p bad 5284 antibodies Search Results


anti phospho bad ser112  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc anti phospho bad ser112
NB upregulated Pim1 expression in NIH3T3 cells. (A) Subcellular localization of NB fusion protein in Di‐NB/NIH3T3. The cells were probed with an anti‐NUP98 antibody and then labeled with Alexa Fluor 568‐conjugated secondary antibody. The nuclei were counterstained with DAPI. (B) A list of 14 upregulated genes with log2 FC >0.58 (fold change>1.5), p adj <0.05, and base mean >50 in Dox‐treated Di‐NB/NIH3T3. (C) Venn diagram showing the overlap of the upregulated genes in NB‐expressing NIH3T3 cells and previously published target promoters of NUP98‐JARID1A and NUP98‐HOXD13. (D) Upregulation of Pim1 in Dox‐treated Di‐NB/NIH3T3. The cells were treated with or without Dox for 72 h, and then total RNA was prepared and analyzed by RT‐qPCR. The values were normalized to the expression levels of Gapdh ( n = 3). Data are presented as the mean ± SEM. * p < 0.05, by two‐tailed Student's t‐ test. (E) Immunoblot analysis of PIM1, p‐BAD <t>(Ser112),</t> and BAD in Di‐NB/NIH3T3. The cells were treated as in Figure . (F) NB bound to the Pim1 promoter. The upper image shows the proximal regulatory region of Pim1 . The lower image shows the results of the ChIP analysis of Di‐NB/NIH3T3. The cells were treated with or without Dox for 48 h to induce NB expression prior to the ChIP assay. Blank (distilled water only); input DNA; H3 (positive control), IgG (negative control), and NUP98 precipitated reactions were amplified with the indicated primer set.
Anti Phospho Bad Ser112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti p bad ser136  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc anti p bad ser136
NB upregulated Pim1 expression in NIH3T3 cells. (A) Subcellular localization of NB fusion protein in Di‐NB/NIH3T3. The cells were probed with an anti‐NUP98 antibody and then labeled with Alexa Fluor 568‐conjugated secondary antibody. The nuclei were counterstained with DAPI. (B) A list of 14 upregulated genes with log2 FC >0.58 (fold change>1.5), p adj <0.05, and base mean >50 in Dox‐treated Di‐NB/NIH3T3. (C) Venn diagram showing the overlap of the upregulated genes in NB‐expressing NIH3T3 cells and previously published target promoters of NUP98‐JARID1A and NUP98‐HOXD13. (D) Upregulation of Pim1 in Dox‐treated Di‐NB/NIH3T3. The cells were treated with or without Dox for 72 h, and then total RNA was prepared and analyzed by RT‐qPCR. The values were normalized to the expression levels of Gapdh ( n = 3). Data are presented as the mean ± SEM. * p < 0.05, by two‐tailed Student's t‐ test. (E) Immunoblot analysis of PIM1, p‐BAD <t>(Ser112),</t> and BAD in Di‐NB/NIH3T3. The cells were treated as in Figure . (F) NB bound to the Pim1 promoter. The upper image shows the proximal regulatory region of Pim1 . The lower image shows the results of the ChIP analysis of Di‐NB/NIH3T3. The cells were treated with or without Dox for 48 h to induce NB expression prior to the ChIP assay. Blank (distilled water only); input DNA; H3 (positive control), IgG (negative control), and NUP98 precipitated reactions were amplified with the indicated primer set.
Anti P Bad Ser136, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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p raf b  (Santa Cruz Biotechnology)
95
Santa Cruz Biotechnology p raf b
NB upregulated Pim1 expression in NIH3T3 cells. (A) Subcellular localization of NB fusion protein in Di‐NB/NIH3T3. The cells were probed with an anti‐NUP98 antibody and then labeled with Alexa Fluor 568‐conjugated secondary antibody. The nuclei were counterstained with DAPI. (B) A list of 14 upregulated genes with log2 FC >0.58 (fold change>1.5), p adj <0.05, and base mean >50 in Dox‐treated Di‐NB/NIH3T3. (C) Venn diagram showing the overlap of the upregulated genes in NB‐expressing NIH3T3 cells and previously published target promoters of NUP98‐JARID1A and NUP98‐HOXD13. (D) Upregulation of Pim1 in Dox‐treated Di‐NB/NIH3T3. The cells were treated with or without Dox for 72 h, and then total RNA was prepared and analyzed by RT‐qPCR. The values were normalized to the expression levels of Gapdh ( n = 3). Data are presented as the mean ± SEM. * p < 0.05, by two‐tailed Student's t‐ test. (E) Immunoblot analysis of PIM1, p‐BAD <t>(Ser112),</t> and BAD in Di‐NB/NIH3T3. The cells were treated as in Figure . (F) NB bound to the Pim1 promoter. The upper image shows the proximal regulatory region of Pim1 . The lower image shows the results of the ChIP analysis of Di‐NB/NIH3T3. The cells were treated with or without Dox for 48 h to induce NB expression prior to the ChIP assay. Blank (distilled water only); input DNA; H3 (positive control), IgG (negative control), and NUP98 precipitated reactions were amplified with the indicated primer set.
P Raf B, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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caspase 3  (Cell Signaling Technology Inc)
99
Cell Signaling Technology Inc caspase 3
NB upregulated Pim1 expression in NIH3T3 cells. (A) Subcellular localization of NB fusion protein in Di‐NB/NIH3T3. The cells were probed with an anti‐NUP98 antibody and then labeled with Alexa Fluor 568‐conjugated secondary antibody. The nuclei were counterstained with DAPI. (B) A list of 14 upregulated genes with log2 FC >0.58 (fold change>1.5), p adj <0.05, and base mean >50 in Dox‐treated Di‐NB/NIH3T3. (C) Venn diagram showing the overlap of the upregulated genes in NB‐expressing NIH3T3 cells and previously published target promoters of NUP98‐JARID1A and NUP98‐HOXD13. (D) Upregulation of Pim1 in Dox‐treated Di‐NB/NIH3T3. The cells were treated with or without Dox for 72 h, and then total RNA was prepared and analyzed by RT‐qPCR. The values were normalized to the expression levels of Gapdh ( n = 3). Data are presented as the mean ± SEM. * p < 0.05, by two‐tailed Student's t‐ test. (E) Immunoblot analysis of PIM1, p‐BAD <t>(Ser112),</t> and BAD in Di‐NB/NIH3T3. The cells were treated as in Figure . (F) NB bound to the Pim1 promoter. The upper image shows the proximal regulatory region of Pim1 . The lower image shows the results of the ChIP analysis of Di‐NB/NIH3T3. The cells were treated with or without Dox for 48 h to induce NB expression prior to the ChIP assay. Blank (distilled water only); input DNA; H3 (positive control), IgG (negative control), and NUP98 precipitated reactions were amplified with the indicated primer set.
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phospho bad s112  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc phospho bad s112
NB upregulated Pim1 expression in NIH3T3 cells. (A) Subcellular localization of NB fusion protein in Di‐NB/NIH3T3. The cells were probed with an anti‐NUP98 antibody and then labeled with Alexa Fluor 568‐conjugated secondary antibody. The nuclei were counterstained with DAPI. (B) A list of 14 upregulated genes with log2 FC >0.58 (fold change>1.5), p adj <0.05, and base mean >50 in Dox‐treated Di‐NB/NIH3T3. (C) Venn diagram showing the overlap of the upregulated genes in NB‐expressing NIH3T3 cells and previously published target promoters of NUP98‐JARID1A and NUP98‐HOXD13. (D) Upregulation of Pim1 in Dox‐treated Di‐NB/NIH3T3. The cells were treated with or without Dox for 72 h, and then total RNA was prepared and analyzed by RT‐qPCR. The values were normalized to the expression levels of Gapdh ( n = 3). Data are presented as the mean ± SEM. * p < 0.05, by two‐tailed Student's t‐ test. (E) Immunoblot analysis of PIM1, p‐BAD <t>(Ser112),</t> and BAD in Di‐NB/NIH3T3. The cells were treated as in Figure . (F) NB bound to the Pim1 promoter. The upper image shows the proximal regulatory region of Pim1 . The lower image shows the results of the ChIP analysis of Di‐NB/NIH3T3. The cells were treated with or without Dox for 48 h to induce NB expression prior to the ChIP assay. Blank (distilled water only); input DNA; H3 (positive control), IgG (negative control), and NUP98 precipitated reactions were amplified with the indicated primer set.
Phospho Bad S112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 95 stars, based on 1 article reviews
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p mek1 t292  (Santa Cruz Biotechnology)
95
Santa Cruz Biotechnology p mek1 t292
A Time-course analysis of p-Raf-1 S338 , p-Raf-1 S259 , <t>p-MEK1</t> <t>T292</t> , p-ERK1/2 T202/Y204 , BRAF and p-BRAF S445 in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. B Dynamics of Raf-1 activation and BRAF inactivation in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. p-Raf-1 S338 band density was normalized to actin and then normalized to t = 6 h. p-BRAF S445 band density was normalized to actin and then normalized to t = 0. C Endogenous interaction between Raf-1 and BRAF in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h or 6 h was examined by co-immunoprecipitation assay. D Western blot analysis of ERK1/2, p-ERK1/2 T202/Y204 , MEK1, p-MEK1 T292 , AKT, p-AKT T308 and β-actin in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h in the presence of L-779450 (20 μM). E HepG2 cells with or without PID1 overexpression upon Raf-1 knockdown were pretreated with Sorafenib (10 μM) for 3 h and then treated with insulin for 0.25 h. Western blot analysis of AKT, p-AKT T308 and β-actin was performed. F Cell apoptosis in HepG2 with or without PID1 overexpression combined with Raf-1 knockdown upon Sorafenib (10 μM) treatment for 24 h was examined by cytometry analysis. Data are expressed as mean ± SD ( n = 3). * p < 0.05; ** p < 0.01; ns not significant.
P Mek1 T292, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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trans-isrib  (Bio-Techne corporation)
99
Bio-Techne corporation trans-isrib
A Time-course analysis of p-Raf-1 S338 , p-Raf-1 S259 , <t>p-MEK1</t> <t>T292</t> , p-ERK1/2 T202/Y204 , BRAF and p-BRAF S445 in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. B Dynamics of Raf-1 activation and BRAF inactivation in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. p-Raf-1 S338 band density was normalized to actin and then normalized to t = 6 h. p-BRAF S445 band density was normalized to actin and then normalized to t = 0. C Endogenous interaction between Raf-1 and BRAF in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h or 6 h was examined by co-immunoprecipitation assay. D Western blot analysis of ERK1/2, p-ERK1/2 T202/Y204 , MEK1, p-MEK1 T292 , AKT, p-AKT T308 and β-actin in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h in the presence of L-779450 (20 μM). E HepG2 cells with or without PID1 overexpression upon Raf-1 knockdown were pretreated with Sorafenib (10 μM) for 3 h and then treated with insulin for 0.25 h. Western blot analysis of AKT, p-AKT T308 and β-actin was performed. F Cell apoptosis in HepG2 with or without PID1 overexpression combined with Raf-1 knockdown upon Sorafenib (10 μM) treatment for 24 h was examined by cytometry analysis. Data are expressed as mean ± SD ( n = 3). * p < 0.05; ** p < 0.01; ns not significant.
Trans Isrib, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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cnrs umr 5284  (Inserm Transfert)
86
Inserm Transfert cnrs umr 5284
A Time-course analysis of p-Raf-1 S338 , p-Raf-1 S259 , <t>p-MEK1</t> <t>T292</t> , p-ERK1/2 T202/Y204 , BRAF and p-BRAF S445 in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. B Dynamics of Raf-1 activation and BRAF inactivation in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. p-Raf-1 S338 band density was normalized to actin and then normalized to t = 6 h. p-BRAF S445 band density was normalized to actin and then normalized to t = 0. C Endogenous interaction between Raf-1 and BRAF in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h or 6 h was examined by co-immunoprecipitation assay. D Western blot analysis of ERK1/2, p-ERK1/2 T202/Y204 , MEK1, p-MEK1 T292 , AKT, p-AKT T308 and β-actin in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h in the presence of L-779450 (20 μM). E HepG2 cells with or without PID1 overexpression upon Raf-1 knockdown were pretreated with Sorafenib (10 μM) for 3 h and then treated with insulin for 0.25 h. Western blot analysis of AKT, p-AKT T308 and β-actin was performed. F Cell apoptosis in HepG2 with or without PID1 overexpression combined with Raf-1 knockdown upon Sorafenib (10 μM) treatment for 24 h was examined by cytometry analysis. Data are expressed as mean ± SD ( n = 3). * p < 0.05; ** p < 0.01; ns not significant.
Cnrs Umr 5284, supplied by Inserm Transfert, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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5284 somamer aptamers  (SomaLogic)
90
SomaLogic 5284 somamer aptamers
A Time-course analysis of p-Raf-1 S338 , p-Raf-1 S259 , <t>p-MEK1</t> <t>T292</t> , p-ERK1/2 T202/Y204 , BRAF and p-BRAF S445 in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. B Dynamics of Raf-1 activation and BRAF inactivation in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. p-Raf-1 S338 band density was normalized to actin and then normalized to t = 6 h. p-BRAF S445 band density was normalized to actin and then normalized to t = 0. C Endogenous interaction between Raf-1 and BRAF in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h or 6 h was examined by co-immunoprecipitation assay. D Western blot analysis of ERK1/2, p-ERK1/2 T202/Y204 , MEK1, p-MEK1 T292 , AKT, p-AKT T308 and β-actin in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h in the presence of L-779450 (20 μM). E HepG2 cells with or without PID1 overexpression upon Raf-1 knockdown were pretreated with Sorafenib (10 μM) for 3 h and then treated with insulin for 0.25 h. Western blot analysis of AKT, p-AKT T308 and β-actin was performed. F Cell apoptosis in HepG2 with or without PID1 overexpression combined with Raf-1 knockdown upon Sorafenib (10 μM) treatment for 24 h was examined by cytometry analysis. Data are expressed as mean ± SD ( n = 3). * p < 0.05; ** p < 0.01; ns not significant.
5284 Somamer Aptamers, supplied by SomaLogic, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pocket refractometer ri 1.3306–1.5284  (ATAGO CO)
90
ATAGO CO pocket refractometer ri 1.3306–1.5284
A Time-course analysis of p-Raf-1 S338 , p-Raf-1 S259 , <t>p-MEK1</t> <t>T292</t> , p-ERK1/2 T202/Y204 , BRAF and p-BRAF S445 in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. B Dynamics of Raf-1 activation and BRAF inactivation in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. p-Raf-1 S338 band density was normalized to actin and then normalized to t = 6 h. p-BRAF S445 band density was normalized to actin and then normalized to t = 0. C Endogenous interaction between Raf-1 and BRAF in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h or 6 h was examined by co-immunoprecipitation assay. D Western blot analysis of ERK1/2, p-ERK1/2 T202/Y204 , MEK1, p-MEK1 T292 , AKT, p-AKT T308 and β-actin in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h in the presence of L-779450 (20 μM). E HepG2 cells with or without PID1 overexpression upon Raf-1 knockdown were pretreated with Sorafenib (10 μM) for 3 h and then treated with insulin for 0.25 h. Western blot analysis of AKT, p-AKT T308 and β-actin was performed. F Cell apoptosis in HepG2 with or without PID1 overexpression combined with Raf-1 knockdown upon Sorafenib (10 μM) treatment for 24 h was examined by cytometry analysis. Data are expressed as mean ± SD ( n = 3). * p < 0.05; ** p < 0.01; ns not significant.
Pocket Refractometer Ri 1.3306–1.5284, supplied by ATAGO CO, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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tnf-a antibody  (ProSci Incorporated)
90
ProSci Incorporated tnf-a antibody
A Time-course analysis of p-Raf-1 S338 , p-Raf-1 S259 , <t>p-MEK1</t> <t>T292</t> , p-ERK1/2 T202/Y204 , BRAF and p-BRAF S445 in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. B Dynamics of Raf-1 activation and BRAF inactivation in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. p-Raf-1 S338 band density was normalized to actin and then normalized to t = 6 h. p-BRAF S445 band density was normalized to actin and then normalized to t = 0. C Endogenous interaction between Raf-1 and BRAF in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h or 6 h was examined by co-immunoprecipitation assay. D Western blot analysis of ERK1/2, p-ERK1/2 T202/Y204 , MEK1, p-MEK1 T292 , AKT, p-AKT T308 and β-actin in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h in the presence of L-779450 (20 μM). E HepG2 cells with or without PID1 overexpression upon Raf-1 knockdown were pretreated with Sorafenib (10 μM) for 3 h and then treated with insulin for 0.25 h. Western blot analysis of AKT, p-AKT T308 and β-actin was performed. F Cell apoptosis in HepG2 with or without PID1 overexpression combined with Raf-1 knockdown upon Sorafenib (10 μM) treatment for 24 h was examined by cytometry analysis. Data are expressed as mean ± SD ( n = 3). * p < 0.05; ** p < 0.01; ns not significant.
Tnf A Antibody, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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trans cinnamic acid d5  (CDN Isotopes)
90
CDN Isotopes trans cinnamic acid d5
A Time-course analysis of p-Raf-1 S338 , p-Raf-1 S259 , <t>p-MEK1</t> <t>T292</t> , p-ERK1/2 T202/Y204 , BRAF and p-BRAF S445 in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. B Dynamics of Raf-1 activation and BRAF inactivation in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. p-Raf-1 S338 band density was normalized to actin and then normalized to t = 6 h. p-BRAF S445 band density was normalized to actin and then normalized to t = 0. C Endogenous interaction between Raf-1 and BRAF in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h or 6 h was examined by co-immunoprecipitation assay. D Western blot analysis of ERK1/2, p-ERK1/2 T202/Y204 , MEK1, p-MEK1 T292 , AKT, p-AKT T308 and β-actin in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h in the presence of L-779450 (20 μM). E HepG2 cells with or without PID1 overexpression upon Raf-1 knockdown were pretreated with Sorafenib (10 μM) for 3 h and then treated with insulin for 0.25 h. Western blot analysis of AKT, p-AKT T308 and β-actin was performed. F Cell apoptosis in HepG2 with or without PID1 overexpression combined with Raf-1 knockdown upon Sorafenib (10 μM) treatment for 24 h was examined by cytometry analysis. Data are expressed as mean ± SD ( n = 3). * p < 0.05; ** p < 0.01; ns not significant.
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Image Search Results


NB upregulated Pim1 expression in NIH3T3 cells. (A) Subcellular localization of NB fusion protein in Di‐NB/NIH3T3. The cells were probed with an anti‐NUP98 antibody and then labeled with Alexa Fluor 568‐conjugated secondary antibody. The nuclei were counterstained with DAPI. (B) A list of 14 upregulated genes with log2 FC >0.58 (fold change>1.5), p adj <0.05, and base mean >50 in Dox‐treated Di‐NB/NIH3T3. (C) Venn diagram showing the overlap of the upregulated genes in NB‐expressing NIH3T3 cells and previously published target promoters of NUP98‐JARID1A and NUP98‐HOXD13. (D) Upregulation of Pim1 in Dox‐treated Di‐NB/NIH3T3. The cells were treated with or without Dox for 72 h, and then total RNA was prepared and analyzed by RT‐qPCR. The values were normalized to the expression levels of Gapdh ( n = 3). Data are presented as the mean ± SEM. * p < 0.05, by two‐tailed Student's t‐ test. (E) Immunoblot analysis of PIM1, p‐BAD (Ser112), and BAD in Di‐NB/NIH3T3. The cells were treated as in Figure . (F) NB bound to the Pim1 promoter. The upper image shows the proximal regulatory region of Pim1 . The lower image shows the results of the ChIP analysis of Di‐NB/NIH3T3. The cells were treated with or without Dox for 48 h to induce NB expression prior to the ChIP assay. Blank (distilled water only); input DNA; H3 (positive control), IgG (negative control), and NUP98 precipitated reactions were amplified with the indicated primer set.

Journal: Cancer Medicine

Article Title: NUP98‐BPTF promotes oncogenic transformation through PIM1 upregulation

doi: 10.1002/cam4.7445

Figure Lengend Snippet: NB upregulated Pim1 expression in NIH3T3 cells. (A) Subcellular localization of NB fusion protein in Di‐NB/NIH3T3. The cells were probed with an anti‐NUP98 antibody and then labeled with Alexa Fluor 568‐conjugated secondary antibody. The nuclei were counterstained with DAPI. (B) A list of 14 upregulated genes with log2 FC >0.58 (fold change>1.5), p adj <0.05, and base mean >50 in Dox‐treated Di‐NB/NIH3T3. (C) Venn diagram showing the overlap of the upregulated genes in NB‐expressing NIH3T3 cells and previously published target promoters of NUP98‐JARID1A and NUP98‐HOXD13. (D) Upregulation of Pim1 in Dox‐treated Di‐NB/NIH3T3. The cells were treated with or without Dox for 72 h, and then total RNA was prepared and analyzed by RT‐qPCR. The values were normalized to the expression levels of Gapdh ( n = 3). Data are presented as the mean ± SEM. * p < 0.05, by two‐tailed Student's t‐ test. (E) Immunoblot analysis of PIM1, p‐BAD (Ser112), and BAD in Di‐NB/NIH3T3. The cells were treated as in Figure . (F) NB bound to the Pim1 promoter. The upper image shows the proximal regulatory region of Pim1 . The lower image shows the results of the ChIP analysis of Di‐NB/NIH3T3. The cells were treated with or without Dox for 48 h to induce NB expression prior to the ChIP assay. Blank (distilled water only); input DNA; H3 (positive control), IgG (negative control), and NUP98 precipitated reactions were amplified with the indicated primer set.

Article Snippet: The membranes were probed with the following primary antibodies: anti‐GAPDH (0411; Santa Cruz Biotechnology, USA), and anti‐NUP98 (#2288; Cell Signaling Technology, USA), anti‐PIM1(12H8; Santa Cruz Biotechnology), anti‐c‐Myc (#5605; Cell Signaling Technology), anti‐Phospho‐c‐Myc (#13748; Cell Signaling Technology), anti‐p70 S6 Kinase (#34475; Cell Signaling Technology), anti‐Phospho‐p70 S6 Kinase (Thr389) (#9234; Cell Signaling Technology), anti‐BAD (#9239; Cell Signaling Technology), and anti‐Phospho‐Bad (Ser112) (#5284; Cell Signaling Technology).

Techniques: Expressing, Labeling, Quantitative RT-PCR, Two Tailed Test, Western Blot, Positive Control, Negative Control, Amplification

NB‐mediated NIH3T3 transformation is dependent on PIM1 expression. (A) Immunoblot analysis of PIM1 and NB after knockdown (KD) of PIM1 in Di‐NB /NIH3T3. The cells were treated as in Figure . (B) Immunoblot analysis of p‐BAD (Ser112) and BAD after KD of PIM1 in Di‐NB /NIH3T3. The cells were treated as in Figure . (C) Suppression of NB‐mediated NIH3T3 cell transformation by PIM1 KD. After 3 weeks of culture, the cells were stained with crystal violet to visualize the foci. (D) Reduced cell numbers of NB‐expressing NIH3T3 cells by PIM1 KD. The cells were counted as in Figure . Data are presented as the mean ± SEM. * p < 0.05, by two‐tailed Student's t‐ test.

Journal: Cancer Medicine

Article Title: NUP98‐BPTF promotes oncogenic transformation through PIM1 upregulation

doi: 10.1002/cam4.7445

Figure Lengend Snippet: NB‐mediated NIH3T3 transformation is dependent on PIM1 expression. (A) Immunoblot analysis of PIM1 and NB after knockdown (KD) of PIM1 in Di‐NB /NIH3T3. The cells were treated as in Figure . (B) Immunoblot analysis of p‐BAD (Ser112) and BAD after KD of PIM1 in Di‐NB /NIH3T3. The cells were treated as in Figure . (C) Suppression of NB‐mediated NIH3T3 cell transformation by PIM1 KD. After 3 weeks of culture, the cells were stained with crystal violet to visualize the foci. (D) Reduced cell numbers of NB‐expressing NIH3T3 cells by PIM1 KD. The cells were counted as in Figure . Data are presented as the mean ± SEM. * p < 0.05, by two‐tailed Student's t‐ test.

Article Snippet: The membranes were probed with the following primary antibodies: anti‐GAPDH (0411; Santa Cruz Biotechnology, USA), and anti‐NUP98 (#2288; Cell Signaling Technology, USA), anti‐PIM1(12H8; Santa Cruz Biotechnology), anti‐c‐Myc (#5605; Cell Signaling Technology), anti‐Phospho‐c‐Myc (#13748; Cell Signaling Technology), anti‐p70 S6 Kinase (#34475; Cell Signaling Technology), anti‐Phospho‐p70 S6 Kinase (Thr389) (#9234; Cell Signaling Technology), anti‐BAD (#9239; Cell Signaling Technology), and anti‐Phospho‐Bad (Ser112) (#5284; Cell Signaling Technology).

Techniques: Transformation Assay, Expressing, Western Blot, Knockdown, Staining, Two Tailed Test

NB decreased serum starvation‐induced apoptosis of human T‐ALL cells. (A) Immunoblot analysis of NB in Di‐NB/Jurkat. Cells were treated as in Figure . (B) Elevated BAD phosphorylation at Ser112 by NB in Di‐NB/Jurkat. The cells were serum‐starved in serum‐free RPMI 1640 medium with or without Dox for 48 h and then lysed for protein extraction. (C, D) Apoptotic cell death decreased by NB in Di‐NB/Jurkat. The cells were treated as in (B), and then the annexin V‐positive cells were scored by flow cytometric analysis ( n = 3). Data are presented as the mean ± SEM. ** p < 0.01, by two‐tailed Student's t‐ test.

Journal: Cancer Medicine

Article Title: NUP98‐BPTF promotes oncogenic transformation through PIM1 upregulation

doi: 10.1002/cam4.7445

Figure Lengend Snippet: NB decreased serum starvation‐induced apoptosis of human T‐ALL cells. (A) Immunoblot analysis of NB in Di‐NB/Jurkat. Cells were treated as in Figure . (B) Elevated BAD phosphorylation at Ser112 by NB in Di‐NB/Jurkat. The cells were serum‐starved in serum‐free RPMI 1640 medium with or without Dox for 48 h and then lysed for protein extraction. (C, D) Apoptotic cell death decreased by NB in Di‐NB/Jurkat. The cells were treated as in (B), and then the annexin V‐positive cells were scored by flow cytometric analysis ( n = 3). Data are presented as the mean ± SEM. ** p < 0.01, by two‐tailed Student's t‐ test.

Article Snippet: The membranes were probed with the following primary antibodies: anti‐GAPDH (0411; Santa Cruz Biotechnology, USA), and anti‐NUP98 (#2288; Cell Signaling Technology, USA), anti‐PIM1(12H8; Santa Cruz Biotechnology), anti‐c‐Myc (#5605; Cell Signaling Technology), anti‐Phospho‐c‐Myc (#13748; Cell Signaling Technology), anti‐p70 S6 Kinase (#34475; Cell Signaling Technology), anti‐Phospho‐p70 S6 Kinase (Thr389) (#9234; Cell Signaling Technology), anti‐BAD (#9239; Cell Signaling Technology), and anti‐Phospho‐Bad (Ser112) (#5284; Cell Signaling Technology).

Techniques: Western Blot, Phospho-proteomics, Protein Extraction, Two Tailed Test

A Time-course analysis of p-Raf-1 S338 , p-Raf-1 S259 , p-MEK1 T292 , p-ERK1/2 T202/Y204 , BRAF and p-BRAF S445 in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. B Dynamics of Raf-1 activation and BRAF inactivation in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. p-Raf-1 S338 band density was normalized to actin and then normalized to t = 6 h. p-BRAF S445 band density was normalized to actin and then normalized to t = 0. C Endogenous interaction between Raf-1 and BRAF in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h or 6 h was examined by co-immunoprecipitation assay. D Western blot analysis of ERK1/2, p-ERK1/2 T202/Y204 , MEK1, p-MEK1 T292 , AKT, p-AKT T308 and β-actin in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h in the presence of L-779450 (20 μM). E HepG2 cells with or without PID1 overexpression upon Raf-1 knockdown were pretreated with Sorafenib (10 μM) for 3 h and then treated with insulin for 0.25 h. Western blot analysis of AKT, p-AKT T308 and β-actin was performed. F Cell apoptosis in HepG2 with or without PID1 overexpression combined with Raf-1 knockdown upon Sorafenib (10 μM) treatment for 24 h was examined by cytometry analysis. Data are expressed as mean ± SD ( n = 3). * p < 0.05; ** p < 0.01; ns not significant.

Journal: Cell Death Discovery

Article Title: Dual role of PID1 in regulating apoptosis induced by distinct anticancer-agents through AKT/Raf-1-dependent pathway in hepatocellular carcinoma

doi: 10.1038/s41420-023-01405-1

Figure Lengend Snippet: A Time-course analysis of p-Raf-1 S338 , p-Raf-1 S259 , p-MEK1 T292 , p-ERK1/2 T202/Y204 , BRAF and p-BRAF S445 in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. B Dynamics of Raf-1 activation and BRAF inactivation in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment. p-Raf-1 S338 band density was normalized to actin and then normalized to t = 6 h. p-BRAF S445 band density was normalized to actin and then normalized to t = 0. C Endogenous interaction between Raf-1 and BRAF in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h or 6 h was examined by co-immunoprecipitation assay. D Western blot analysis of ERK1/2, p-ERK1/2 T202/Y204 , MEK1, p-MEK1 T292 , AKT, p-AKT T308 and β-actin in HepG2 cells with or without PID1 overexpression upon Sorafenib (10 μM) treatment for 3 h in the presence of L-779450 (20 μM). E HepG2 cells with or without PID1 overexpression upon Raf-1 knockdown were pretreated with Sorafenib (10 μM) for 3 h and then treated with insulin for 0.25 h. Western blot analysis of AKT, p-AKT T308 and β-actin was performed. F Cell apoptosis in HepG2 with or without PID1 overexpression combined with Raf-1 knockdown upon Sorafenib (10 μM) treatment for 24 h was examined by cytometry analysis. Data are expressed as mean ± SD ( n = 3). * p < 0.05; ** p < 0.01; ns not significant.

Article Snippet: Antibodies used to determine the protein expression were the following: PID1 (#27951; Signalway Antibody, Greenbelt, Maryland, USA), β-actin (#66009-1-lg; Proteintech, USA), Bcl-xL (#2764; Cell Signaling Technology, USA), Bcl2 (#12789-1-AP; Proteintech), BAD (#sc-8044 Santa Cruz Technology, Texas, USA), p-BAD S112 (#5284; Cell Signaling Technology), p-BAD S136 (#4366; Cell Signaling Technology), cytochrome c (#sc-13156; Santa Cruz Technology), cleaved caspase-3 (#9664; Cell Signaling Technology), Tom20 (#42406; Cell Signaling Technology), Raf-1 (#9422; Cell Signaling Technology), p-Raf-1 S259 (#9421; Cell Signaling Technology), p-Raf-1 S338 (#9427; Cell Signaling Technology), AKT (#4691; Cell Signaling Technology), p-AKT T308 (#13038; Cell Signaling Technology), HA-tag (#sc-7392; Santa Cruz Technology), His-tag (#sc-8036; Santa Cruz Technology), HA-tag (#14793; Cell Signaling Technology), His-tag (#12698; Cell Signal Technology), FLAG-tag (#3724; Cell Signaling Technology), FLAG-tag (#8146; Cell Signaling Technology), ERK1/2 (#4695; Cell Signaling Technology), p-ERK1/2 T202/Y204 (#4370; Cell Signaling Technology), MEK1 (#9122; Cell Signaling Technology), p-MEK1 T292 (#07-852; Upstate, Darmstadt, Germany), BRAF (#sc-5284; Santa Cruz Technology), p-BRAF S445 (#2696; Cell Signaling Technology).

Techniques: Over Expression, Activation Assay, Co-Immunoprecipitation Assay, Western Blot, Cytometry