c2c12 cells Search Results


c2c12  (ATCC)
99
ATCC c2c12
C2c12, supplied by ATCC, 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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c2c12 myoblasts  (CLS Cell Lines Service GmbH)
93
CLS Cell Lines Service GmbH c2c12 myoblasts
A) Epitope mapping of pt IgG4s binding to different parts of human MuSK. B) Sensorgrams of the binding of patient IgG4 to mouse Fz-domain of MuSK in competition with ARGX-119. C) ) Sensorgrams of the binding of patient IgG4 to human Fz-domain of MuSK in competition with ARGX-119. D) Maximum endogenous agonistic potential of patient material on MuSK phosphorylation in <t>C2C12</t> myotubes. Concentration of IgG4 per patient material: Pt 1 293.41 nM, Pt 2 146.75 nM, Pt 3 292.50 nM, Pt 4 293.48 nM. E) Maximum endogenous agonistic potential of patient material on AChR clustering in C2C12 myotubes. Concentration of IgG4 per patient material: Pt 1 730.72 nM, Pt 5.42 nM, Pt 3 34.91 nM and Pt 4 62.94 nM. F) AChR cluster size distribution of each conditions in D. G) Representative images of each condition in D (visualized by BTX488 staining). H) MuSK biobridging assay detecting bivalent MuSK binding antibodies. Data represent mean ± SEM. One-way ANOVA with Tukey multiple comparisons test (C and D). Scale bar: 100 µm.
C2c12 Myoblasts, supplied by CLS Cell Lines Service GmbH, 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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c2c12 cells  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology c2c12 cells
miR-193b decreases activation of Akt by inhibiting PDK1 expression. ( a ) Graphical representation of the conserved miR-193b binding motifs within the 3′-UTR of Pdk1 . Complementary sequences to the seed regions of miR-193b within the 3′-UTRs are conserved between human (Homo) and mouse (Mus) sequences. ( b , c ) <t>C2C12</t> cells were treated with miR-193b mimic or control (Ctrl) RNA and qPCR analysis was used to determine the mRNA level of PDK1 ( n = 5). ** p < 0.01, *** p < 0.001 vs time 0 ( b ) or Ctrl RNA treatment alone ( c ), by one-way ANOVA with Bonferroni correction. ( d ) Luciferase (luc) activity of the reporter constructs containing either wild-type or mutated (MT) 3′-UTR of murine Pdk1 after treatment of C2C12 cells with miR-193b mimic or Ctrl RNA ( n = 5). *** p < 0.001 vs Ctrl RNA treatment alone in the 3′-UTR-transfected group, by one-way ANOVA with Bonferroni correction. ( e ) C2C12 cells were treated with miR-193b mimic (40 nmol/l) or miR-193b inhibitor (100 nmol/l) and the protein level of PDK1, Akt and p-Akt was detected by western blot analysis. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). ( f ) Pdk1 siRNA was transfected into C2C12 cells. Cells were then treated with miR-193b inhibitor or nontargeting negative Ctrl RNA and western blot analysis was used to determine the protein level of PDK1, Akt and p-Akt. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). ( g ) C2C12 cells were treated with DEX alone or with a combination of miR-193b inhibitor and DEX and the protein level of PDK1, Akt and p-Akt was detected by western blot. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). In ( e – g ): * p < 0.05, ** p < 0.01, *** p < 0.001 vs untreated cells, by one-way ANOVA with Bonferroni correction
C2c12 Cells, supplied by Santa Cruz Biotechnology, 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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l6  (ATCC)
96
ATCC l6
miR-193b decreases activation of Akt by inhibiting PDK1 expression. ( a ) Graphical representation of the conserved miR-193b binding motifs within the 3′-UTR of Pdk1 . Complementary sequences to the seed regions of miR-193b within the 3′-UTRs are conserved between human (Homo) and mouse (Mus) sequences. ( b , c ) <t>C2C12</t> cells were treated with miR-193b mimic or control (Ctrl) RNA and qPCR analysis was used to determine the mRNA level of PDK1 ( n = 5). ** p < 0.01, *** p < 0.001 vs time 0 ( b ) or Ctrl RNA treatment alone ( c ), by one-way ANOVA with Bonferroni correction. ( d ) Luciferase (luc) activity of the reporter constructs containing either wild-type or mutated (MT) 3′-UTR of murine Pdk1 after treatment of C2C12 cells with miR-193b mimic or Ctrl RNA ( n = 5). *** p < 0.001 vs Ctrl RNA treatment alone in the 3′-UTR-transfected group, by one-way ANOVA with Bonferroni correction. ( e ) C2C12 cells were treated with miR-193b mimic (40 nmol/l) or miR-193b inhibitor (100 nmol/l) and the protein level of PDK1, Akt and p-Akt was detected by western blot analysis. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). ( f ) Pdk1 siRNA was transfected into C2C12 cells. Cells were then treated with miR-193b inhibitor or nontargeting negative Ctrl RNA and western blot analysis was used to determine the protein level of PDK1, Akt and p-Akt. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). ( g ) C2C12 cells were treated with DEX alone or with a combination of miR-193b inhibitor and DEX and the protein level of PDK1, Akt and p-Akt was detected by western blot. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). In ( e – g ): * p < 0.05, ** p < 0.01, *** p < 0.001 vs untreated cells, by one-way ANOVA with Bonferroni correction
L6, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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c2c12 lysates  (Rockland Immunochemicals)
85
Rockland Immunochemicals c2c12 lysates
Forced expression of NF-YA in differentiated muscle cells inhibits the down-regulation of several cell cycle gene expression and the induction of p21, myogenin, and creatine kinase activity. <t>C2C12</t> cells were transiently transfected with a plasmid carrying NF-YA (+) or the empty vector (–) as indicated. After transfection, cells were grown in the absence of growth factor for 6, 12, 24, or 48 h and lysed to prepare whole cell extract (WCE) (A) and measured creatine kinase activity (B). WCEs from cells cultured in growth medium (GM) and in the absence of growth factor were subjected to Western blot analysis by using antibodies against the indicated proteins. (B) Creatine kinase activity was measured on extracts prepared from transfected and untrasfected cells. Results are the mean ± S.E. of three independent experiments.
C2c12 Lysates, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


A) Epitope mapping of pt IgG4s binding to different parts of human MuSK. B) Sensorgrams of the binding of patient IgG4 to mouse Fz-domain of MuSK in competition with ARGX-119. C) ) Sensorgrams of the binding of patient IgG4 to human Fz-domain of MuSK in competition with ARGX-119. D) Maximum endogenous agonistic potential of patient material on MuSK phosphorylation in C2C12 myotubes. Concentration of IgG4 per patient material: Pt 1 293.41 nM, Pt 2 146.75 nM, Pt 3 292.50 nM, Pt 4 293.48 nM. E) Maximum endogenous agonistic potential of patient material on AChR clustering in C2C12 myotubes. Concentration of IgG4 per patient material: Pt 1 730.72 nM, Pt 5.42 nM, Pt 3 34.91 nM and Pt 4 62.94 nM. F) AChR cluster size distribution of each conditions in D. G) Representative images of each condition in D (visualized by BTX488 staining). H) MuSK biobridging assay detecting bivalent MuSK binding antibodies. Data represent mean ± SEM. One-way ANOVA with Tukey multiple comparisons test (C and D). Scale bar: 100 µm.

Journal: bioRxiv

Article Title: Patient-specific therapeutic benefit of MuSK agonist antibody ARGX-119 in MuSK myasthenia gravis passive transfer models

doi: 10.1101/2024.08.01.606156

Figure Lengend Snippet: A) Epitope mapping of pt IgG4s binding to different parts of human MuSK. B) Sensorgrams of the binding of patient IgG4 to mouse Fz-domain of MuSK in competition with ARGX-119. C) ) Sensorgrams of the binding of patient IgG4 to human Fz-domain of MuSK in competition with ARGX-119. D) Maximum endogenous agonistic potential of patient material on MuSK phosphorylation in C2C12 myotubes. Concentration of IgG4 per patient material: Pt 1 293.41 nM, Pt 2 146.75 nM, Pt 3 292.50 nM, Pt 4 293.48 nM. E) Maximum endogenous agonistic potential of patient material on AChR clustering in C2C12 myotubes. Concentration of IgG4 per patient material: Pt 1 730.72 nM, Pt 5.42 nM, Pt 3 34.91 nM and Pt 4 62.94 nM. F) AChR cluster size distribution of each conditions in D. G) Representative images of each condition in D (visualized by BTX488 staining). H) MuSK biobridging assay detecting bivalent MuSK binding antibodies. Data represent mean ± SEM. One-way ANOVA with Tukey multiple comparisons test (C and D). Scale bar: 100 µm.

Article Snippet: C2C12 myoblasts were obtained from CLS Cell Line Service.

Techniques: Binding Assay, Concentration Assay, Staining

A) Experimental setup of the AChR clustering assay. B) Inhibition potential of patient IgG4 on AChR clustering in C2C12 myotubes. C) Quantification and D) representative images of the therapeutic effect by ARGX-119 (0.1563 nM) on AChR clustering in C2C12 myotubes treated with patient IgG4. Data represent mean ± SEM. Paired t-test was used in C. *P < 0.05, **P < 0.01, ***P < 0.001. Scale bar: 100 µm.

Journal: bioRxiv

Article Title: Patient-specific therapeutic benefit of MuSK agonist antibody ARGX-119 in MuSK myasthenia gravis passive transfer models

doi: 10.1101/2024.08.01.606156

Figure Lengend Snippet: A) Experimental setup of the AChR clustering assay. B) Inhibition potential of patient IgG4 on AChR clustering in C2C12 myotubes. C) Quantification and D) representative images of the therapeutic effect by ARGX-119 (0.1563 nM) on AChR clustering in C2C12 myotubes treated with patient IgG4. Data represent mean ± SEM. Paired t-test was used in C. *P < 0.05, **P < 0.01, ***P < 0.001. Scale bar: 100 µm.

Article Snippet: C2C12 myoblasts were obtained from CLS Cell Line Service.

Techniques: Inhibition

miR-193b decreases activation of Akt by inhibiting PDK1 expression. ( a ) Graphical representation of the conserved miR-193b binding motifs within the 3′-UTR of Pdk1 . Complementary sequences to the seed regions of miR-193b within the 3′-UTRs are conserved between human (Homo) and mouse (Mus) sequences. ( b , c ) C2C12 cells were treated with miR-193b mimic or control (Ctrl) RNA and qPCR analysis was used to determine the mRNA level of PDK1 ( n = 5). ** p < 0.01, *** p < 0.001 vs time 0 ( b ) or Ctrl RNA treatment alone ( c ), by one-way ANOVA with Bonferroni correction. ( d ) Luciferase (luc) activity of the reporter constructs containing either wild-type or mutated (MT) 3′-UTR of murine Pdk1 after treatment of C2C12 cells with miR-193b mimic or Ctrl RNA ( n = 5). *** p < 0.001 vs Ctrl RNA treatment alone in the 3′-UTR-transfected group, by one-way ANOVA with Bonferroni correction. ( e ) C2C12 cells were treated with miR-193b mimic (40 nmol/l) or miR-193b inhibitor (100 nmol/l) and the protein level of PDK1, Akt and p-Akt was detected by western blot analysis. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). ( f ) Pdk1 siRNA was transfected into C2C12 cells. Cells were then treated with miR-193b inhibitor or nontargeting negative Ctrl RNA and western blot analysis was used to determine the protein level of PDK1, Akt and p-Akt. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). ( g ) C2C12 cells were treated with DEX alone or with a combination of miR-193b inhibitor and DEX and the protein level of PDK1, Akt and p-Akt was detected by western blot. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). In ( e – g ): * p < 0.05, ** p < 0.01, *** p < 0.001 vs untreated cells, by one-way ANOVA with Bonferroni correction

Journal: Diabetologia

Article Title: MicroRNA-193b impairs muscle growth in mouse models of type 2 diabetes by targeting the PDK1/Akt signalling pathway

doi: 10.1007/s00125-021-05616-y

Figure Lengend Snippet: miR-193b decreases activation of Akt by inhibiting PDK1 expression. ( a ) Graphical representation of the conserved miR-193b binding motifs within the 3′-UTR of Pdk1 . Complementary sequences to the seed regions of miR-193b within the 3′-UTRs are conserved between human (Homo) and mouse (Mus) sequences. ( b , c ) C2C12 cells were treated with miR-193b mimic or control (Ctrl) RNA and qPCR analysis was used to determine the mRNA level of PDK1 ( n = 5). ** p < 0.01, *** p < 0.001 vs time 0 ( b ) or Ctrl RNA treatment alone ( c ), by one-way ANOVA with Bonferroni correction. ( d ) Luciferase (luc) activity of the reporter constructs containing either wild-type or mutated (MT) 3′-UTR of murine Pdk1 after treatment of C2C12 cells with miR-193b mimic or Ctrl RNA ( n = 5). *** p < 0.001 vs Ctrl RNA treatment alone in the 3′-UTR-transfected group, by one-way ANOVA with Bonferroni correction. ( e ) C2C12 cells were treated with miR-193b mimic (40 nmol/l) or miR-193b inhibitor (100 nmol/l) and the protein level of PDK1, Akt and p-Akt was detected by western blot analysis. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). ( f ) Pdk1 siRNA was transfected into C2C12 cells. Cells were then treated with miR-193b inhibitor or nontargeting negative Ctrl RNA and western blot analysis was used to determine the protein level of PDK1, Akt and p-Akt. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). ( g ) C2C12 cells were treated with DEX alone or with a combination of miR-193b inhibitor and DEX and the protein level of PDK1, Akt and p-Akt was detected by western blot. Quantification of the relative levels of PDK1 and p-Akt proteins is shown ( n = 3). In ( e – g ): * p < 0.05, ** p < 0.01, *** p < 0.001 vs untreated cells, by one-way ANOVA with Bonferroni correction

Article Snippet: C2C12 cells were transfected with 3′ untranslated region (UTR) luciferase reporter constructs ( Pdk1 3′-UTR or Pdk1 3′-UTR-mutant), miRNA (control RNA [catalogue no.: sc-36,869; Santa Cruz Biotechnology] or miR-193b-3p) and Renilla luciferase using Lipofectamine 3000 (Invitrogen).

Techniques: Activation Assay, Expressing, Binding Assay, Luciferase, Activity Assay, Construct, Transfection, Western Blot

Forced expression of NF-YA in differentiated muscle cells inhibits the down-regulation of several cell cycle gene expression and the induction of p21, myogenin, and creatine kinase activity. C2C12 cells were transiently transfected with a plasmid carrying NF-YA (+) or the empty vector (–) as indicated. After transfection, cells were grown in the absence of growth factor for 6, 12, 24, or 48 h and lysed to prepare whole cell extract (WCE) (A) and measured creatine kinase activity (B). WCEs from cells cultured in growth medium (GM) and in the absence of growth factor were subjected to Western blot analysis by using antibodies against the indicated proteins. (B) Creatine kinase activity was measured on extracts prepared from transfected and untrasfected cells. Results are the mean ± S.E. of three independent experiments.

Journal:

Article Title: Requirement for Down-Regulation of the CCAAT-binding Activity of the NF-Y Transcription Factor during Skeletal Muscle Differentiation

doi: 10.1091/mbc.E02-09-0600

Figure Lengend Snippet: Forced expression of NF-YA in differentiated muscle cells inhibits the down-regulation of several cell cycle gene expression and the induction of p21, myogenin, and creatine kinase activity. C2C12 cells were transiently transfected with a plasmid carrying NF-YA (+) or the empty vector (–) as indicated. After transfection, cells were grown in the absence of growth factor for 6, 12, 24, or 48 h and lysed to prepare whole cell extract (WCE) (A) and measured creatine kinase activity (B). WCEs from cells cultured in growth medium (GM) and in the absence of growth factor were subjected to Western blot analysis by using antibodies against the indicated proteins. (B) Creatine kinase activity was measured on extracts prepared from transfected and untrasfected cells. Results are the mean ± S.E. of three independent experiments.

Article Snippet: The filters containing C2C12 lysates were immunoreacted with 0.3 μg/ml anti-NF-YA rabbit polyclonal antibody (Rockland), 0.1 μg/ml anti-cyclin B1 rabbit polyclonal antibody, 0.1 μg/ml anti-cyclin A rabbit polyclonal antibody, 0.1 μg/ml anti-cdk1 p34 rabbit polyclonal antibody, 1 μg/ml anti-myogenin rabbit polyclonal antibody (Santa Cruz Biotechnology, Santa Cruz, CA), 1:500 anti-mouse p21 (kindly provided by C. Schneider, Laboratorio Nazionale CIB, Trieste, Italy), rabbit polyclonal antibody 0.25 μg/ml anti-Hsp70 mouse mAb (StressGen, Biotechnologies), following the manufacturer's directions.

Techniques: Expressing, Activity Assay, Transfection, Plasmid Preparation, Cell Culture, Western Blot

Cyclin B2 and cyclin A promoters are devoid of sequence-specific transcription factor interactions in differentiated cells. Genomic footprinting of the coding strand of the mouse cyclin B2 and the noncoding strand of the mouse cyclin A promoters from P and TD C2C12 cells. As a control, the DMS reactivity for DNA purified from asynchronous C2C12 cells is shown (in vitro). The CCAAT boxes are indicated.

Journal:

Article Title: Requirement for Down-Regulation of the CCAAT-binding Activity of the NF-Y Transcription Factor during Skeletal Muscle Differentiation

doi: 10.1091/mbc.E02-09-0600

Figure Lengend Snippet: Cyclin B2 and cyclin A promoters are devoid of sequence-specific transcription factor interactions in differentiated cells. Genomic footprinting of the coding strand of the mouse cyclin B2 and the noncoding strand of the mouse cyclin A promoters from P and TD C2C12 cells. As a control, the DMS reactivity for DNA purified from asynchronous C2C12 cells is shown (in vitro). The CCAAT boxes are indicated.

Article Snippet: The filters containing C2C12 lysates were immunoreacted with 0.3 μg/ml anti-NF-YA rabbit polyclonal antibody (Rockland), 0.1 μg/ml anti-cyclin B1 rabbit polyclonal antibody, 0.1 μg/ml anti-cyclin A rabbit polyclonal antibody, 0.1 μg/ml anti-cdk1 p34 rabbit polyclonal antibody, 1 μg/ml anti-myogenin rabbit polyclonal antibody (Santa Cruz Biotechnology, Santa Cruz, CA), 1:500 anti-mouse p21 (kindly provided by C. Schneider, Laboratorio Nazionale CIB, Trieste, Italy), rabbit polyclonal antibody 0.25 μg/ml anti-Hsp70 mouse mAb (StressGen, Biotechnologies), following the manufacturer's directions.

Techniques: Sequencing, Footprinting, Purification, In Vitro

Promoter activities of NF-Y cell cycle target genes are down-regulated in differentiated muscle cells. CAT or Luc-reporter constructs carrying the cyclin B1, cdk1, cyclin A, cyclin B2, cdc25A, cdc25C, and cyclin E promoters were stably transfected by calcium-phosphate in C2C12 cells. The obtained polyclonal cell lines were analyzed for CAT or luciferase activity. The values in TD cells are expressed, on the y-axis, as percentages of the CAT or luciferase activity obtained from proliferating cells (100%). Results represent one typical experiment performed in triplicate.

Journal:

Article Title: Requirement for Down-Regulation of the CCAAT-binding Activity of the NF-Y Transcription Factor during Skeletal Muscle Differentiation

doi: 10.1091/mbc.E02-09-0600

Figure Lengend Snippet: Promoter activities of NF-Y cell cycle target genes are down-regulated in differentiated muscle cells. CAT or Luc-reporter constructs carrying the cyclin B1, cdk1, cyclin A, cyclin B2, cdc25A, cdc25C, and cyclin E promoters were stably transfected by calcium-phosphate in C2C12 cells. The obtained polyclonal cell lines were analyzed for CAT or luciferase activity. The values in TD cells are expressed, on the y-axis, as percentages of the CAT or luciferase activity obtained from proliferating cells (100%). Results represent one typical experiment performed in triplicate.

Article Snippet: The filters containing C2C12 lysates were immunoreacted with 0.3 μg/ml anti-NF-YA rabbit polyclonal antibody (Rockland), 0.1 μg/ml anti-cyclin B1 rabbit polyclonal antibody, 0.1 μg/ml anti-cyclin A rabbit polyclonal antibody, 0.1 μg/ml anti-cdk1 p34 rabbit polyclonal antibody, 1 μg/ml anti-myogenin rabbit polyclonal antibody (Santa Cruz Biotechnology, Santa Cruz, CA), 1:500 anti-mouse p21 (kindly provided by C. Schneider, Laboratorio Nazionale CIB, Trieste, Italy), rabbit polyclonal antibody 0.25 μg/ml anti-Hsp70 mouse mAb (StressGen, Biotechnologies), following the manufacturer's directions.

Techniques: Construct, Stable Transfection, Transfection, Luciferase, Activity Assay

NF-YA does not directly modulate the transcriptional activity of p21 and myogenin promoters. Eighty nanograms of a vector carrying p21 promoter (A) and 2 μg of a vector carrying myogenin promoter (B) have been transiently cotransfected in proliferating C2C12 cells together with the same amount of the empty vector or vector expressing wild-type or mutant (YA13m29) NF-YA proteins. As positive control, vector carrying p21 promoter has been cotransfected with an eukaryotic vector expressing p53 protein, and the luciferase activity of the vector carrying myogenin promoter has been measured in low-serum (1%) growth condition. As internal control of transfection efficiency, all samples have been cotransfected with the CMVβgal reporter construct. Values are the means ± standard deviations of four independent experiments.

Journal:

Article Title: Requirement for Down-Regulation of the CCAAT-binding Activity of the NF-Y Transcription Factor during Skeletal Muscle Differentiation

doi: 10.1091/mbc.E02-09-0600

Figure Lengend Snippet: NF-YA does not directly modulate the transcriptional activity of p21 and myogenin promoters. Eighty nanograms of a vector carrying p21 promoter (A) and 2 μg of a vector carrying myogenin promoter (B) have been transiently cotransfected in proliferating C2C12 cells together with the same amount of the empty vector or vector expressing wild-type or mutant (YA13m29) NF-YA proteins. As positive control, vector carrying p21 promoter has been cotransfected with an eukaryotic vector expressing p53 protein, and the luciferase activity of the vector carrying myogenin promoter has been measured in low-serum (1%) growth condition. As internal control of transfection efficiency, all samples have been cotransfected with the CMVβgal reporter construct. Values are the means ± standard deviations of four independent experiments.

Article Snippet: The filters containing C2C12 lysates were immunoreacted with 0.3 μg/ml anti-NF-YA rabbit polyclonal antibody (Rockland), 0.1 μg/ml anti-cyclin B1 rabbit polyclonal antibody, 0.1 μg/ml anti-cyclin A rabbit polyclonal antibody, 0.1 μg/ml anti-cdk1 p34 rabbit polyclonal antibody, 1 μg/ml anti-myogenin rabbit polyclonal antibody (Santa Cruz Biotechnology, Santa Cruz, CA), 1:500 anti-mouse p21 (kindly provided by C. Schneider, Laboratorio Nazionale CIB, Trieste, Italy), rabbit polyclonal antibody 0.25 μg/ml anti-Hsp70 mouse mAb (StressGen, Biotechnologies), following the manufacturer's directions.

Techniques: Activity Assay, Plasmid Preparation, Expressing, Mutagenesis, Positive Control, Luciferase, Transfection, Construct