p21 Search Results


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  • 99
    Millipore α p21 f5
    α P21 F5, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p 21  (Abcam)
    95
    Abcam p 21
    Effects of AK156230 on cell cycle progression and autophagy in MEFs A. Cell cycle analysis was performed at 48h after transfection in passage 2 cells transfected with the indicated GapmeRs. The percentage of G0/G1, S, and G2/M are demonstrated as shown. B. Western blot analysis of p53, phosphorylated p53, <t>p21,</t> CDK1, CDK2, and Cyclin D1 from MEFs transfected with the indicated GapmeRs for 72h. C. MEFs at passage 2 were transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Western blotting were performed to detect the levels of non-lipidated LC3 (LC3-I) and its lipidated variant (LC3-II). D. Transmission electron microscopy images of MEFs at passage 2 transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Black arrowheads indicate representative autophagosomes or autophagolysosomes, and the nucleus is denoted by N . These sections were examined at 120kV with a JEOL JEM-1400 transmission electron microscope. β-Actin was used as the loading control. All experiments are represented as mean ± SEM from at least there independent experiments. Student's t -test, ** P
    P 21, supplied by Abcam, used in various techniques. Bioz Stars score: 95/100, based on 229 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Bar Harbor BioTechnology p 21
    Effects of AK156230 on cell cycle progression and autophagy in MEFs A. Cell cycle analysis was performed at 48h after transfection in passage 2 cells transfected with the indicated GapmeRs. The percentage of G0/G1, S, and G2/M are demonstrated as shown. B. Western blot analysis of p53, phosphorylated p53, <t>p21,</t> CDK1, CDK2, and Cyclin D1 from MEFs transfected with the indicated GapmeRs for 72h. C. MEFs at passage 2 were transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Western blotting were performed to detect the levels of non-lipidated LC3 (LC3-I) and its lipidated variant (LC3-II). D. Transmission electron microscopy images of MEFs at passage 2 transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Black arrowheads indicate representative autophagosomes or autophagolysosomes, and the nucleus is denoted by N . These sections were examined at 120kV with a JEOL JEM-1400 transmission electron microscope. β-Actin was used as the loading control. All experiments are represented as mean ± SEM from at least there independent experiments. Student's t -test, ** P
    P 21, supplied by Bar Harbor BioTechnology, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Santa Cruz Biotechnology anti p 21 antibody
    Effects of AK156230 on cell cycle progression and autophagy in MEFs A. Cell cycle analysis was performed at 48h after transfection in passage 2 cells transfected with the indicated GapmeRs. The percentage of G0/G1, S, and G2/M are demonstrated as shown. B. Western blot analysis of p53, phosphorylated p53, <t>p21,</t> CDK1, CDK2, and Cyclin D1 from MEFs transfected with the indicated GapmeRs for 72h. C. MEFs at passage 2 were transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Western blotting were performed to detect the levels of non-lipidated LC3 (LC3-I) and its lipidated variant (LC3-II). D. Transmission electron microscopy images of MEFs at passage 2 transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Black arrowheads indicate representative autophagosomes or autophagolysosomes, and the nucleus is denoted by N . These sections were examined at 120kV with a JEOL JEM-1400 transmission electron microscope. β-Actin was used as the loading control. All experiments are represented as mean ± SEM from at least there independent experiments. Student's t -test, ** P
    Anti P 21 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti p 21 antibody/product/Santa Cruz Biotechnology
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    93
    The Jackson Laboratory p 21 c57bl 6j mice
    Effects of AK156230 on cell cycle progression and autophagy in MEFs A. Cell cycle analysis was performed at 48h after transfection in passage 2 cells transfected with the indicated GapmeRs. The percentage of G0/G1, S, and G2/M are demonstrated as shown. B. Western blot analysis of p53, phosphorylated p53, <t>p21,</t> CDK1, CDK2, and Cyclin D1 from MEFs transfected with the indicated GapmeRs for 72h. C. MEFs at passage 2 were transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Western blotting were performed to detect the levels of non-lipidated LC3 (LC3-I) and its lipidated variant (LC3-II). D. Transmission electron microscopy images of MEFs at passage 2 transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Black arrowheads indicate representative autophagosomes or autophagolysosomes, and the nucleus is denoted by N . These sections were examined at 120kV with a JEOL JEM-1400 transmission electron microscope. β-Actin was used as the loading control. All experiments are represented as mean ± SEM from at least there independent experiments. Student's t -test, ** P
    P 21 C57bl 6j Mice, supplied by The Jackson Laboratory, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Schiff Nutrition International p 21 schiff
    Effects of AK156230 on cell cycle progression and autophagy in MEFs A. Cell cycle analysis was performed at 48h after transfection in passage 2 cells transfected with the indicated GapmeRs. The percentage of G0/G1, S, and G2/M are demonstrated as shown. B. Western blot analysis of p53, phosphorylated p53, <t>p21,</t> CDK1, CDK2, and Cyclin D1 from MEFs transfected with the indicated GapmeRs for 72h. C. MEFs at passage 2 were transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Western blotting were performed to detect the levels of non-lipidated LC3 (LC3-I) and its lipidated variant (LC3-II). D. Transmission electron microscopy images of MEFs at passage 2 transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Black arrowheads indicate representative autophagosomes or autophagolysosomes, and the nucleus is denoted by N . These sections were examined at 120kV with a JEOL JEM-1400 transmission electron microscope. β-Actin was used as the loading control. All experiments are represented as mean ± SEM from at least there independent experiments. Student's t -test, ** P
    P 21 Schiff, supplied by Schiff Nutrition International, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Santa Cruz Biotechnology monoclonal anti p 21
    Effects of AK156230 on cell cycle progression and autophagy in MEFs A. Cell cycle analysis was performed at 48h after transfection in passage 2 cells transfected with the indicated GapmeRs. The percentage of G0/G1, S, and G2/M are demonstrated as shown. B. Western blot analysis of p53, phosphorylated p53, <t>p21,</t> CDK1, CDK2, and Cyclin D1 from MEFs transfected with the indicated GapmeRs for 72h. C. MEFs at passage 2 were transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Western blotting were performed to detect the levels of non-lipidated LC3 (LC3-I) and its lipidated variant (LC3-II). D. Transmission electron microscopy images of MEFs at passage 2 transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Black arrowheads indicate representative autophagosomes or autophagolysosomes, and the nucleus is denoted by N . These sections were examined at 120kV with a JEOL JEM-1400 transmission electron microscope. β-Actin was used as the loading control. All experiments are represented as mean ± SEM from at least there independent experiments. Student's t -test, ** P
    Monoclonal Anti P 21, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    FUJIFILM visceral probe p 21
    Effects of AK156230 on cell cycle progression and autophagy in MEFs A. Cell cycle analysis was performed at 48h after transfection in passage 2 cells transfected with the indicated GapmeRs. The percentage of G0/G1, S, and G2/M are demonstrated as shown. B. Western blot analysis of p53, phosphorylated p53, <t>p21,</t> CDK1, CDK2, and Cyclin D1 from MEFs transfected with the indicated GapmeRs for 72h. C. MEFs at passage 2 were transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Western blotting were performed to detect the levels of non-lipidated LC3 (LC3-I) and its lipidated variant (LC3-II). D. Transmission electron microscopy images of MEFs at passage 2 transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Black arrowheads indicate representative autophagosomes or autophagolysosomes, and the nucleus is denoted by N . These sections were examined at 120kV with a JEOL JEM-1400 transmission electron microscope. β-Actin was used as the loading control. All experiments are represented as mean ± SEM from at least there independent experiments. Student's t -test, ** P
    Visceral Probe P 21, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Santa Cruz Biotechnology a p21
    RG7388 upregulates mRNA and protein expression of the p53 pathway. ( a ) MDM2 inhibition with RG7388 increases mRNA expression of p53 transcription targets related to apoptosis in SH-SY5Y (left) and NGP (right) cells. Significant increases with RG7388 treatment is seen for <t>p21,</t> GADD45 (Growth Arrest and DNA Damage genes), PUMA (p53 upregulated modulator of apoptosis), BAX (Bcl-2-associated X protein), and DR5 (death receptor 5) expression in both cell lines by quantitative PCR (* P
    A P21, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Cell Signaling Technology Inc p21
    Losmapimod inhibits gefitinib-induced tetraploidization in gefitinib-resistant NSCLC cells. (A) Cell cycle analysis in untreated gefitinib-resistant NSCLC cells (left, HCC827GR and right, H1975) and in cells treated for 24 h with gefitinib or a p38 MAPK inhibitor (SB203580 or losmapimod) either alone or in combination. Tetraploid subpopulations were analyzed by the ModFit LT V4.0 software program. (B) Western blot analysis of p-YAP, p-MKK3/6 and p-p38 expressions in untreated gefitinib-resistant cells (left, HCC827GR and right, H1975) or cells treated for 2, 6 or 10 h with gefitinib (1 μM) or losmapimod (1 μM) either alone or in combination. Total YAP, MKK3/6 and p38 MAPK proteins were used as loading controls. (C) Western blot analysis of p-STAT3, <t>p21</t> and cyclin D1 expressions in untreated gefitinib-resistant cells (left, HCC827GR and right, H1975) or cells treated for 10 or 24 h with gefitinib (1 μM) or losmapimod (1 μM) either alone or in combination. Total STAT3 and GAPDH proteins were used as loading controls.
    P21, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 5934 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Charles River Laboratories p21
    Losmapimod inhibits gefitinib-induced tetraploidization in gefitinib-resistant NSCLC cells. (A) Cell cycle analysis in untreated gefitinib-resistant NSCLC cells (left, HCC827GR and right, H1975) and in cells treated for 24 h with gefitinib or a p38 MAPK inhibitor (SB203580 or losmapimod) either alone or in combination. Tetraploid subpopulations were analyzed by the ModFit LT V4.0 software program. (B) Western blot analysis of p-YAP, p-MKK3/6 and p-p38 expressions in untreated gefitinib-resistant cells (left, HCC827GR and right, H1975) or cells treated for 2, 6 or 10 h with gefitinib (1 μM) or losmapimod (1 μM) either alone or in combination. Total YAP, MKK3/6 and p38 MAPK proteins were used as loading controls. (C) Western blot analysis of p-STAT3, <t>p21</t> and cyclin D1 expressions in untreated gefitinib-resistant cells (left, HCC827GR and right, H1975) or cells treated for 10 or 24 h with gefitinib (1 μM) or losmapimod (1 μM) either alone or in combination. Total STAT3 and GAPDH proteins were used as loading controls.
    P21, supplied by Charles River Laboratories, used in various techniques. Bioz Stars score: 92/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore p21
    FXR1 involves both <t>p21</t> and TERC RNA to promote senescence. (A) qRT-PCR analyses of RNA levels of UMSCC74B cells transfected with single or combination of p21 overexpression plasmid or si TERC RNA. GAPDH serves as a loading control. (B) Immunoblot of protein expression levels of FXR1 and p21 in UMSCC74B cells transfected independently o r together with p21 overexpression plasmid or si TERC . GAPDH serves as a loading control. (C) Quantification of the western blot shown in Fig 6B. (D) Staining of SA-β-gal in UMSCC74B cells transfected independently or together with p21 overexpression plasmid or si TERC . (E) Quantitative values of MUG conversion to 4-MU by senescence associated β-galactosidase for Fig 6D. (F) SA-β-gal staining of shControl and shFXR1 treated UMSCC74B cells, also co-transduced and/or co-transfected together or independently with shp21 or TERC overexpression plasmid. (G) qRT-PCR analyses of TERC RNA levels in shControl and shFXR1 treated UMSCC74B cells also co-transduced and/or co-transfected together or independently with shp21 or TERC overexpression plasmid. GAPDH serves as a loading control (n = 2). Statistical significance for TERC overexpressing cells from a plasmid-borne copy is not calculated. (H) Immunoblot of protein expression levels of FXR1 and p21 in shControl and shFXR1 treated UMSCC74B cells also co-transduced and/or co-transfected together or independently with shp21 or TERC overexpression plasmid. β-Actin serves as a loading control. (* p
    P21, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1246 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Santa Cruz Biotechnology p21
    SsnB treatment increased p53, <t>p21</t> expression in vitro. A : qRT-PCR analysis of mRNA expression of p53 and p21 from control (untreated), LPS-treated, and LPS+SsnB100 (100 μM) treated Rat primary hepatic stellate cells, normalized against control (*P
    P21, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 8012 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Addgene inc p21 prc cmv p21
    Effects of the overexpression of <t>p21</t> on cell growth in the presence or absence of Zyflamend. CWR22Rv1 cells were transfected with <t>pRc/CMV</t> (empty vector) or pRc/CMV-p21 and treated in the presence or absence of Zyflamend for 24 hr. Relative expression of p21 (protein) is presented in the insert. Following transfection with the empty vector (pRc/CMV) or pRc/CMV-p21 (p21), cells were treated ± Zyflamend for 0–96 hr. Cell proliferation was determined using the MTT assay. Control, open bar, Control + Zyflamend (Zyf), light grey bar; Control + pRc/CMV-p21 (p21), dark grey bar; Zyflamend + pRc/CMV-p21 (p21), black bar. Data are presented as the mean ± SEM. *p
    P21 Prc Cmv P21, supplied by Addgene inc, used in various techniques. Bioz Stars score: 86/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Santa Cruz Biotechnology p 21 antibody
    Effects of the overexpression of <t>p21</t> on cell growth in the presence or absence of Zyflamend. CWR22Rv1 cells were transfected with <t>pRc/CMV</t> (empty vector) or pRc/CMV-p21 and treated in the presence or absence of Zyflamend for 24 hr. Relative expression of p21 (protein) is presented in the insert. Following transfection with the empty vector (pRc/CMV) or pRc/CMV-p21 (p21), cells were treated ± Zyflamend for 0–96 hr. Cell proliferation was determined using the MTT assay. Control, open bar, Control + Zyflamend (Zyf), light grey bar; Control + pRc/CMV-p21 (p21), dark grey bar; Zyflamend + pRc/CMV-p21 (p21), black bar. Data are presented as the mean ± SEM. *p
    P 21 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Becton Dickinson p21
    Increased acetylated tubulin in siRNA NM II-A/II-B–treated HL-1 cells. Immunofluorescence confocal images of B + C + /B + C + HL-1 cells (A–C) and NM II-A/II-B siRNA-treated HL-1 cells (D–F) stained with antibodies to NMHC II-A (A and D, green), <t>p21</t> (A and D, red), acetylated tubulin (B and E, red), activated caspase-3 (C and F, green), and β-tubulin (C and F, red). NMHC II-A is significantly lower in siRNA-treated cells (D, green) compared with controls (A, green). Although the number of p21-positive cells increases after siRNA treatment, the overall expression level of p21 is not obviously different in siRNA-treated individual cells (D) compared with control cells (A). siRNA-treated HL-1 cells show marked increase in acetylated tubulin (E, red) compared with control cells (B, red). siRNA treatment also increases the number of apoptotic cells detected by activated caspase-3 (F, green) compared with control HL-1 cells (C). DAPI (blue) stains the nuclei.
    P21, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 94/100, based on 1771 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Abcam p21 ab109199
    Increased acetylated tubulin in siRNA NM II-A/II-B–treated HL-1 cells. Immunofluorescence confocal images of B + C + /B + C + HL-1 cells (A–C) and NM II-A/II-B siRNA-treated HL-1 cells (D–F) stained with antibodies to NMHC II-A (A and D, green), <t>p21</t> (A and D, red), acetylated tubulin (B and E, red), activated caspase-3 (C and F, green), and β-tubulin (C and F, red). NMHC II-A is significantly lower in siRNA-treated cells (D, green) compared with controls (A, green). Although the number of p21-positive cells increases after siRNA treatment, the overall expression level of p21 is not obviously different in siRNA-treated individual cells (D) compared with control cells (A). siRNA-treated HL-1 cells show marked increase in acetylated tubulin (E, red) compared with control cells (B, red). siRNA treatment also increases the number of apoptotic cells detected by activated caspase-3 (F, green) compared with control HL-1 cells (C). DAPI (blue) stains the nuclei.
    P21 Ab109199, supplied by Abcam, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Santa Cruz Biotechnology p 21 sc 817
    Increased acetylated tubulin in siRNA NM II-A/II-B–treated HL-1 cells. Immunofluorescence confocal images of B + C + /B + C + HL-1 cells (A–C) and NM II-A/II-B siRNA-treated HL-1 cells (D–F) stained with antibodies to NMHC II-A (A and D, green), <t>p21</t> (A and D, red), acetylated tubulin (B and E, red), activated caspase-3 (C and F, green), and β-tubulin (C and F, red). NMHC II-A is significantly lower in siRNA-treated cells (D, green) compared with controls (A, green). Although the number of p21-positive cells increases after siRNA treatment, the overall expression level of p21 is not obviously different in siRNA-treated individual cells (D) compared with control cells (A). siRNA-treated HL-1 cells show marked increase in acetylated tubulin (E, red) compared with control cells (B, red). siRNA treatment also increases the number of apoptotic cells detected by activated caspase-3 (F, green) compared with control HL-1 cells (C). DAPI (blue) stains the nuclei.
    P 21 Sc 817, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Cell Signaling Technology Inc anti p 21
    Increased acetylated tubulin in siRNA NM II-A/II-B–treated HL-1 cells. Immunofluorescence confocal images of B + C + /B + C + HL-1 cells (A–C) and NM II-A/II-B siRNA-treated HL-1 cells (D–F) stained with antibodies to NMHC II-A (A and D, green), <t>p21</t> (A and D, red), acetylated tubulin (B and E, red), activated caspase-3 (C and F, green), and β-tubulin (C and F, red). NMHC II-A is significantly lower in siRNA-treated cells (D, green) compared with controls (A, green). Although the number of p21-positive cells increases after siRNA treatment, the overall expression level of p21 is not obviously different in siRNA-treated individual cells (D) compared with control cells (A). siRNA-treated HL-1 cells show marked increase in acetylated tubulin (E, red) compared with control cells (B, red). siRNA treatment also increases the number of apoptotic cells detected by activated caspase-3 (F, green) compared with control HL-1 cells (C). DAPI (blue) stains the nuclei.
    Anti P 21, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Abcam anti p21 antibody
    MDM2DD inhibited apoptosis and decreased p53 expression in MMTV/ neu tumor. (A–C) Histological patterns of MMTV/ neu (A), MMTV/ neu /MDM2DD (B) and MMTV/ neu /MDM2 (C) tumors. (D–F) Immunohistochemical analysis of MDM2 expressions in MMTV/ neu (D), MMTV/ neu /MDM2DD (E) and MMTV/ neu /MDM2 (F) tumors. (G, H) TUNEL analysis in MMTV/ neu (G) and MMTV/ neu /MDM2DD (H) tumors. Arrows indicated the apoptotic cells. (I, J) Immunohistochemical analysis of p53 expressions in MMTV/ neu (I) and MMTV/ neu /MDM2DD (J) tumors. (K) Apoptotic indices of MMTV/ neu and MMTV/ neu /MDM2DD mammary tumors. (L) Immunoblot analysis of p53, <t>p21</t> and FOXO3a expressions in mammary tumors from MMTV/ neu , MMTV/ neu /MDM2DD and MMTV/ neu /MDM2 mice.
    Anti P21 Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 280 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Durect Corporation p21
    Comparative growth of nicotine-exposed and/or maternally deprived rat pups from P2–P70. The weight trend of male (A, B) and female (C, D) pups from P2–P24 (A, C) and P24–P70 (B, D) is shown. In E, animals were exposed to prenatal and postnatal nicotine (PP-NIC) until <t>P21</t> when they were weaned. MD and MD+NIC significantly reduced animal weight, in the P2–P24 groups compared to CTLs. Please see tables 1 and S1 for significance values.
    P21, supplied by Durect Corporation, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher p21
    Effect of CM on <t>p21</t> and p16 ( A ) Protein levels of p21 were assessed by ELISA. OA chondrocytes were incubated with IL-1β and/or CM for the indicated times. ( B ) p21 mRNA expression was determined by quantitative real-time PCR. OA chondrocytes were incubated with IL-1β and/or CM for 24 hours. ( C ) Protein levels of p16 were assessed by ELISA. OA chondrocytes were incubated with IL-1β and/or CM for the indicated times. ( D ) p16 mRNA expression was determined by quantitative real-time PCR. OA chondrocytes were incubated with IL-1β and/or CM for 24 hours. Data are shown as mean±standard deviation of N=8 separate experiments with cells from separate donors. +p
    P21, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 904 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    InvivoGen p21
    Effect of CM on <t>p21</t> and p16 ( A ) Protein levels of p21 were assessed by ELISA. OA chondrocytes were incubated with IL-1β and/or CM for the indicated times. ( B ) p21 mRNA expression was determined by quantitative real-time PCR. OA chondrocytes were incubated with IL-1β and/or CM for 24 hours. ( C ) Protein levels of p16 were assessed by ELISA. OA chondrocytes were incubated with IL-1β and/or CM for the indicated times. ( D ) p16 mRNA expression was determined by quantitative real-time PCR. OA chondrocytes were incubated with IL-1β and/or CM for 24 hours. Data are shown as mean±standard deviation of N=8 separate experiments with cells from separate donors. +p
    P21, supplied by InvivoGen, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Effects of AK156230 on cell cycle progression and autophagy in MEFs A. Cell cycle analysis was performed at 48h after transfection in passage 2 cells transfected with the indicated GapmeRs. The percentage of G0/G1, S, and G2/M are demonstrated as shown. B. Western blot analysis of p53, phosphorylated p53, p21, CDK1, CDK2, and Cyclin D1 from MEFs transfected with the indicated GapmeRs for 72h. C. MEFs at passage 2 were transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Western blotting were performed to detect the levels of non-lipidated LC3 (LC3-I) and its lipidated variant (LC3-II). D. Transmission electron microscopy images of MEFs at passage 2 transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Black arrowheads indicate representative autophagosomes or autophagolysosomes, and the nucleus is denoted by N . These sections were examined at 120kV with a JEOL JEM-1400 transmission electron microscope. β-Actin was used as the loading control. All experiments are represented as mean ± SEM from at least there independent experiments. Student's t -test, ** P

    Journal: Oncotarget

    Article Title: Identification of the lncRNA, AK156230, as a novel regulator of cellular senescence in mouse embryonic fibroblasts

    doi: 10.18632/oncotarget.10170

    Figure Lengend Snippet: Effects of AK156230 on cell cycle progression and autophagy in MEFs A. Cell cycle analysis was performed at 48h after transfection in passage 2 cells transfected with the indicated GapmeRs. The percentage of G0/G1, S, and G2/M are demonstrated as shown. B. Western blot analysis of p53, phosphorylated p53, p21, CDK1, CDK2, and Cyclin D1 from MEFs transfected with the indicated GapmeRs for 72h. C. MEFs at passage 2 were transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Western blotting were performed to detect the levels of non-lipidated LC3 (LC3-I) and its lipidated variant (LC3-II). D. Transmission electron microscopy images of MEFs at passage 2 transfected with the indicated GapmeRs for 48h, or treated with 3-MA (10mM) for 4h. Black arrowheads indicate representative autophagosomes or autophagolysosomes, and the nucleus is denoted by N . These sections were examined at 120kV with a JEOL JEM-1400 transmission electron microscope. β-Actin was used as the loading control. All experiments are represented as mean ± SEM from at least there independent experiments. Student's t -test, ** P

    Article Snippet: The following primary antibodies were used in this study: p21, CDK1 (Abcam, Cambridge, MA, USA); phosphorylated p53 (Ser 15), p53, CDK2, Cyclin D1, p62 (Cell Signaling Technology, Danvers, MA, USA); LC3B (NOVUS Biologicals, Littleton, CO, USA) and β-actin (Santa Cruz Biotech, Santa Cruz, CA, USA).

    Techniques: Cell Cycle Assay, Transfection, Western Blot, Variant Assay, Transmission Assay, Electron Microscopy, Microscopy

    Rapamycin enhances autophagosome formation and rescues cellular senescence induced by AK156230 knockdown in MEFs A. Western blotting for LC3, p53 and p21 using lysates from the indicated cells. β-Actin was used as the loading control. B. Transmission electron microscopy images of MEFs treated with 2.5μM rapamycin or DMSO for an additional 48h after transfection with control GapmeR control or GapmeR AK156230 for 24h. Black arrowheads indicate representative autophagosomes or autophagolysosomes, and the nucleus is denoted by N . These sections were examined at 120kV with a JEOL JEM-1400 transmission electron microscope. C. Representative images of the SA-β-gal activity staining for the indicated cells. D. Percentage of the indicated cells positive for SA-β-gal activity was shown. Cells were quantitated by randomly choosing at least four independent fields. Student's t -test, ** P

    Journal: Oncotarget

    Article Title: Identification of the lncRNA, AK156230, as a novel regulator of cellular senescence in mouse embryonic fibroblasts

    doi: 10.18632/oncotarget.10170

    Figure Lengend Snippet: Rapamycin enhances autophagosome formation and rescues cellular senescence induced by AK156230 knockdown in MEFs A. Western blotting for LC3, p53 and p21 using lysates from the indicated cells. β-Actin was used as the loading control. B. Transmission electron microscopy images of MEFs treated with 2.5μM rapamycin or DMSO for an additional 48h after transfection with control GapmeR control or GapmeR AK156230 for 24h. Black arrowheads indicate representative autophagosomes or autophagolysosomes, and the nucleus is denoted by N . These sections were examined at 120kV with a JEOL JEM-1400 transmission electron microscope. C. Representative images of the SA-β-gal activity staining for the indicated cells. D. Percentage of the indicated cells positive for SA-β-gal activity was shown. Cells were quantitated by randomly choosing at least four independent fields. Student's t -test, ** P

    Article Snippet: The following primary antibodies were used in this study: p21, CDK1 (Abcam, Cambridge, MA, USA); phosphorylated p53 (Ser 15), p53, CDK2, Cyclin D1, p62 (Cell Signaling Technology, Danvers, MA, USA); LC3B (NOVUS Biologicals, Littleton, CO, USA) and β-actin (Santa Cruz Biotech, Santa Cruz, CA, USA).

    Techniques: Western Blot, Transmission Assay, Electron Microscopy, Transfection, Microscopy, Activity Assay, Staining

    RG7388 upregulates mRNA and protein expression of the p53 pathway. ( a ) MDM2 inhibition with RG7388 increases mRNA expression of p53 transcription targets related to apoptosis in SH-SY5Y (left) and NGP (right) cells. Significant increases with RG7388 treatment is seen for p21, GADD45 (Growth Arrest and DNA Damage genes), PUMA (p53 upregulated modulator of apoptosis), BAX (Bcl-2-associated X protein), and DR5 (death receptor 5) expression in both cell lines by quantitative PCR (* P

    Journal: Cell death discovery

    Article Title: The MDM2 small-molecule inhibitor RG7388 leads to potent tumor inhibition in p53 wild-type neuroblastoma

    doi: 10.1038/cddiscovery.2015.26

    Figure Lengend Snippet: RG7388 upregulates mRNA and protein expression of the p53 pathway. ( a ) MDM2 inhibition with RG7388 increases mRNA expression of p53 transcription targets related to apoptosis in SH-SY5Y (left) and NGP (right) cells. Significant increases with RG7388 treatment is seen for p21, GADD45 (Growth Arrest and DNA Damage genes), PUMA (p53 upregulated modulator of apoptosis), BAX (Bcl-2-associated X protein), and DR5 (death receptor 5) expression in both cell lines by quantitative PCR (* P

    Article Snippet: Antibodies and western blot analysis Primary antibodies for western blot analysis are the following: a-HIF-1α (Millipore, Billerica, MA, USA, Cat 07-1585), a-p53 (Santa Cruz Biotechnology, Dallas, TX, USA, Cat sc-126), a-p21 (Santa Cruz Biotechnology, Cat sc-397), a-MDM2 (Millipore, Cat MABE340), a-PARP (Cell Signaling Technology, Beverly, MA, USA, Cat 9542), and a-CyPB (Santa Cruz Biotechnology, Cat sc-20361).

    Techniques: Expressing, Inhibition, Real-time Polymerase Chain Reaction

    Losmapimod inhibits gefitinib-induced tetraploidization in gefitinib-resistant NSCLC cells. (A) Cell cycle analysis in untreated gefitinib-resistant NSCLC cells (left, HCC827GR and right, H1975) and in cells treated for 24 h with gefitinib or a p38 MAPK inhibitor (SB203580 or losmapimod) either alone or in combination. Tetraploid subpopulations were analyzed by the ModFit LT V4.0 software program. (B) Western blot analysis of p-YAP, p-MKK3/6 and p-p38 expressions in untreated gefitinib-resistant cells (left, HCC827GR and right, H1975) or cells treated for 2, 6 or 10 h with gefitinib (1 μM) or losmapimod (1 μM) either alone or in combination. Total YAP, MKK3/6 and p38 MAPK proteins were used as loading controls. (C) Western blot analysis of p-STAT3, p21 and cyclin D1 expressions in untreated gefitinib-resistant cells (left, HCC827GR and right, H1975) or cells treated for 10 or 24 h with gefitinib (1 μM) or losmapimod (1 μM) either alone or in combination. Total STAT3 and GAPDH proteins were used as loading controls.

    Journal: EBioMedicine

    Article Title: Losmapimod Overcomes Gefitinib Resistance in Non-small Cell Lung Cancer by Preventing Tetraploidization

    doi: 10.1016/j.ebiom.2018.01.017

    Figure Lengend Snippet: Losmapimod inhibits gefitinib-induced tetraploidization in gefitinib-resistant NSCLC cells. (A) Cell cycle analysis in untreated gefitinib-resistant NSCLC cells (left, HCC827GR and right, H1975) and in cells treated for 24 h with gefitinib or a p38 MAPK inhibitor (SB203580 or losmapimod) either alone or in combination. Tetraploid subpopulations were analyzed by the ModFit LT V4.0 software program. (B) Western blot analysis of p-YAP, p-MKK3/6 and p-p38 expressions in untreated gefitinib-resistant cells (left, HCC827GR and right, H1975) or cells treated for 2, 6 or 10 h with gefitinib (1 μM) or losmapimod (1 μM) either alone or in combination. Total YAP, MKK3/6 and p38 MAPK proteins were used as loading controls. (C) Western blot analysis of p-STAT3, p21 and cyclin D1 expressions in untreated gefitinib-resistant cells (left, HCC827GR and right, H1975) or cells treated for 10 or 24 h with gefitinib (1 μM) or losmapimod (1 μM) either alone or in combination. Total STAT3 and GAPDH proteins were used as loading controls.

    Article Snippet: All other antibodies, including phospho-p38 MAPK (Cell Signaling Technology Cat# 9211, RRID: AB_331641 ), p38 MAPK (Cell Signaling Technology Cat# 9212, RRID: AB_330713 ), p38α MAPK (Cell Signaling Technology Cat# 9218S, RRID: AB_10694846 ), p21 (Cell Signaling Technology Cat# 2947S, RRID: AB_823586 ), cyclin D1 (Cell Signaling Technology Cat# 2922, RRID: AB_2228523 ), p-MKK3 (Ser189)/MKK6 (Ser207) (Cell Signaling Technology Cat# 9236S, RRID: AB_491009 ), MKK3 (Cell Signaling Technology Cat# 8535S, RRID: AB_1122023 ), MKK6 (Cell Signaling Technology Cat# 8550S, RRID: AB_1122022 ), p-Stat3 (Tyr705) (Cell Signaling Technology Cat# 9145, RRID: AB_2491009 ), Stat3 (Cell Signaling Technology Cat# 9139, RRID: AB_331757 ), p-YAP (Ser109) (Cell Signaling Technology Cat# 46931), p-YAP (Ser127) (Cell Signaling Technology Cat# 13008, RRID: AB_2650553 ), YAP (Cell Signaling Technology Cat# 14074, RRID: AB_2650491 ) and GAPDH (Cell Signaling Technology Cat# 2118, RRID: AB_561053 ) were purchased from Cell Signaling Technology (Danvers, MA).

    Techniques: Cell Cycle Assay, Software, Western Blot

    FXR1 involves both p21 and TERC RNA to promote senescence. (A) qRT-PCR analyses of RNA levels of UMSCC74B cells transfected with single or combination of p21 overexpression plasmid or si TERC RNA. GAPDH serves as a loading control. (B) Immunoblot of protein expression levels of FXR1 and p21 in UMSCC74B cells transfected independently o r together with p21 overexpression plasmid or si TERC . GAPDH serves as a loading control. (C) Quantification of the western blot shown in Fig 6B. (D) Staining of SA-β-gal in UMSCC74B cells transfected independently or together with p21 overexpression plasmid or si TERC . (E) Quantitative values of MUG conversion to 4-MU by senescence associated β-galactosidase for Fig 6D. (F) SA-β-gal staining of shControl and shFXR1 treated UMSCC74B cells, also co-transduced and/or co-transfected together or independently with shp21 or TERC overexpression plasmid. (G) qRT-PCR analyses of TERC RNA levels in shControl and shFXR1 treated UMSCC74B cells also co-transduced and/or co-transfected together or independently with shp21 or TERC overexpression plasmid. GAPDH serves as a loading control (n = 2). Statistical significance for TERC overexpressing cells from a plasmid-borne copy is not calculated. (H) Immunoblot of protein expression levels of FXR1 and p21 in shControl and shFXR1 treated UMSCC74B cells also co-transduced and/or co-transfected together or independently with shp21 or TERC overexpression plasmid. β-Actin serves as a loading control. (* p

    Journal: PLoS Genetics

    Article Title: RNA-Binding Protein FXR1 Regulates p21 and TERC RNA to Bypass p53-Mediated Cellular Senescence in OSCC

    doi: 10.1371/journal.pgen.1006306

    Figure Lengend Snippet: FXR1 involves both p21 and TERC RNA to promote senescence. (A) qRT-PCR analyses of RNA levels of UMSCC74B cells transfected with single or combination of p21 overexpression plasmid or si TERC RNA. GAPDH serves as a loading control. (B) Immunoblot of protein expression levels of FXR1 and p21 in UMSCC74B cells transfected independently o r together with p21 overexpression plasmid or si TERC . GAPDH serves as a loading control. (C) Quantification of the western blot shown in Fig 6B. (D) Staining of SA-β-gal in UMSCC74B cells transfected independently or together with p21 overexpression plasmid or si TERC . (E) Quantitative values of MUG conversion to 4-MU by senescence associated β-galactosidase for Fig 6D. (F) SA-β-gal staining of shControl and shFXR1 treated UMSCC74B cells, also co-transduced and/or co-transfected together or independently with shp21 or TERC overexpression plasmid. (G) qRT-PCR analyses of TERC RNA levels in shControl and shFXR1 treated UMSCC74B cells also co-transduced and/or co-transfected together or independently with shp21 or TERC overexpression plasmid. GAPDH serves as a loading control (n = 2). Statistical significance for TERC overexpressing cells from a plasmid-borne copy is not calculated. (H) Immunoblot of protein expression levels of FXR1 and p21 in shControl and shFXR1 treated UMSCC74B cells also co-transduced and/or co-transfected together or independently with shp21 or TERC overexpression plasmid. β-Actin serves as a loading control. (* p

    Article Snippet: Different shRNA constructs for FXR1 (TRCN0000158932 and TRCN0000159153) and p21 (TRCN0000287021) were obtained from Sigma Mission.

    Techniques: Quantitative RT-PCR, Transfection, Over Expression, Plasmid Preparation, Expressing, Western Blot, Staining

    Depletion of FXR1 alters cell cycle proteins in HNSCC. (A) Relative quantity of RNAs extracted from control and FXR1 KD cells are estimated by using qRT-PCR. GAPDH serves as a control. (B) Immunoblot analysis of senescence marker proteins in both FXR1 depleted UMSCC74 and 74B cells. β-Actin used as a loading control. (C) Relative quantity of p21 and p53 mRNAs, extracted from shcontrol and shFXR1 treated P53wt and P53mut cells, are estimated by using qRT-PCR. GAPDH serves as a control. (D) Western blot analysis of FXR1 depleted p53Wt and mutant oral cancer cells. GAPDH is used as a loading control. (E) FXR1 depleted p53Wt and mutant oral cancer cells stained with SA-β-gal. (F) Western blot yH2AX expression in UMSCC74A and UMSCC74B cells upon FXR1 KD. (G) Protein lysates of UMSCC74B cells are subjected to RNP IP followed by qRT-PCR analysis to measure the relative quantities of RNAs in FXR1 IP compared with control IgG IP. GAPDH serves as a loading control. (H) RT-PCR of products acquired from inputs and IPs respectively from Mouse IgG as control (Lanes 1, 3) and IP of FXR1 (Lanes 2, 4) were separated and visualized by agarose gel electrophoresis. It clearly shows that p21 mRNA and TERC RNA are enriched in the IP samples, whereas p27 is not. NEB 50bp DNA ladder #N3236S (L) was loaded as a molecular marker. (* p

    Journal: PLoS Genetics

    Article Title: RNA-Binding Protein FXR1 Regulates p21 and TERC RNA to Bypass p53-Mediated Cellular Senescence in OSCC

    doi: 10.1371/journal.pgen.1006306

    Figure Lengend Snippet: Depletion of FXR1 alters cell cycle proteins in HNSCC. (A) Relative quantity of RNAs extracted from control and FXR1 KD cells are estimated by using qRT-PCR. GAPDH serves as a control. (B) Immunoblot analysis of senescence marker proteins in both FXR1 depleted UMSCC74 and 74B cells. β-Actin used as a loading control. (C) Relative quantity of p21 and p53 mRNAs, extracted from shcontrol and shFXR1 treated P53wt and P53mut cells, are estimated by using qRT-PCR. GAPDH serves as a control. (D) Western blot analysis of FXR1 depleted p53Wt and mutant oral cancer cells. GAPDH is used as a loading control. (E) FXR1 depleted p53Wt and mutant oral cancer cells stained with SA-β-gal. (F) Western blot yH2AX expression in UMSCC74A and UMSCC74B cells upon FXR1 KD. (G) Protein lysates of UMSCC74B cells are subjected to RNP IP followed by qRT-PCR analysis to measure the relative quantities of RNAs in FXR1 IP compared with control IgG IP. GAPDH serves as a loading control. (H) RT-PCR of products acquired from inputs and IPs respectively from Mouse IgG as control (Lanes 1, 3) and IP of FXR1 (Lanes 2, 4) were separated and visualized by agarose gel electrophoresis. It clearly shows that p21 mRNA and TERC RNA are enriched in the IP samples, whereas p27 is not. NEB 50bp DNA ladder #N3236S (L) was loaded as a molecular marker. (* p

    Article Snippet: Different shRNA constructs for FXR1 (TRCN0000158932 and TRCN0000159153) and p21 (TRCN0000287021) were obtained from Sigma Mission.

    Techniques: Quantitative RT-PCR, Marker, Western Blot, Mutagenesis, Staining, Expressing, Reverse Transcription Polymerase Chain Reaction, Agarose Gel Electrophoresis

    FXR1-regulated senescence is irreversible. (A) Relative quantity of FXR1 , p21 , and TERC are quantified by qRT-PCR under non-inducible, Inducible and reverse inducible FXR1 silencing conditions in UMSCC74B cells. (B) Immunoblot analysis of protein levels of UMSCC74B cells as described above. (C) The UMSCC74B cells are subjected to SA-β-gal staining as described in Fig 7A. (D) Representative culture dishes from clonogenic assays of cells transfected with indicated conditions. (E) The panel depicts the colony forming efficiency from clonogenic assays of UMSCC74B cells. The data are presented as the means ± S.D. from three independent experiments. (F) Model representation of evasion of cellular senescence through FXR1 by destabilizing p21 and stabilizing TERC in conjunction with activation of p53. (* p

    Journal: PLoS Genetics

    Article Title: RNA-Binding Protein FXR1 Regulates p21 and TERC RNA to Bypass p53-Mediated Cellular Senescence in OSCC

    doi: 10.1371/journal.pgen.1006306

    Figure Lengend Snippet: FXR1-regulated senescence is irreversible. (A) Relative quantity of FXR1 , p21 , and TERC are quantified by qRT-PCR under non-inducible, Inducible and reverse inducible FXR1 silencing conditions in UMSCC74B cells. (B) Immunoblot analysis of protein levels of UMSCC74B cells as described above. (C) The UMSCC74B cells are subjected to SA-β-gal staining as described in Fig 7A. (D) Representative culture dishes from clonogenic assays of cells transfected with indicated conditions. (E) The panel depicts the colony forming efficiency from clonogenic assays of UMSCC74B cells. The data are presented as the means ± S.D. from three independent experiments. (F) Model representation of evasion of cellular senescence through FXR1 by destabilizing p21 and stabilizing TERC in conjunction with activation of p53. (* p

    Article Snippet: Different shRNA constructs for FXR1 (TRCN0000158932 and TRCN0000159153) and p21 (TRCN0000287021) were obtained from Sigma Mission.

    Techniques: Quantitative RT-PCR, Staining, Transfection, Activation Assay

    FXR1 destabilizes p21 mRNA. (A) FISH analysis of p21 in a HNSCC TMA. Green indicates p21 and red denotes the control loci (scale bar 5μm). (B) Relative p21 expression data obtained from cancer genome browser (N-43, T-521) ( S4 Table ). (C) Relative mRNA quantity of p21 in eight matched HNSCC tumor compared to normal adjacent tissue samples estimated using qRT-PCR. GAPDH serves as a control. (D) Immunoblot analysis of p21 protein from eight representative matched HNSCC tumor and normal adjacent samples. GAPDH is used as a loading control. (E) Relative quantity of FXR1 and p21 levels estimated by qRT-PCR in UMSCC74B cells after treatment with FXR1 shRNA. Cells were collected at indicated time points. FXR1 and p21 levels in shControl treated UMSCC74B cells were taken as 1 for each time points. (F) Immunoblot analysis of p21 protein at different time points, as, mentioned in Fig 4E. (G) The mRNA decay rate of p21 as indicated in UMSCC74B cells by qRT-PCR after silencing FXR1 followed by transcription inhibition with actinomycin-D for mentioned time points in the graph. Actin serves as a control. Data here represents the mean of n = 3 experiments. (H) Forty-eight hours after transfection of UM74B FXR1 KD and control cells with empty 3’UTR luciferase plasmid, luciferase-fused GAPDH 3′UTR plasmid or different segments of P21 3′UTR, the lysates were analyzed for luciferase activity using luminometer. The empty 3’UTR luciferase plasmid and luciferase-fused GAPDH 3′UTR served as a transfection and loading control. Values are the means ± SD from three independent experiments by using unpaired two sample t-test. (I) Binding of FXR1 with the 3′UTR of p21seg1 and p21seg2 RNAs at the G4 region. RNP IP was performed 48 h post-transfection of UMSCC74B cells with seg1 and seg2 3′UTR fused to a luciferase reporter construct. Luciferase mRNA was detected using qRT-PCR. The luciferase gene in the empty-3′UTR was used as a transfection and qRT-PCR control. (* p

    Journal: PLoS Genetics

    Article Title: RNA-Binding Protein FXR1 Regulates p21 and TERC RNA to Bypass p53-Mediated Cellular Senescence in OSCC

    doi: 10.1371/journal.pgen.1006306

    Figure Lengend Snippet: FXR1 destabilizes p21 mRNA. (A) FISH analysis of p21 in a HNSCC TMA. Green indicates p21 and red denotes the control loci (scale bar 5μm). (B) Relative p21 expression data obtained from cancer genome browser (N-43, T-521) ( S4 Table ). (C) Relative mRNA quantity of p21 in eight matched HNSCC tumor compared to normal adjacent tissue samples estimated using qRT-PCR. GAPDH serves as a control. (D) Immunoblot analysis of p21 protein from eight representative matched HNSCC tumor and normal adjacent samples. GAPDH is used as a loading control. (E) Relative quantity of FXR1 and p21 levels estimated by qRT-PCR in UMSCC74B cells after treatment with FXR1 shRNA. Cells were collected at indicated time points. FXR1 and p21 levels in shControl treated UMSCC74B cells were taken as 1 for each time points. (F) Immunoblot analysis of p21 protein at different time points, as, mentioned in Fig 4E. (G) The mRNA decay rate of p21 as indicated in UMSCC74B cells by qRT-PCR after silencing FXR1 followed by transcription inhibition with actinomycin-D for mentioned time points in the graph. Actin serves as a control. Data here represents the mean of n = 3 experiments. (H) Forty-eight hours after transfection of UM74B FXR1 KD and control cells with empty 3’UTR luciferase plasmid, luciferase-fused GAPDH 3′UTR plasmid or different segments of P21 3′UTR, the lysates were analyzed for luciferase activity using luminometer. The empty 3’UTR luciferase plasmid and luciferase-fused GAPDH 3′UTR served as a transfection and loading control. Values are the means ± SD from three independent experiments by using unpaired two sample t-test. (I) Binding of FXR1 with the 3′UTR of p21seg1 and p21seg2 RNAs at the G4 region. RNP IP was performed 48 h post-transfection of UMSCC74B cells with seg1 and seg2 3′UTR fused to a luciferase reporter construct. Luciferase mRNA was detected using qRT-PCR. The luciferase gene in the empty-3′UTR was used as a transfection and qRT-PCR control. (* p

    Article Snippet: Different shRNA constructs for FXR1 (TRCN0000158932 and TRCN0000159153) and p21 (TRCN0000287021) were obtained from Sigma Mission.

    Techniques: Fluorescence In Situ Hybridization, Expressing, Quantitative RT-PCR, shRNA, Inhibition, Transfection, Luciferase, Plasmid Preparation, Activity Assay, Binding Assay, Construct

    SsnB treatment increased p53, p21 expression in vitro. A : qRT-PCR analysis of mRNA expression of p53 and p21 from control (untreated), LPS-treated, and LPS+SsnB100 (100 μM) treated Rat primary hepatic stellate cells, normalized against control (*P

    Journal: European journal of pharmacology

    Article Title: Sparstolonin B (SsnB) attenuates liver fibrosis via a parallel conjugate pathway involving P53-P21 axis, TGF-beta signaling and focal adhesion that is TLR4 dependent

    doi: 10.1016/j.ejphar.2018.08.040

    Figure Lengend Snippet: SsnB treatment increased p53, p21 expression in vitro. A : qRT-PCR analysis of mRNA expression of p53 and p21 from control (untreated), LPS-treated, and LPS+SsnB100 (100 μM) treated Rat primary hepatic stellate cells, normalized against control (*P

    Article Snippet: Cells were incubated with α-SMA (Abeam, MA), p53 (CST, Danvers MA), and p21 (Santa cruz Biotechnology, TX) primary antibodies followed by species-specific Alexa Fluor 633 (R) and 488 (G) (described above), for immunofluorescence dual-labeling staining.

    Techniques: Expressing, In Vitro, Quantitative RT-PCR

    SsnB treatment induced PTEN expression increases p53, p21 upregulation and decreases hedgehog signaling in liver. A and B : Representative images of MDM2 (A) and Gli1 (B) immunoreactivity as shown by immunofluorescence microscopy on liver slices of Control, NASH and NASH+SsnB mice, images taken at 20× magnification using immunofluorescence microscopy. C and D : Representative images of p21 (C) and p53 (D) immunoreactivity as shown by immunohistochemistry on liver slices of Control, NASH and NASH+SsnB mice, taken at 20× magnification.

    Journal: European journal of pharmacology

    Article Title: Sparstolonin B (SsnB) attenuates liver fibrosis via a parallel conjugate pathway involving P53-P21 axis, TGF-beta signaling and focal adhesion that is TLR4 dependent

    doi: 10.1016/j.ejphar.2018.08.040

    Figure Lengend Snippet: SsnB treatment induced PTEN expression increases p53, p21 upregulation and decreases hedgehog signaling in liver. A and B : Representative images of MDM2 (A) and Gli1 (B) immunoreactivity as shown by immunofluorescence microscopy on liver slices of Control, NASH and NASH+SsnB mice, images taken at 20× magnification using immunofluorescence microscopy. C and D : Representative images of p21 (C) and p53 (D) immunoreactivity as shown by immunohistochemistry on liver slices of Control, NASH and NASH+SsnB mice, taken at 20× magnification.

    Article Snippet: Cells were incubated with α-SMA (Abeam, MA), p53 (CST, Danvers MA), and p21 (Santa cruz Biotechnology, TX) primary antibodies followed by species-specific Alexa Fluor 633 (R) and 488 (G) (described above), for immunofluorescence dual-labeling staining.

    Techniques: Expressing, Immunofluorescence, Microscopy, Mouse Assay, Immunohistochemistry

    Effects of the overexpression of p21 on cell growth in the presence or absence of Zyflamend. CWR22Rv1 cells were transfected with pRc/CMV (empty vector) or pRc/CMV-p21 and treated in the presence or absence of Zyflamend for 24 hr. Relative expression of p21 (protein) is presented in the insert. Following transfection with the empty vector (pRc/CMV) or pRc/CMV-p21 (p21), cells were treated ± Zyflamend for 0–96 hr. Cell proliferation was determined using the MTT assay. Control, open bar, Control + Zyflamend (Zyf), light grey bar; Control + pRc/CMV-p21 (p21), dark grey bar; Zyflamend + pRc/CMV-p21 (p21), black bar. Data are presented as the mean ± SEM. *p

    Journal: BMC Complementary and Alternative Medicine

    Article Title: Zyflamend, a polyherbal mixture, down regulates class I and class II histone deacetylases and increases p21 levels in castrate-resistant prostate cancer cells

    doi: 10.1186/1472-6882-14-68

    Figure Lengend Snippet: Effects of the overexpression of p21 on cell growth in the presence or absence of Zyflamend. CWR22Rv1 cells were transfected with pRc/CMV (empty vector) or pRc/CMV-p21 and treated in the presence or absence of Zyflamend for 24 hr. Relative expression of p21 (protein) is presented in the insert. Following transfection with the empty vector (pRc/CMV) or pRc/CMV-p21 (p21), cells were treated ± Zyflamend for 0–96 hr. Cell proliferation was determined using the MTT assay. Control, open bar, Control + Zyflamend (Zyf), light grey bar; Control + pRc/CMV-p21 (p21), dark grey bar; Zyflamend + pRc/CMV-p21 (p21), black bar. Data are presented as the mean ± SEM. *p

    Article Snippet: Overexpression of p21 pRc/CMV-p21 (Addgene Inc., Cambridge, MA), containing full length wild-type p21 cDNA, was used to overexpress p21.

    Techniques: Over Expression, Transfection, Plasmid Preparation, Expressing, MTT Assay

    Increased acetylated tubulin in siRNA NM II-A/II-B–treated HL-1 cells. Immunofluorescence confocal images of B + C + /B + C + HL-1 cells (A–C) and NM II-A/II-B siRNA-treated HL-1 cells (D–F) stained with antibodies to NMHC II-A (A and D, green), p21 (A and D, red), acetylated tubulin (B and E, red), activated caspase-3 (C and F, green), and β-tubulin (C and F, red). NMHC II-A is significantly lower in siRNA-treated cells (D, green) compared with controls (A, green). Although the number of p21-positive cells increases after siRNA treatment, the overall expression level of p21 is not obviously different in siRNA-treated individual cells (D) compared with control cells (A). siRNA-treated HL-1 cells show marked increase in acetylated tubulin (E, red) compared with control cells (B, red). siRNA treatment also increases the number of apoptotic cells detected by activated caspase-3 (F, green) compared with control HL-1 cells (C). DAPI (blue) stains the nuclei.

    Journal: Molecular Biology of the Cell

    Article Title: Ablation of Nonmuscle Myosin II-B and II-C Reveals a Role for Nonmuscle Myosin II in Cardiac Myocyte Karyokinesis

    doi: 10.1091/mbc.E10-04-0293

    Figure Lengend Snippet: Increased acetylated tubulin in siRNA NM II-A/II-B–treated HL-1 cells. Immunofluorescence confocal images of B + C + /B + C + HL-1 cells (A–C) and NM II-A/II-B siRNA-treated HL-1 cells (D–F) stained with antibodies to NMHC II-A (A and D, green), p21 (A and D, red), acetylated tubulin (B and E, red), activated caspase-3 (C and F, green), and β-tubulin (C and F, red). NMHC II-A is significantly lower in siRNA-treated cells (D, green) compared with controls (A, green). Although the number of p21-positive cells increases after siRNA treatment, the overall expression level of p21 is not obviously different in siRNA-treated individual cells (D) compared with control cells (A). siRNA-treated HL-1 cells show marked increase in acetylated tubulin (E, red) compared with control cells (B, red). siRNA treatment also increases the number of apoptotic cells detected by activated caspase-3 (F, green) compared with control HL-1 cells (C). DAPI (blue) stains the nuclei.

    Article Snippet: The following primary antibodies were used in this study: rabbit polyclonal antibodies NMHC II-A, II-B, and II-C (IF, 1:1000; ; ); connexin43 (IF, 1:100; Cell Signaling Technology, Danvers, MA); and desmin (IF, 1:200; Abcam, Cambridge, MA); and mouse monoclonal antibodies desmin (IF, 1:200; Dako North America, Carpinteria, CA), MF20 (IF, 1:30; Developmental Studies Hybridoma Bank, University of Iowa, Iowa City, IA), E-cadherin (IF, 1:1000; BD Biosciences, San Jose, CA), N-cadherin (IF, 1:200; Zymed Laboratories, South San Francisco, CA), β-catenin (IF, 1:200; Zymed Laboratories), β-actin (IB, 1:5000; Sigma-Aldrich, St. Louis, MO), β-tubulin (IF, 1:1000; Sigma-Aldrich), acetylated α-tubulin (IF, 1:200; Sigma-Aldrich), γ-tubulin (IF, 1:1000; Sigma-Aldrich), and p21 (IB, 1:500; IF, 1:50; BD Biosciences).

    Techniques: Immunofluorescence, Staining, Expressing

    Increased p21 expression in B − C − /B − C − cardiac myocytes. (A) Immunoblot analysis of p21 expression from 5 and 2 μg of E13.5 mouse heart extracts shows increased expression of p21 in B − C − /B − C − hearts compared with B + C + /B + C + hearts. Actin expression is used as a loading control. (B) Immunofluorescence confocal images of E13.5 heart sections from B + C + /B + C + (a and b) and B − C − /B − C − (c and d) mice stained for p21 (green). DAPI stains the nuclei (blue). B − C − /B − C − cardiac myocytes (large nuclei) but not the nonmyocytes show increased p21 expression (c, green) compared with B + C + /B + C + cardiac myocytes (a, green). Note the multilobed nuclei of B − C − /B − C − cardiac myocytes (d, arrows).

    Journal: Molecular Biology of the Cell

    Article Title: Ablation of Nonmuscle Myosin II-B and II-C Reveals a Role for Nonmuscle Myosin II in Cardiac Myocyte Karyokinesis

    doi: 10.1091/mbc.E10-04-0293

    Figure Lengend Snippet: Increased p21 expression in B − C − /B − C − cardiac myocytes. (A) Immunoblot analysis of p21 expression from 5 and 2 μg of E13.5 mouse heart extracts shows increased expression of p21 in B − C − /B − C − hearts compared with B + C + /B + C + hearts. Actin expression is used as a loading control. (B) Immunofluorescence confocal images of E13.5 heart sections from B + C + /B + C + (a and b) and B − C − /B − C − (c and d) mice stained for p21 (green). DAPI stains the nuclei (blue). B − C − /B − C − cardiac myocytes (large nuclei) but not the nonmyocytes show increased p21 expression (c, green) compared with B + C + /B + C + cardiac myocytes (a, green). Note the multilobed nuclei of B − C − /B − C − cardiac myocytes (d, arrows).

    Article Snippet: The following primary antibodies were used in this study: rabbit polyclonal antibodies NMHC II-A, II-B, and II-C (IF, 1:1000; ; ); connexin43 (IF, 1:100; Cell Signaling Technology, Danvers, MA); and desmin (IF, 1:200; Abcam, Cambridge, MA); and mouse monoclonal antibodies desmin (IF, 1:200; Dako North America, Carpinteria, CA), MF20 (IF, 1:30; Developmental Studies Hybridoma Bank, University of Iowa, Iowa City, IA), E-cadherin (IF, 1:1000; BD Biosciences, San Jose, CA), N-cadherin (IF, 1:200; Zymed Laboratories, South San Francisco, CA), β-catenin (IF, 1:200; Zymed Laboratories), β-actin (IB, 1:5000; Sigma-Aldrich, St. Louis, MO), β-tubulin (IF, 1:1000; Sigma-Aldrich), acetylated α-tubulin (IF, 1:200; Sigma-Aldrich), γ-tubulin (IF, 1:1000; Sigma-Aldrich), and p21 (IB, 1:500; IF, 1:50; BD Biosciences).

    Techniques: Expressing, Immunofluorescence, Mouse Assay, Staining

    MDM2DD inhibited apoptosis and decreased p53 expression in MMTV/ neu tumor. (A–C) Histological patterns of MMTV/ neu (A), MMTV/ neu /MDM2DD (B) and MMTV/ neu /MDM2 (C) tumors. (D–F) Immunohistochemical analysis of MDM2 expressions in MMTV/ neu (D), MMTV/ neu /MDM2DD (E) and MMTV/ neu /MDM2 (F) tumors. (G, H) TUNEL analysis in MMTV/ neu (G) and MMTV/ neu /MDM2DD (H) tumors. Arrows indicated the apoptotic cells. (I, J) Immunohistochemical analysis of p53 expressions in MMTV/ neu (I) and MMTV/ neu /MDM2DD (J) tumors. (K) Apoptotic indices of MMTV/ neu and MMTV/ neu /MDM2DD mammary tumors. (L) Immunoblot analysis of p53, p21 and FOXO3a expressions in mammary tumors from MMTV/ neu , MMTV/ neu /MDM2DD and MMTV/ neu /MDM2 mice.

    Journal: Cancer research

    Article Title: Activation of MDM2 by Akt in Mammary Epithelium Delays Mammary Involution and Accelerates Mammary Tumorigenesis

    doi: 10.1158/0008-5472.CAN-09-3231

    Figure Lengend Snippet: MDM2DD inhibited apoptosis and decreased p53 expression in MMTV/ neu tumor. (A–C) Histological patterns of MMTV/ neu (A), MMTV/ neu /MDM2DD (B) and MMTV/ neu /MDM2 (C) tumors. (D–F) Immunohistochemical analysis of MDM2 expressions in MMTV/ neu (D), MMTV/ neu /MDM2DD (E) and MMTV/ neu /MDM2 (F) tumors. (G, H) TUNEL analysis in MMTV/ neu (G) and MMTV/ neu /MDM2DD (H) tumors. Arrows indicated the apoptotic cells. (I, J) Immunohistochemical analysis of p53 expressions in MMTV/ neu (I) and MMTV/ neu /MDM2DD (J) tumors. (K) Apoptotic indices of MMTV/ neu and MMTV/ neu /MDM2DD mammary tumors. (L) Immunoblot analysis of p53, p21 and FOXO3a expressions in mammary tumors from MMTV/ neu , MMTV/ neu /MDM2DD and MMTV/ neu /MDM2 mice.

    Article Snippet: Primary antibodies used include: rabbit polyclonal anti-MDM2 (N-20; Santa Cruz Biotechnology Inc); rabbit polyclonalanti-p53 (FL-393; Santa Cruz Biotechnology Inc); anti-p53 antibody (FL-393; Santa Cruz Biotechnology Inc); anti-p21 antibody (ab7960; abcam); anti-FOXO3a antibody (H-144; Santa Cruz Biotechnology Inc).

    Techniques: Expressing, Immunohistochemistry, TUNEL Assay, Mouse Assay

    Concomitant treatment with the prodrug Nav‐Gal and cisplatin significantly inhibits tumour growth in a human lung cancer xenograft mouse model. (a) Representative images of A549 xenografts stained for SA‐β‐Gal activity (in blue) after treatment with cisplatin or vehicle. (b) Schematic representation of concomitant treatment on A549 xenograft‐bearing mice. (c) Tumour volume of A549 xenografts in mice concomitantly treated with cisplatin and Navitoclax or Nav‐Gal (as described in (b); n ≥ 10 tumours per group. Data represent mean ± SEM . (d) Representative histological images of tumours at the end of concomitant treatment, stained for Ki67 and p21 expression, and labelled using TUNEL staining. Scale bar = 100 μm. (e) Percentage of Ki67‐ (top), p21‐ (middle) and TUNEL‐positive (bottom) cells in tumours from animals treated with vehicle, cisplatin, or cisplatin and Navitoclax or Nav‐Gal concomitantly ( n ≥ 5 tumours per group). For quantification, a total of 4 fields per tumour was analyzed, covering most of the total tumour area. Two‐way ANOVA followed by Bonferroni post‐tests was performed to calculate the significance of the results; * p

    Journal: Aging Cell

    Article Title: Galacto‐conjugation of Navitoclax as an efficient strategy to increase senolytic specificity and reduce platelet toxicity, et al. Galacto‐conjugation of Navitoclax as an efficient strategy to increase senolytic specificity and reduce platelet toxicity

    doi: 10.1111/acel.13142

    Figure Lengend Snippet: Concomitant treatment with the prodrug Nav‐Gal and cisplatin significantly inhibits tumour growth in a human lung cancer xenograft mouse model. (a) Representative images of A549 xenografts stained for SA‐β‐Gal activity (in blue) after treatment with cisplatin or vehicle. (b) Schematic representation of concomitant treatment on A549 xenograft‐bearing mice. (c) Tumour volume of A549 xenografts in mice concomitantly treated with cisplatin and Navitoclax or Nav‐Gal (as described in (b); n ≥ 10 tumours per group. Data represent mean ± SEM . (d) Representative histological images of tumours at the end of concomitant treatment, stained for Ki67 and p21 expression, and labelled using TUNEL staining. Scale bar = 100 μm. (e) Percentage of Ki67‐ (top), p21‐ (middle) and TUNEL‐positive (bottom) cells in tumours from animals treated with vehicle, cisplatin, or cisplatin and Navitoclax or Nav‐Gal concomitantly ( n ≥ 5 tumours per group). For quantification, a total of 4 fields per tumour was analyzed, covering most of the total tumour area. Two‐way ANOVA followed by Bonferroni post‐tests was performed to calculate the significance of the results; * p

    Article Snippet: For immunohistochemistry, 5 mm paraffin sections were deparaffinized and re‐hydrated, and slides were incubated with anti‐p21 (Abcam) and Ki67 (Abcam) antibodies at 4°C overnight, or processed for TUNEL staining using the DeadEnd™ fluorometric TUNEL System (Promega) as per manufacturer's instructions.

    Techniques: Staining, Activity Assay, Mouse Assay, Expressing, TUNEL Assay

    Comparative growth of nicotine-exposed and/or maternally deprived rat pups from P2–P70. The weight trend of male (A, B) and female (C, D) pups from P2–P24 (A, C) and P24–P70 (B, D) is shown. In E, animals were exposed to prenatal and postnatal nicotine (PP-NIC) until P21 when they were weaned. MD and MD+NIC significantly reduced animal weight, in the P2–P24 groups compared to CTLs. Please see tables 1 and S1 for significance values.

    Journal: PLoS ONE

    Article Title: Prenatal Nicotine and Maternal Deprivation Stress De-Regulate the Development of CA1, CA3, and Dentate Gyrus Neurons in Hippocampus of Infant Rats

    doi: 10.1371/journal.pone.0065517

    Figure Lengend Snippet: Comparative growth of nicotine-exposed and/or maternally deprived rat pups from P2–P70. The weight trend of male (A, B) and female (C, D) pups from P2–P24 (A, C) and P24–P70 (B, D) is shown. In E, animals were exposed to prenatal and postnatal nicotine (PP-NIC) until P21 when they were weaned. MD and MD+NIC significantly reduced animal weight, in the P2–P24 groups compared to CTLs. Please see tables 1 and S1 for significance values.

    Article Snippet: PP-NIC pups were exposed to nursing mothers with nicotine pumps implanted until weaning day, i.e., postnatal day 21 (P21) (Alzet mini-osmotic pump Model #2006).

    Techniques:

    Effect of CM on p21 and p16 ( A ) Protein levels of p21 were assessed by ELISA. OA chondrocytes were incubated with IL-1β and/or CM for the indicated times. ( B ) p21 mRNA expression was determined by quantitative real-time PCR. OA chondrocytes were incubated with IL-1β and/or CM for 24 hours. ( C ) Protein levels of p16 were assessed by ELISA. OA chondrocytes were incubated with IL-1β and/or CM for the indicated times. ( D ) p16 mRNA expression was determined by quantitative real-time PCR. OA chondrocytes were incubated with IL-1β and/or CM for 24 hours. Data are shown as mean±standard deviation of N=8 separate experiments with cells from separate donors. +p

    Journal: Aging (Albany NY)

    Article Title: Paracrine effects of human adipose-derived mesenchymal stem cells in inflammatory stress-induced senescence features of osteoarthritic chondrocytes

    doi: 10.18632/aging.101007

    Figure Lengend Snippet: Effect of CM on p21 and p16 ( A ) Protein levels of p21 were assessed by ELISA. OA chondrocytes were incubated with IL-1β and/or CM for the indicated times. ( B ) p21 mRNA expression was determined by quantitative real-time PCR. OA chondrocytes were incubated with IL-1β and/or CM for 24 hours. ( C ) Protein levels of p16 were assessed by ELISA. OA chondrocytes were incubated with IL-1β and/or CM for the indicated times. ( D ) p16 mRNA expression was determined by quantitative real-time PCR. OA chondrocytes were incubated with IL-1β and/or CM for 24 hours. Data are shown as mean±standard deviation of N=8 separate experiments with cells from separate donors. +p

    Article Snippet: Enzyme-Linked Immunosorbent Assay (ELISA) Several proteins were measured using ELISA kits: p21 (Invitrogen, Barcelona, Spain, with sensitivity of < 5 pg/ml), p16 (YH Biosearch Laboratory, Sanghai, China, with sensitivity of 2.24 ng/ml), Sirt1 (Abnova, Walnut, CA, USA, with sensitivity of 30 pg/ml), HNE-proteins (Cell biolabs, San Diego, CA, USA, with sensitivity of 1.56 μg/ml), and caveolin-1 (ElabScience, BioNova Cientifica S.L., Madrid, Spain, with sensitivity of 188 pg/ml).

    Techniques: Enzyme-linked Immunosorbent Assay, Incubation, Expressing, Real-time Polymerase Chain Reaction, Standard Deviation