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Rockland Immunochemicals
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Oncogene Science Inc
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Beyotime
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Verlag GmbH
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Merck & Co
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Sangon Biotech
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Boehringer Mannheim
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Progen Biotechnik
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Amersham Life Sciences Inc
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Alpha Diagnostics
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Wanleibio
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Seikagaku corporation
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Image Search Results
Journal: Cell Death & Disease
Article Title: MEIS2 is essential for neuroblastoma cell survival and proliferation by transcriptional control of M-phase progression
doi: 10.1038/cddis.2014.370
Figure Lengend Snippet: MEIS2 is essential for neuroblastoma cell survival. ( a ) Immunoblotting of MEIS2 in a panel of 13 human neuroblastoma cell lines. β -Actin levels are shown as a loading control. ( b and c ) qRT-PCR ( b ) and immunoblot ( c ) analyses of MEIS2 expression in BE(2)-C cells infected with lentiviruses expressing either shGFP or shMEIS2. Error bars ( b ) represent S.D. ( n =3). GAPDH ( c ) serves as a loading control. ( d ) Micrographs of BE(2)-C cells infected for 3 days with lentiviruses expressing either shGFP or shMEIS2. ( e ) Trypan blue exclusion assay of viable BE(2)-C cells infected for 4 days with lentiviruses expressing either shGFP or shMEIS2
Article Snippet: Immunoblotting was conducted according to standard procedures using the following primary antibodies: rabbit anti-BCL2 (sc-783, 1 : 200), rabbit anti-caspase 3 (sc-7148, 1 : 200), rabbit anti-Flag (F7425, 1 : 1000; Sigma-Aldrich), rabbit anti-FOXM1 (sc-502, 1 : 100), rabbit anti-GAPDH (sc-25778, 1 : 3000), mouse anti-MEIS2 (sc-81986, 1 : 400),
Techniques: Western Blot, Quantitative RT-PCR, Expressing, Infection, Trypan Blue Exclusion Assay
Journal: Cell Death & Disease
Article Title: MEIS2 is essential for neuroblastoma cell survival and proliferation by transcriptional control of M-phase progression
doi: 10.1038/cddis.2014.370
Figure Lengend Snippet: MEIS2 targets the MuvB-BMYB-FOXM1 complex for transcriptional control of M-phase progression. ( a ) qRT-PCR analysis of mRNA expression of MEIS2, FOXM1, BMYB, and RBBP4 in BE(2)-C cells infected with lentiviruses expressing either shGFP or shMEIS2. ( b ) Immunoblotting of MEIS2 and FOXM1 in BE(2)-C cells infected with lentiviruses expressing either shGFP or shMEIS2. β -Actin levels are shown as a loading control. MEIS2 and FOXM1 levels were quantified against β -actin. ( c ) GSEA showing marked downregulation of the FOXM1 pathway genes in BE(2)-C cells with MEIS2 depletion. ( d ) ChIP-qPCR analysis showing MEIS2 binding to the FOXM1 promoter region (−312 to −158) containing a consensus TGIF/MEIS2-binding sequence TGTCA. Error bars, S.D. ( n =3). ( e ) Immunoblotting of FOXM1 in BE(2)-C and SK-N-DZ cells with or without FOXM1 knockdown. β -Actin levels are shown as a loading control. ( f ) qRT-PCR analysis of mRNA expression of key FOXM1 target genes in BE(2)-C and SK-N-DZ cells with or without FOXM1 knockdown. ( g ) Growth assay of BE(2)-C and SK-N-DZ cells with or without FOXM1 knockdown. Error bars, S.D. ( n =3). ** P <0.001. Data ( d and g ) were analyzed with two-tailed Student's t -test
Article Snippet: Immunoblotting was conducted according to standard procedures using the following primary antibodies: rabbit anti-BCL2 (sc-783, 1 : 200), rabbit anti-caspase 3 (sc-7148, 1 : 200), rabbit anti-Flag (F7425, 1 : 1000; Sigma-Aldrich), rabbit anti-FOXM1 (sc-502, 1 : 100), rabbit anti-GAPDH (sc-25778, 1 : 3000), mouse anti-MEIS2 (sc-81986, 1 : 400),
Techniques: Quantitative RT-PCR, Expressing, Infection, Western Blot, Binding Assay, Sequencing, Growth Assay, Two Tailed Test
Journal: Asian Biomedicine: Research, Reviews and News
Article Title: An 85-amino-acid polypeptide from Myrmeleon bore larvae (antlions) homologous to heat shock factor binding protein 1 with antiproliferative activity against MG-63 osteosarcoma cells in vitro
doi: 10.2478/abm-2022-0024
Figure Lengend Snippet: Effect of ALAPP on the levels of HSF1, HSP90, CDK4, and AKT1 expression by MG-63 osteosarcoma cells and level of Hsf1, Hsp90, Cdk4, and Akt1 expression by MC3T3 osteoblasts. The levels of protein expression were determined by western blotting. After treatment with 50 μg/mL ALAPP for 48 h, MC3T3 osteoblasts and MG-63 osteosarcoma cells were collected and mixed with 100 μL xTractor Buffer (Clontech). Total cell protein extracts were adjusted to the same protein concentration using the Bradford method, and their protein components were separated by electrophoresis in a 12% polyacrylamide gel containing SDS and transferred to PVDF membranes. Primary antibodies, each with immunoreactivity for human and mouse homologs of the proteins, were purchased from Sangon Biotech, including the rabbit polyclonal antibodies anti-ACTC1 (catalog No. D224905), anti-HSF1 (catalog No. D220782), anti-HSP90AA1 (catalog No. D220009), anti-CDK4 (catalog No. D120396), and anti-AKT1(Ab-129) (catalog No. D151616). Immunoreactivity was detected with secondary antibody HRP-conjugated goat anti-rabbit IgG (catalog No. D110058, Sangon) using an ECL chemiluminescence substrate (catalog No. T7101A, TaKaRa). Expression of the various proteins was calculated relative to β-actin used as a control. Each bar represents the average of n = 3 and error bars indicate standard deviation. Student t tests were conducted to determine differences in expression. * P < 0.05, ** P < 0.005 vs untreated control cells. A . HSF1. B. HSP90. C. CDK4, D. AKT1. ACTC1, β-actin; AKT1, serine-threonine protein kinase encoded by AKT1 ; ALAPP, antlion antiproliferative polypeptide; CDK4, cyclin-dependent kinase 4; HRP, horseradish peroxidase; HSF1, heat shock transcription factor 1; HSP90, heat shock protein 90 kDa alpha (cytosolic), class A member 1 (HSP90AA1); PVDF, polyvinylidene difluoride.
Article Snippet: Primary antibodies, including rabbit polyclonal antibodies to
Techniques: Expressing, Western Blot, Protein Concentration, Electrophoresis, Control, Standard Deviation