 66555–6-Ig, Proteintech, USA), mouse anti-human P53 antibody (1:400, 60283–2-Ig, Proteintech, USA), mouse anti-human CCND1 antibody (1:100, 60186–1-Ig, Proteintech, USA), mouse anti-human TERT antibody (1: 100, MA5−16033, Invitrogen, USA), mouse anti-human KRAS antibody (1:250, 415700, Invitrogen, USA), and mouse anti-human TNFα antibody (1:50, MA5−23720, Invitrogen, USA).

    Techniques: Cell Culture, Mutagenesis

    In co-culture, we observed upregulation of TNFα, KRAS and p53 in wildtype organoids, proposing a cooperative mechanism of early oncogenesis.

    Journal: PLOS One

    Article Title: STAG2 mutations in the normal colon induce upregulation of oncogenic pathways in neighbouring wildtype cells

    doi: 10.1371/journal.pone.0332499

    Figure Lengend Snippet: In co-culture, we observed upregulation of TNFα, KRAS and p53 in wildtype organoids, proposing a cooperative mechanism of early oncogenesis.

    Article Snippet: Primary antibodies used included rabbit anti-human STAG2 antibody (1:100, 19837–1-AP, Proteintech, USA), mouse anti-human KI67 antibody (1:500, 66555–6-Ig, Proteintech, USA), mouse anti-human P53 antibody (1:400, 60283–2-Ig, Proteintech, USA), mouse anti-human CCND1 antibody (1:100, 60186–1-Ig, Proteintech, USA), mouse anti-human TERT antibody (1: 100, MA5−16033, Invitrogen, USA), mouse anti-human KRAS antibody (1:250, 415700, Invitrogen, USA), and mouse anti-human TNFα antibody (1:50, MA5−23720, Invitrogen, USA).

    Techniques: Co-Culture Assay