polyclonal anti rabbit cdc2 p34  (Santa Cruz Biotechnology)

 
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    Santa Cruz Biotechnology polyclonal anti rabbit cdc2 p34
    Polyclonal Anti Rabbit Cdc2 P34, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal anti rabbit cdc2 p34/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    polyclonal anti rabbit cdc2 p34 - by Bioz Stars, 2023-11
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    polyclonal rabbit anti cdk1  (Santa Cruz Biotechnology)

     
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    Santa Cruz Biotechnology polyclonal rabbit anti cdk1
    Analysis of expression of E2F1 and its transcriptional target genes in intact and injured spinal cord were performed by western blotting. A . 5-mm-long segment centered at the injury epicenter was dissected and homogenized in RIPA buffer. Equal amounts of protein were electrophoretically separated on NuPAGE Novex Bis-Tris gradient gels, transferred to nitrocellulose membranes, and blotted with antibodies to E2F1 and <t>CDK1.</t> GAPDH signal served as a loading control. B–C . The signal quantifications for E2F1 (B) and CDK1 (C) using Gel-Pro Analyzer software are displayed. E2F1 and CDK1 expression level was upregulated as early as 15 min and sustained until 3 days after injury. D–E . Cyclin A expression was increased at all time points. F . Bim and c-Myb, downstream targets of E2F1 were upregulated as early as 5 h post-injury and sustained until day 3 after SCI. G–H . Quantification of respective western blots in panel D. N = 4 rats/time point. *P<0.05 vs sham group.
    Polyclonal Rabbit Anti Cdk1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal rabbit anti cdk1/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    polyclonal rabbit anti cdk1 - by Bioz Stars, 2023-11
    86/100 stars

    Images

    1) Product Images from "Inhibition of E2F1/CDK1 Pathway Attenuates Neuronal Apoptosis In Vitro and Confers Neuroprotection after Spinal Cord Injury In Vivo"

    Article Title: Inhibition of E2F1/CDK1 Pathway Attenuates Neuronal Apoptosis In Vitro and Confers Neuroprotection after Spinal Cord Injury In Vivo

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0042129

    Analysis of expression of E2F1 and its transcriptional target genes in intact and injured spinal cord were performed by western blotting. A . 5-mm-long segment centered at the injury epicenter was dissected and homogenized in RIPA buffer. Equal amounts of protein were electrophoretically separated on NuPAGE Novex Bis-Tris gradient gels, transferred to nitrocellulose membranes, and blotted with antibodies to E2F1 and CDK1. GAPDH signal served as a loading control. B–C . The signal quantifications for E2F1 (B) and CDK1 (C) using Gel-Pro Analyzer software are displayed. E2F1 and CDK1 expression level was upregulated as early as 15 min and sustained until 3 days after injury. D–E . Cyclin A expression was increased at all time points. F . Bim and c-Myb, downstream targets of E2F1 were upregulated as early as 5 h post-injury and sustained until day 3 after SCI. G–H . Quantification of respective western blots in panel D. N = 4 rats/time point. *P<0.05 vs sham group.
    Figure Legend Snippet: Analysis of expression of E2F1 and its transcriptional target genes in intact and injured spinal cord were performed by western blotting. A . 5-mm-long segment centered at the injury epicenter was dissected and homogenized in RIPA buffer. Equal amounts of protein were electrophoretically separated on NuPAGE Novex Bis-Tris gradient gels, transferred to nitrocellulose membranes, and blotted with antibodies to E2F1 and CDK1. GAPDH signal served as a loading control. B–C . The signal quantifications for E2F1 (B) and CDK1 (C) using Gel-Pro Analyzer software are displayed. E2F1 and CDK1 expression level was upregulated as early as 15 min and sustained until 3 days after injury. D–E . Cyclin A expression was increased at all time points. F . Bim and c-Myb, downstream targets of E2F1 were upregulated as early as 5 h post-injury and sustained until day 3 after SCI. G–H . Quantification of respective western blots in panel D. N = 4 rats/time point. *P<0.05 vs sham group.

    Techniques Used: Expressing, Western Blot, Software

    Western blotting analysis of common CDK substrates, CDK1 co-activator cyclin B1 and phosphorylations of specific CDK1 substrate (Ser54)-n-myc was performed in homogenates obtained from intact and injured spinal cord. A . Cyclin B1 expression was upregulated at all time points tested. Phosphorylation (Ser54) of n-myc and phospho-CDK substrate motif signal levels were increased from 5 h to day 7. B–D . Quantification of respective western blots in panel A. n = 4 rats/time point. *P<0.05 vs sham group.
    Figure Legend Snippet: Western blotting analysis of common CDK substrates, CDK1 co-activator cyclin B1 and phosphorylations of specific CDK1 substrate (Ser54)-n-myc was performed in homogenates obtained from intact and injured spinal cord. A . Cyclin B1 expression was upregulated at all time points tested. Phosphorylation (Ser54) of n-myc and phospho-CDK substrate motif signal levels were increased from 5 h to day 7. B–D . Quantification of respective western blots in panel A. n = 4 rats/time point. *P<0.05 vs sham group.

    Techniques Used: Western Blot, Expressing

    A–B . Coronal section in intact spinal cord (A) showed that E2F1 is relatively weak and detected mainly in neurons of the gray matter. At 24 h after SCI, E2F1 immunoreactivity was upregulated not only in gray matter but also in lesion area (B). C. E2F1 + cells were also co-labelled with NeuN in the dorsal horn of the gray matter at 1 day after SCI. D–E. Only a small subset of E2F1 + cells in the lesion area were positive for OX42 at 24 h (D) and 7 d (E) after SCI. F–G. In the intact spinal cord (F), CDK1 immunoreactivity is relatively weak and detected mainly in motor neurons in the ventral horn and CC1 + oligodendrocytes. At 24 h after SCI (G), CDK1 immunoreactivity was upregulated not only in the ventral horn but also in the spared white matter, colocalized with CC1 + oligodendrocytes. CDK1 + cells also appeared in the lesion area. H–I . CDK1 was expressed by CC1 + oligodendrocytes in the white matter in the intact spinal cord (H) and at 1 day after SCI. J . Only a small subset of CDK1 + cells in the lesion area were positive for OX42 at 24 h after SCI. K . Coronal section in intact spinal cord (a) shows that E2F1 was expressed in the motor neurons in the ventral horn. Immunoreactivity of E2F1 (b–d) was increased at 5 h, and 1–3 days post injury, and highly expressed by motor neurons. L. In intact spinal cord (a), CDK1/NeuN was detected in the motor neurons in the ventral horn. At 5 h after injury, immunoreactivity of CDK1 (b) was increased and sustained until 3 days post injury (c–d), and highly expressed by motor neurons. All images were taken at 2 mm rostral to epicenter. Scale bar = 500 µm for A–B, F–G. Scale bar = 100 µm for C–E, H–J, K–L.
    Figure Legend Snippet: A–B . Coronal section in intact spinal cord (A) showed that E2F1 is relatively weak and detected mainly in neurons of the gray matter. At 24 h after SCI, E2F1 immunoreactivity was upregulated not only in gray matter but also in lesion area (B). C. E2F1 + cells were also co-labelled with NeuN in the dorsal horn of the gray matter at 1 day after SCI. D–E. Only a small subset of E2F1 + cells in the lesion area were positive for OX42 at 24 h (D) and 7 d (E) after SCI. F–G. In the intact spinal cord (F), CDK1 immunoreactivity is relatively weak and detected mainly in motor neurons in the ventral horn and CC1 + oligodendrocytes. At 24 h after SCI (G), CDK1 immunoreactivity was upregulated not only in the ventral horn but also in the spared white matter, colocalized with CC1 + oligodendrocytes. CDK1 + cells also appeared in the lesion area. H–I . CDK1 was expressed by CC1 + oligodendrocytes in the white matter in the intact spinal cord (H) and at 1 day after SCI. J . Only a small subset of CDK1 + cells in the lesion area were positive for OX42 at 24 h after SCI. K . Coronal section in intact spinal cord (a) shows that E2F1 was expressed in the motor neurons in the ventral horn. Immunoreactivity of E2F1 (b–d) was increased at 5 h, and 1–3 days post injury, and highly expressed by motor neurons. L. In intact spinal cord (a), CDK1/NeuN was detected in the motor neurons in the ventral horn. At 5 h after injury, immunoreactivity of CDK1 (b) was increased and sustained until 3 days post injury (c–d), and highly expressed by motor neurons. All images were taken at 2 mm rostral to epicenter. Scale bar = 500 µm for A–B, F–G. Scale bar = 100 µm for C–E, H–J, K–L.

    Techniques Used:

    A . 27 mer siRNA duplexes for human E2F1 or trilencer-27 universal scrambled negative control siRNA duplex was transfected in the human neuroblastoma SH-SY5Y cells. Two days after transfection, the cells were harvested and subjected to western blotting using mouse monoclonal antibodies to E2F1 and CDK1. Transfection with shRNA against E2F1 resulted in reduction of E2F1 expression (58% to 66% of control), accompanied by 50% of reduction of CDK1 expression. B . Primary rat cerebral cortical neurons were transfected with shRNA against rat E2F1. E2F1 protein expression was robust reduced to 47% or 59% for shRNAs 1 and 2 respectively, and E2F1 knockdown resulted in reduction of CDK1 expression from 47% to 64% for shRNAs 1 and 2 respectively. N = 4 dishes from 3 independent culture. *P<0.05 vs sham group.
    Figure Legend Snippet: A . 27 mer siRNA duplexes for human E2F1 or trilencer-27 universal scrambled negative control siRNA duplex was transfected in the human neuroblastoma SH-SY5Y cells. Two days after transfection, the cells were harvested and subjected to western blotting using mouse monoclonal antibodies to E2F1 and CDK1. Transfection with shRNA against E2F1 resulted in reduction of E2F1 expression (58% to 66% of control), accompanied by 50% of reduction of CDK1 expression. B . Primary rat cerebral cortical neurons were transfected with shRNA against rat E2F1. E2F1 protein expression was robust reduced to 47% or 59% for shRNAs 1 and 2 respectively, and E2F1 knockdown resulted in reduction of CDK1 expression from 47% to 64% for shRNAs 1 and 2 respectively. N = 4 dishes from 3 independent culture. *P<0.05 vs sham group.

    Techniques Used: Negative Control, Transfection, Western Blot, shRNA, Expressing

    A–C . Western blot analysis shows a significant increase in biochemical markers of apoptosis, active caspase-3 signal, as well as 145/150 kDa cleavage product of α-fodrin after SCI. N = 4 rats/time points. * p <0.05 vs sham group. D . E2F1 + cells were co-label with cleaved caspase 3 (yellow, arrow heads) in the gray matter at 2 mm rostral to the epicenter at 1 day after SCI. Scale bar = 100 µm. E . Coronal section in intact spinal cord (top panel) shows that CDK1 was expressed in the motor neurons in the ventral horn (VH). At 1 day after injury, immunoreactivity of CDK1 (middle panel, green) was increased, and highly expressed by apoptotic motor neurons (red), as shown at 2 mm rostral to epicenter. CDK1 was rarely expressed by inter-neurons in the dorsal horn (DH) after SCI (bottom panel). Scale bar = 100 µm for D(a–h) and 500 µm for D(i–l).
    Figure Legend Snippet: A–C . Western blot analysis shows a significant increase in biochemical markers of apoptosis, active caspase-3 signal, as well as 145/150 kDa cleavage product of α-fodrin after SCI. N = 4 rats/time points. * p <0.05 vs sham group. D . E2F1 + cells were co-label with cleaved caspase 3 (yellow, arrow heads) in the gray matter at 2 mm rostral to the epicenter at 1 day after SCI. Scale bar = 100 µm. E . Coronal section in intact spinal cord (top panel) shows that CDK1 was expressed in the motor neurons in the ventral horn (VH). At 1 day after injury, immunoreactivity of CDK1 (middle panel, green) was increased, and highly expressed by apoptotic motor neurons (red), as shown at 2 mm rostral to epicenter. CDK1 was rarely expressed by inter-neurons in the dorsal horn (DH) after SCI (bottom panel). Scale bar = 100 µm for D(a–h) and 500 µm for D(i–l).

    Techniques Used: Western Blot

    Rat cortical neurons were co-transfected with expression plasmids for ß-galactosidase with, either empty vector or vector expressing E2F1 or CDK1 (A and B). Similarly, ß-galactosidase plasmid was co-transfected along with scrambled, E2F1 or CDK1 shRNAs (C, D and E) and the extent of apoptosis was examined 48 h after transfection, or after an additional 24 h of trophic deprivation (TD) induction post 48 h transfection. A . Neurons transfected with E2F1 vector (0.6 µg DNA/0.5×10 6 neurons) increased basal apoptosis as compared to empty vector. B . Neurons transfected with CDK1 (0.8 µg DNA/0.5×10 6 neurons) vector enhanced TD-induced apoptosis as compared to empty vector transfected cells. C–D . A quantitative assessment of the percentage of nuclei featuring chromatin condensation demonstrates a significant attenuation of TD-induced apoptosis in neurons transfected with two different shRNAs targeting either E2F1 or CDK1. E . Attenuation of TD-induced chromatin condensation in neurons transfected by CDK1 shRNA1 is shown. Representative photomicrographs of the shRNA transfected neurons, which also co-express GFP protein from the separate promoter are shown. In all experiments ß-galactosidase was co-transfected at 0.01 µg DNA/0.5×10 6 neurons to visualize transfected neurons at later apoptotic stage. Neurons with either normal diffuse chromatin morphology or apoptotic condensation of nuclei (after Hoechst 33258 chromatin staining) are indicated by arrowheads or arrows, respectively. Statistical analysis was performed by Kruskal-Wallis one-way ANOVA on ranks, followed by post hoc adjustments using Dunnett's test. For A * p<0.001, vs. vector; For C * p<0.01, vs. TD vector; For D * p<0.05, vs. TD vector; Error bars are ± S.E.M. from three independent experiments.
    Figure Legend Snippet: Rat cortical neurons were co-transfected with expression plasmids for ß-galactosidase with, either empty vector or vector expressing E2F1 or CDK1 (A and B). Similarly, ß-galactosidase plasmid was co-transfected along with scrambled, E2F1 or CDK1 shRNAs (C, D and E) and the extent of apoptosis was examined 48 h after transfection, or after an additional 24 h of trophic deprivation (TD) induction post 48 h transfection. A . Neurons transfected with E2F1 vector (0.6 µg DNA/0.5×10 6 neurons) increased basal apoptosis as compared to empty vector. B . Neurons transfected with CDK1 (0.8 µg DNA/0.5×10 6 neurons) vector enhanced TD-induced apoptosis as compared to empty vector transfected cells. C–D . A quantitative assessment of the percentage of nuclei featuring chromatin condensation demonstrates a significant attenuation of TD-induced apoptosis in neurons transfected with two different shRNAs targeting either E2F1 or CDK1. E . Attenuation of TD-induced chromatin condensation in neurons transfected by CDK1 shRNA1 is shown. Representative photomicrographs of the shRNA transfected neurons, which also co-express GFP protein from the separate promoter are shown. In all experiments ß-galactosidase was co-transfected at 0.01 µg DNA/0.5×10 6 neurons to visualize transfected neurons at later apoptotic stage. Neurons with either normal diffuse chromatin morphology or apoptotic condensation of nuclei (after Hoechst 33258 chromatin staining) are indicated by arrowheads or arrows, respectively. Statistical analysis was performed by Kruskal-Wallis one-way ANOVA on ranks, followed by post hoc adjustments using Dunnett's test. For A * p<0.001, vs. vector; For C * p<0.01, vs. TD vector; For D * p<0.05, vs. TD vector; Error bars are ± S.E.M. from three independent experiments.

    Techniques Used: Transfection, Expressing, Plasmid Preparation, shRNA, Staining

    Cortical neurons were pre-treated with Roscovitine or CR8 (CDK1 inhibitors) or vehicle and then exposed to TD-or campthotecin induced apoptosis. A . Representative photomicrographs of control and trophic deprived neurons treated with the indicated concentrations Roscovitine and CR8 are shown. Upper row presents phase contrast images (Healthy neurons are indicated by larger cell bodies and abundant processes; Apoptotic neurons display shrunken cell bodies and sparse or lost processes). Lower row shows chromatin staining with Hoechst 33258. Arrows and arrowheads indicate surviving and apoptotic neurons, respectively suggesting an attenuation of TD-induced neuronal death in neurons pre-treated with Roscovinine or CR8. B . A quantitative assessment of the percentage of nuclei featuring chromatin condensation demonstrates a significant attenuation of TD-induced apoptosis in neurons pre-treated with Roscovitine (10 µM; * p<0.05, vs. TD vehicle) whereas CR8 at concentrations as low as 1 µM ( *** p<0.001, vs. TD vehicle) almost completely blocked development of apoptotic features in neuronal nuclei. C . Significant attenuation of campthotecin-induced apoptosis in neurons pre-treated with Roscovitine (50 µM; * p<0.001, vs. vehicle) and CR8 at concentrations as low as 1 µM ( *** p<0.001, vs. vehicle).
    Figure Legend Snippet: Cortical neurons were pre-treated with Roscovitine or CR8 (CDK1 inhibitors) or vehicle and then exposed to TD-or campthotecin induced apoptosis. A . Representative photomicrographs of control and trophic deprived neurons treated with the indicated concentrations Roscovitine and CR8 are shown. Upper row presents phase contrast images (Healthy neurons are indicated by larger cell bodies and abundant processes; Apoptotic neurons display shrunken cell bodies and sparse or lost processes). Lower row shows chromatin staining with Hoechst 33258. Arrows and arrowheads indicate surviving and apoptotic neurons, respectively suggesting an attenuation of TD-induced neuronal death in neurons pre-treated with Roscovinine or CR8. B . A quantitative assessment of the percentage of nuclei featuring chromatin condensation demonstrates a significant attenuation of TD-induced apoptosis in neurons pre-treated with Roscovitine (10 µM; * p<0.05, vs. TD vehicle) whereas CR8 at concentrations as low as 1 µM ( *** p<0.001, vs. TD vehicle) almost completely blocked development of apoptotic features in neuronal nuclei. C . Significant attenuation of campthotecin-induced apoptosis in neurons pre-treated with Roscovitine (50 µM; * p<0.001, vs. vehicle) and CR8 at concentrations as low as 1 µM ( *** p<0.001, vs. vehicle).

    Techniques Used: Staining

    A . Coronal section in intact spinal cord (a–c) shows that E2F1 was expressed in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of E2F1 (d–f) was increased, and highly expressed by motor neurons. The upregulation of E2F1 was clearly attenuated by CR8 treatment (g–i). B . In intact spinal cord (a–c), CDK1/NeuN was detected in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of CDK1 (d–f) was increased, and highly expressed by motor neurons. CDK1 upregulation was attenuated by CR8 treatment (g–i). All images were taken at 2 mm rostral to epicenter. Scale bar = 100 µm for C–F.
    Figure Legend Snippet: A . Coronal section in intact spinal cord (a–c) shows that E2F1 was expressed in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of E2F1 (d–f) was increased, and highly expressed by motor neurons. The upregulation of E2F1 was clearly attenuated by CR8 treatment (g–i). B . In intact spinal cord (a–c), CDK1/NeuN was detected in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of CDK1 (d–f) was increased, and highly expressed by motor neurons. CDK1 upregulation was attenuated by CR8 treatment (g–i). All images were taken at 2 mm rostral to epicenter. Scale bar = 100 µm for C–F.

    Techniques Used:

    rabbit polyclonal anti cdc2  (Santa Cruz Biotechnology)

     
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    Santa Cruz Biotechnology rabbit polyclonal anti cdc2
    Western blot analysis of <t>cdc2</t> (CDK1) and cdc25C in Abrams OSA cells at day 4 and 5. Both CPFX and ENFX inhibit G 2 checkpoint kinase cdc2 although CPFX showed more potent than ENFX. The level of phospho-cdc25C was increased in both CPFX and ENFX treated canine Abrams OSA cells.
    Rabbit Polyclonal Anti Cdc2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti cdc2/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
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    rabbit polyclonal anti cdc2 - by Bioz Stars, 2023-11
    86/100 stars

    Images

    1) Product Images from "Fluoroquinolone-Mediated Inhibition of Cell Growth, S-G 2 /M Cell Cycle Arrest, and Apoptosis in Canine Osteosarcoma Cell Lines"

    Article Title: Fluoroquinolone-Mediated Inhibition of Cell Growth, S-G 2 /M Cell Cycle Arrest, and Apoptosis in Canine Osteosarcoma Cell Lines

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0042960

    Western blot analysis of cdc2 (CDK1) and cdc25C in Abrams OSA cells at day 4 and 5. Both CPFX and ENFX inhibit G 2 checkpoint kinase cdc2 although CPFX showed more potent than ENFX. The level of phospho-cdc25C was increased in both CPFX and ENFX treated canine Abrams OSA cells.
    Figure Legend Snippet: Western blot analysis of cdc2 (CDK1) and cdc25C in Abrams OSA cells at day 4 and 5. Both CPFX and ENFX inhibit G 2 checkpoint kinase cdc2 although CPFX showed more potent than ENFX. The level of phospho-cdc25C was increased in both CPFX and ENFX treated canine Abrams OSA cells.

    Techniques Used: Western Blot

    polyclonal rabbit anti phospho tyr15 cdc2  (Santa Cruz Biotechnology)

     
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    Santa Cruz Biotechnology polyclonal rabbit anti phospho tyr15 cdc2
    (A) BJAB cells transfected with the pA3M vector or pA3M-LANA were treated with nocodazole (200 ng/mL) for 24 hours. The cells were then harvested, total cell lysate were prepared and western blot was performed using antibodies against cyclin B1, <t>Cdc2,</t> <t>Tyr15-phosphorylated</t> Cdc2 [Cdc2 (Tyr15)], and Histone H3 as a protein loading control. (B) BJAB cells transfected with the pA3M vector or pA3M-LANA were grown in 6 well culture plates and treated with nocodazole and observed for colocolaization in a confocal microscope. The result shown is the representative of 3 independent experiments. +, present; −, absent.
    Polyclonal Rabbit Anti Phospho Tyr15 Cdc2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal rabbit anti phospho tyr15 cdc2/product/Santa Cruz Biotechnology
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    Images

    1) Product Images from "Kaposi Sarcoma Herpes Virus Latency Associated Nuclear Antigen Protein Release the G2/M Cell Cycle Blocks by Modulating ATM/ATR Mediated Checkpoint Pathway"

    Article Title: Kaposi Sarcoma Herpes Virus Latency Associated Nuclear Antigen Protein Release the G2/M Cell Cycle Blocks by Modulating ATM/ATR Mediated Checkpoint Pathway

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0100228

    (A) BJAB cells transfected with the pA3M vector or pA3M-LANA were treated with nocodazole (200 ng/mL) for 24 hours. The cells were then harvested, total cell lysate were prepared and western blot was performed using antibodies against cyclin B1, Cdc2, Tyr15-phosphorylated Cdc2 [Cdc2 (Tyr15)], and Histone H3 as a protein loading control. (B) BJAB cells transfected with the pA3M vector or pA3M-LANA were grown in 6 well culture plates and treated with nocodazole and observed for colocolaization in a confocal microscope. The result shown is the representative of 3 independent experiments. +, present; −, absent.
    Figure Legend Snippet: (A) BJAB cells transfected with the pA3M vector or pA3M-LANA were treated with nocodazole (200 ng/mL) for 24 hours. The cells were then harvested, total cell lysate were prepared and western blot was performed using antibodies against cyclin B1, Cdc2, Tyr15-phosphorylated Cdc2 [Cdc2 (Tyr15)], and Histone H3 as a protein loading control. (B) BJAB cells transfected with the pA3M vector or pA3M-LANA were grown in 6 well culture plates and treated with nocodazole and observed for colocolaization in a confocal microscope. The result shown is the representative of 3 independent experiments. +, present; −, absent.

    Techniques Used: Transfection, Plasmid Preparation, Western Blot, Microscopy

    Nocodazole treatment reduces the level of phosphorylated Cdc2. The viral nuclear antigen LANA binds directly to Chk2, which may result in the phosphorylation of Cdc25c and sequester it in the cytoplasm. Thus, it may be unable to regulate the phosphorylation of nuclear Cdc2 resulting the activation of cyclin B-Cdc2 and progression through the G2/M phase, releasing the nocodozole induced block.
    Figure Legend Snippet: Nocodazole treatment reduces the level of phosphorylated Cdc2. The viral nuclear antigen LANA binds directly to Chk2, which may result in the phosphorylation of Cdc25c and sequester it in the cytoplasm. Thus, it may be unable to regulate the phosphorylation of nuclear Cdc2 resulting the activation of cyclin B-Cdc2 and progression through the G2/M phase, releasing the nocodozole induced block.

    Techniques Used: Activation Assay, Blocking Assay

    rabbit polyclonal anti cdc2 pstaire  (Santa Cruz Biotechnology)

     
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    Santa Cruz Biotechnology rabbit polyclonal anti cdc2 pstaire

    Rabbit Polyclonal Anti Cdc2 Pstaire, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti cdc2 pstaire/product/Santa Cruz Biotechnology
    Average 94 stars, based on 1 article reviews
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    Images

    1) Product Images from "The Arabidopsis F-box protein FBW2 targets AGO1 for degradation to prevent spurious loading of illegitimate small RNA"

    Article Title: The Arabidopsis F-box protein FBW2 targets AGO1 for degradation to prevent spurious loading of illegitimate small RNA

    Journal: Cell Reports

    doi: 10.1016/j.celrep.2022.110671


    Figure Legend Snippet:

    Techniques Used: Recombinant, SYBR Green Assay, Western Blot, Protease Inhibitor, Isolation, Magnetic Beads, Mass Spectrometry, Clone Assay, Sequencing, Software

    rabbit polyclonal  (Santa Cruz Biotechnology)

     
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    Santa Cruz Biotechnology rabbit polyclonal
    Primary and secondary antibodies used for immunohistochemistry.
    Rabbit Polyclonal, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal/product/Santa Cruz Biotechnology
    Average 97 stars, based on 1 article reviews
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    1) Product Images from "Selective Depletion of Adult GFAP-Expressing Tanycytes Leads to Hypogonadotropic Hypogonadism in Males"

    Article Title: Selective Depletion of Adult GFAP-Expressing Tanycytes Leads to Hypogonadotropic Hypogonadism in Males

    Journal: Frontiers in Endocrinology

    doi: 10.3389/fendo.2022.869019

    Primary and secondary antibodies used for immunohistochemistry.
    Figure Legend Snippet: Primary and secondary antibodies used for immunohistochemistry.

    Techniques Used: Immunohistochemistry

    rabbit polyclonal anti cdk1 p34  (Santa Cruz Biotechnology)

     
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    Santa Cruz Biotechnology rabbit polyclonal anti cdk1 p34
    Rabbit Polyclonal Anti Cdk1 P34, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti cdk1 p34/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
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    rabbit polyclonal anti cdk1 p34 - by Bioz Stars, 2023-11
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    rabbit polyclonal anti phospho cdk1  (Santa Cruz Biotechnology)

     
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    Santa Cruz Biotechnology rabbit polyclonal anti phospho cdk1
    KEY RESOURCES TABLE
    Rabbit Polyclonal Anti Phospho Cdk1, supplied by Santa Cruz Biotechnology, 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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    1) Product Images from "Comprehensive Molecular Characterization Identifies Distinct Genomic and Immune Hallmarks of Renal Medullary Carcinoma"

    Article Title: Comprehensive Molecular Characterization Identifies Distinct Genomic and Immune Hallmarks of Renal Medullary Carcinoma

    Journal: Cancer cell

    doi: 10.1016/j.ccell.2020.04.002

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    Techniques Used: Recombinant, DNA Methylation Assay, Empire Assay, Imaging, Sequencing, Plasmid Preparation, Software

    rabbit polyclonal anti phospho cdk1  (Santa Cruz Biotechnology)

     
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    Santa Cruz Biotechnology rabbit polyclonal anti phospho cdk1
    KEY RESOURCES TABLE
    Rabbit Polyclonal Anti Phospho Cdk1, supplied by Santa Cruz Biotechnology, 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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    1) Product Images from "Comprehensive Molecular Characterization Identifies Distinct Genomic and Immune Hallmarks of Renal Medullary Carcinoma"

    Article Title: Comprehensive Molecular Characterization Identifies Distinct Genomic and Immune Hallmarks of Renal Medullary Carcinoma

    Journal: Cancer cell

    doi: 10.1016/j.ccell.2020.04.002

    KEY RESOURCES TABLE
    Figure Legend Snippet: KEY RESOURCES TABLE

    Techniques Used: Recombinant, DNA Methylation Assay, Empire Assay, Imaging, Sequencing, Plasmid Preparation, Software

    rabbit polyclonal anti phospho cdk1  (Santa Cruz Biotechnology)

     
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    Santa Cruz Biotechnology rabbit polyclonal anti phospho cdk1
    KEY RESOURCES TABLE
    Rabbit Polyclonal Anti Phospho Cdk1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti phospho cdk1/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti phospho cdk1 - by Bioz Stars, 2023-11
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    1) Product Images from "Comprehensive Molecular Characterization Identifies Distinct Genomic and Immune Hallmarks of Renal Medullary Carcinoma"

    Article Title: Comprehensive Molecular Characterization Identifies Distinct Genomic and Immune Hallmarks of Renal Medullary Carcinoma

    Journal: Cancer cell

    doi: 10.1016/j.ccell.2020.04.002

    KEY RESOURCES TABLE
    Figure Legend Snippet: KEY RESOURCES TABLE

    Techniques Used: Recombinant, DNA Methylation Assay, Empire Assay, Imaging, Sequencing, Plasmid Preparation, Software

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    Analysis of expression of E2F1 and its transcriptional target genes in intact and injured spinal cord were performed by western blotting. A . 5-mm-long segment centered at the injury epicenter was dissected and homogenized in RIPA buffer. Equal amounts of protein were electrophoretically separated on NuPAGE Novex Bis-Tris gradient gels, transferred to nitrocellulose membranes, and blotted with antibodies to E2F1 and <t>CDK1.</t> GAPDH signal served as a loading control. B–C . The signal quantifications for E2F1 (B) and CDK1 (C) using Gel-Pro Analyzer software are displayed. E2F1 and CDK1 expression level was upregulated as early as 15 min and sustained until 3 days after injury. D–E . Cyclin A expression was increased at all time points. F . Bim and c-Myb, downstream targets of E2F1 were upregulated as early as 5 h post-injury and sustained until day 3 after SCI. G–H . Quantification of respective western blots in panel D. N = 4 rats/time point. *P<0.05 vs sham group.
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    Analysis of expression of E2F1 and its transcriptional target genes in intact and injured spinal cord were performed by western blotting. A . 5-mm-long segment centered at the injury epicenter was dissected and homogenized in RIPA buffer. Equal amounts of protein were electrophoretically separated on NuPAGE Novex Bis-Tris gradient gels, transferred to nitrocellulose membranes, and blotted with antibodies to E2F1 and CDK1. GAPDH signal served as a loading control. B–C . The signal quantifications for E2F1 (B) and CDK1 (C) using Gel-Pro Analyzer software are displayed. E2F1 and CDK1 expression level was upregulated as early as 15 min and sustained until 3 days after injury. D–E . Cyclin A expression was increased at all time points. F . Bim and c-Myb, downstream targets of E2F1 were upregulated as early as 5 h post-injury and sustained until day 3 after SCI. G–H . Quantification of respective western blots in panel D. N = 4 rats/time point. *P<0.05 vs sham group.

    Journal: PLoS ONE

    Article Title: Inhibition of E2F1/CDK1 Pathway Attenuates Neuronal Apoptosis In Vitro and Confers Neuroprotection after Spinal Cord Injury In Vivo

    doi: 10.1371/journal.pone.0042129

    Figure Lengend Snippet: Analysis of expression of E2F1 and its transcriptional target genes in intact and injured spinal cord were performed by western blotting. A . 5-mm-long segment centered at the injury epicenter was dissected and homogenized in RIPA buffer. Equal amounts of protein were electrophoretically separated on NuPAGE Novex Bis-Tris gradient gels, transferred to nitrocellulose membranes, and blotted with antibodies to E2F1 and CDK1. GAPDH signal served as a loading control. B–C . The signal quantifications for E2F1 (B) and CDK1 (C) using Gel-Pro Analyzer software are displayed. E2F1 and CDK1 expression level was upregulated as early as 15 min and sustained until 3 days after injury. D–E . Cyclin A expression was increased at all time points. F . Bim and c-Myb, downstream targets of E2F1 were upregulated as early as 5 h post-injury and sustained until day 3 after SCI. G–H . Quantification of respective western blots in panel D. N = 4 rats/time point. *P<0.05 vs sham group.

    Article Snippet: The following antibodies and reagents were obtained from commercial sources: polyclonal rabbit anti-CDK1, cyclin B1, cyclin A, Bim, and c-Myb (Santa Cruz Biotechnology), mouse anti-CDK1 (Santa Cruz Biotechnology), mouse anti-E2F1 (BD pharmingenTM), rabbit anti-phospho(Ser)-CDK substrate, rabbit anti-cleaved caspase 3 (Cell Signaling Technology), anti-pS54-n-myc (Bethyl Laboratories Inc), rabbit anti-β-galactosidase (MP Biomedicals), monoclonal mouse anti-GAPDH and NeuN (Chemicon), mouse anti-fodrin (Affinity Research Products), mouse anti-APC (CC1, Abcam), mouse anti-CD11b (OX42, Serotec), Hoechst 33258 and other reagents and supplies (Sigma).

    Techniques: Expressing, Western Blot, Software

    Western blotting analysis of common CDK substrates, CDK1 co-activator cyclin B1 and phosphorylations of specific CDK1 substrate (Ser54)-n-myc was performed in homogenates obtained from intact and injured spinal cord. A . Cyclin B1 expression was upregulated at all time points tested. Phosphorylation (Ser54) of n-myc and phospho-CDK substrate motif signal levels were increased from 5 h to day 7. B–D . Quantification of respective western blots in panel A. n = 4 rats/time point. *P<0.05 vs sham group.

    Journal: PLoS ONE

    Article Title: Inhibition of E2F1/CDK1 Pathway Attenuates Neuronal Apoptosis In Vitro and Confers Neuroprotection after Spinal Cord Injury In Vivo

    doi: 10.1371/journal.pone.0042129

    Figure Lengend Snippet: Western blotting analysis of common CDK substrates, CDK1 co-activator cyclin B1 and phosphorylations of specific CDK1 substrate (Ser54)-n-myc was performed in homogenates obtained from intact and injured spinal cord. A . Cyclin B1 expression was upregulated at all time points tested. Phosphorylation (Ser54) of n-myc and phospho-CDK substrate motif signal levels were increased from 5 h to day 7. B–D . Quantification of respective western blots in panel A. n = 4 rats/time point. *P<0.05 vs sham group.

    Article Snippet: The following antibodies and reagents were obtained from commercial sources: polyclonal rabbit anti-CDK1, cyclin B1, cyclin A, Bim, and c-Myb (Santa Cruz Biotechnology), mouse anti-CDK1 (Santa Cruz Biotechnology), mouse anti-E2F1 (BD pharmingenTM), rabbit anti-phospho(Ser)-CDK substrate, rabbit anti-cleaved caspase 3 (Cell Signaling Technology), anti-pS54-n-myc (Bethyl Laboratories Inc), rabbit anti-β-galactosidase (MP Biomedicals), monoclonal mouse anti-GAPDH and NeuN (Chemicon), mouse anti-fodrin (Affinity Research Products), mouse anti-APC (CC1, Abcam), mouse anti-CD11b (OX42, Serotec), Hoechst 33258 and other reagents and supplies (Sigma).

    Techniques: Western Blot, Expressing

    A–B . Coronal section in intact spinal cord (A) showed that E2F1 is relatively weak and detected mainly in neurons of the gray matter. At 24 h after SCI, E2F1 immunoreactivity was upregulated not only in gray matter but also in lesion area (B). C. E2F1 + cells were also co-labelled with NeuN in the dorsal horn of the gray matter at 1 day after SCI. D–E. Only a small subset of E2F1 + cells in the lesion area were positive for OX42 at 24 h (D) and 7 d (E) after SCI. F–G. In the intact spinal cord (F), CDK1 immunoreactivity is relatively weak and detected mainly in motor neurons in the ventral horn and CC1 + oligodendrocytes. At 24 h after SCI (G), CDK1 immunoreactivity was upregulated not only in the ventral horn but also in the spared white matter, colocalized with CC1 + oligodendrocytes. CDK1 + cells also appeared in the lesion area. H–I . CDK1 was expressed by CC1 + oligodendrocytes in the white matter in the intact spinal cord (H) and at 1 day after SCI. J . Only a small subset of CDK1 + cells in the lesion area were positive for OX42 at 24 h after SCI. K . Coronal section in intact spinal cord (a) shows that E2F1 was expressed in the motor neurons in the ventral horn. Immunoreactivity of E2F1 (b–d) was increased at 5 h, and 1–3 days post injury, and highly expressed by motor neurons. L. In intact spinal cord (a), CDK1/NeuN was detected in the motor neurons in the ventral horn. At 5 h after injury, immunoreactivity of CDK1 (b) was increased and sustained until 3 days post injury (c–d), and highly expressed by motor neurons. All images were taken at 2 mm rostral to epicenter. Scale bar = 500 µm for A–B, F–G. Scale bar = 100 µm for C–E, H–J, K–L.

    Journal: PLoS ONE

    Article Title: Inhibition of E2F1/CDK1 Pathway Attenuates Neuronal Apoptosis In Vitro and Confers Neuroprotection after Spinal Cord Injury In Vivo

    doi: 10.1371/journal.pone.0042129

    Figure Lengend Snippet: A–B . Coronal section in intact spinal cord (A) showed that E2F1 is relatively weak and detected mainly in neurons of the gray matter. At 24 h after SCI, E2F1 immunoreactivity was upregulated not only in gray matter but also in lesion area (B). C. E2F1 + cells were also co-labelled with NeuN in the dorsal horn of the gray matter at 1 day after SCI. D–E. Only a small subset of E2F1 + cells in the lesion area were positive for OX42 at 24 h (D) and 7 d (E) after SCI. F–G. In the intact spinal cord (F), CDK1 immunoreactivity is relatively weak and detected mainly in motor neurons in the ventral horn and CC1 + oligodendrocytes. At 24 h after SCI (G), CDK1 immunoreactivity was upregulated not only in the ventral horn but also in the spared white matter, colocalized with CC1 + oligodendrocytes. CDK1 + cells also appeared in the lesion area. H–I . CDK1 was expressed by CC1 + oligodendrocytes in the white matter in the intact spinal cord (H) and at 1 day after SCI. J . Only a small subset of CDK1 + cells in the lesion area were positive for OX42 at 24 h after SCI. K . Coronal section in intact spinal cord (a) shows that E2F1 was expressed in the motor neurons in the ventral horn. Immunoreactivity of E2F1 (b–d) was increased at 5 h, and 1–3 days post injury, and highly expressed by motor neurons. L. In intact spinal cord (a), CDK1/NeuN was detected in the motor neurons in the ventral horn. At 5 h after injury, immunoreactivity of CDK1 (b) was increased and sustained until 3 days post injury (c–d), and highly expressed by motor neurons. All images were taken at 2 mm rostral to epicenter. Scale bar = 500 µm for A–B, F–G. Scale bar = 100 µm for C–E, H–J, K–L.

    Article Snippet: The following antibodies and reagents were obtained from commercial sources: polyclonal rabbit anti-CDK1, cyclin B1, cyclin A, Bim, and c-Myb (Santa Cruz Biotechnology), mouse anti-CDK1 (Santa Cruz Biotechnology), mouse anti-E2F1 (BD pharmingenTM), rabbit anti-phospho(Ser)-CDK substrate, rabbit anti-cleaved caspase 3 (Cell Signaling Technology), anti-pS54-n-myc (Bethyl Laboratories Inc), rabbit anti-β-galactosidase (MP Biomedicals), monoclonal mouse anti-GAPDH and NeuN (Chemicon), mouse anti-fodrin (Affinity Research Products), mouse anti-APC (CC1, Abcam), mouse anti-CD11b (OX42, Serotec), Hoechst 33258 and other reagents and supplies (Sigma).

    Techniques:

    A . 27 mer siRNA duplexes for human E2F1 or trilencer-27 universal scrambled negative control siRNA duplex was transfected in the human neuroblastoma SH-SY5Y cells. Two days after transfection, the cells were harvested and subjected to western blotting using mouse monoclonal antibodies to E2F1 and CDK1. Transfection with shRNA against E2F1 resulted in reduction of E2F1 expression (58% to 66% of control), accompanied by 50% of reduction of CDK1 expression. B . Primary rat cerebral cortical neurons were transfected with shRNA against rat E2F1. E2F1 protein expression was robust reduced to 47% or 59% for shRNAs 1 and 2 respectively, and E2F1 knockdown resulted in reduction of CDK1 expression from 47% to 64% for shRNAs 1 and 2 respectively. N = 4 dishes from 3 independent culture. *P<0.05 vs sham group.

    Journal: PLoS ONE

    Article Title: Inhibition of E2F1/CDK1 Pathway Attenuates Neuronal Apoptosis In Vitro and Confers Neuroprotection after Spinal Cord Injury In Vivo

    doi: 10.1371/journal.pone.0042129

    Figure Lengend Snippet: A . 27 mer siRNA duplexes for human E2F1 or trilencer-27 universal scrambled negative control siRNA duplex was transfected in the human neuroblastoma SH-SY5Y cells. Two days after transfection, the cells were harvested and subjected to western blotting using mouse monoclonal antibodies to E2F1 and CDK1. Transfection with shRNA against E2F1 resulted in reduction of E2F1 expression (58% to 66% of control), accompanied by 50% of reduction of CDK1 expression. B . Primary rat cerebral cortical neurons were transfected with shRNA against rat E2F1. E2F1 protein expression was robust reduced to 47% or 59% for shRNAs 1 and 2 respectively, and E2F1 knockdown resulted in reduction of CDK1 expression from 47% to 64% for shRNAs 1 and 2 respectively. N = 4 dishes from 3 independent culture. *P<0.05 vs sham group.

    Article Snippet: The following antibodies and reagents were obtained from commercial sources: polyclonal rabbit anti-CDK1, cyclin B1, cyclin A, Bim, and c-Myb (Santa Cruz Biotechnology), mouse anti-CDK1 (Santa Cruz Biotechnology), mouse anti-E2F1 (BD pharmingenTM), rabbit anti-phospho(Ser)-CDK substrate, rabbit anti-cleaved caspase 3 (Cell Signaling Technology), anti-pS54-n-myc (Bethyl Laboratories Inc), rabbit anti-β-galactosidase (MP Biomedicals), monoclonal mouse anti-GAPDH and NeuN (Chemicon), mouse anti-fodrin (Affinity Research Products), mouse anti-APC (CC1, Abcam), mouse anti-CD11b (OX42, Serotec), Hoechst 33258 and other reagents and supplies (Sigma).

    Techniques: Negative Control, Transfection, Western Blot, shRNA, Expressing

    A–C . Western blot analysis shows a significant increase in biochemical markers of apoptosis, active caspase-3 signal, as well as 145/150 kDa cleavage product of α-fodrin after SCI. N = 4 rats/time points. * p <0.05 vs sham group. D . E2F1 + cells were co-label with cleaved caspase 3 (yellow, arrow heads) in the gray matter at 2 mm rostral to the epicenter at 1 day after SCI. Scale bar = 100 µm. E . Coronal section in intact spinal cord (top panel) shows that CDK1 was expressed in the motor neurons in the ventral horn (VH). At 1 day after injury, immunoreactivity of CDK1 (middle panel, green) was increased, and highly expressed by apoptotic motor neurons (red), as shown at 2 mm rostral to epicenter. CDK1 was rarely expressed by inter-neurons in the dorsal horn (DH) after SCI (bottom panel). Scale bar = 100 µm for D(a–h) and 500 µm for D(i–l).

    Journal: PLoS ONE

    Article Title: Inhibition of E2F1/CDK1 Pathway Attenuates Neuronal Apoptosis In Vitro and Confers Neuroprotection after Spinal Cord Injury In Vivo

    doi: 10.1371/journal.pone.0042129

    Figure Lengend Snippet: A–C . Western blot analysis shows a significant increase in biochemical markers of apoptosis, active caspase-3 signal, as well as 145/150 kDa cleavage product of α-fodrin after SCI. N = 4 rats/time points. * p <0.05 vs sham group. D . E2F1 + cells were co-label with cleaved caspase 3 (yellow, arrow heads) in the gray matter at 2 mm rostral to the epicenter at 1 day after SCI. Scale bar = 100 µm. E . Coronal section in intact spinal cord (top panel) shows that CDK1 was expressed in the motor neurons in the ventral horn (VH). At 1 day after injury, immunoreactivity of CDK1 (middle panel, green) was increased, and highly expressed by apoptotic motor neurons (red), as shown at 2 mm rostral to epicenter. CDK1 was rarely expressed by inter-neurons in the dorsal horn (DH) after SCI (bottom panel). Scale bar = 100 µm for D(a–h) and 500 µm for D(i–l).

    Article Snippet: The following antibodies and reagents were obtained from commercial sources: polyclonal rabbit anti-CDK1, cyclin B1, cyclin A, Bim, and c-Myb (Santa Cruz Biotechnology), mouse anti-CDK1 (Santa Cruz Biotechnology), mouse anti-E2F1 (BD pharmingenTM), rabbit anti-phospho(Ser)-CDK substrate, rabbit anti-cleaved caspase 3 (Cell Signaling Technology), anti-pS54-n-myc (Bethyl Laboratories Inc), rabbit anti-β-galactosidase (MP Biomedicals), monoclonal mouse anti-GAPDH and NeuN (Chemicon), mouse anti-fodrin (Affinity Research Products), mouse anti-APC (CC1, Abcam), mouse anti-CD11b (OX42, Serotec), Hoechst 33258 and other reagents and supplies (Sigma).

    Techniques: Western Blot

    Rat cortical neurons were co-transfected with expression plasmids for ß-galactosidase with, either empty vector or vector expressing E2F1 or CDK1 (A and B). Similarly, ß-galactosidase plasmid was co-transfected along with scrambled, E2F1 or CDK1 shRNAs (C, D and E) and the extent of apoptosis was examined 48 h after transfection, or after an additional 24 h of trophic deprivation (TD) induction post 48 h transfection. A . Neurons transfected with E2F1 vector (0.6 µg DNA/0.5×10 6 neurons) increased basal apoptosis as compared to empty vector. B . Neurons transfected with CDK1 (0.8 µg DNA/0.5×10 6 neurons) vector enhanced TD-induced apoptosis as compared to empty vector transfected cells. C–D . A quantitative assessment of the percentage of nuclei featuring chromatin condensation demonstrates a significant attenuation of TD-induced apoptosis in neurons transfected with two different shRNAs targeting either E2F1 or CDK1. E . Attenuation of TD-induced chromatin condensation in neurons transfected by CDK1 shRNA1 is shown. Representative photomicrographs of the shRNA transfected neurons, which also co-express GFP protein from the separate promoter are shown. In all experiments ß-galactosidase was co-transfected at 0.01 µg DNA/0.5×10 6 neurons to visualize transfected neurons at later apoptotic stage. Neurons with either normal diffuse chromatin morphology or apoptotic condensation of nuclei (after Hoechst 33258 chromatin staining) are indicated by arrowheads or arrows, respectively. Statistical analysis was performed by Kruskal-Wallis one-way ANOVA on ranks, followed by post hoc adjustments using Dunnett's test. For A * p<0.001, vs. vector; For C * p<0.01, vs. TD vector; For D * p<0.05, vs. TD vector; Error bars are ± S.E.M. from three independent experiments.

    Journal: PLoS ONE

    Article Title: Inhibition of E2F1/CDK1 Pathway Attenuates Neuronal Apoptosis In Vitro and Confers Neuroprotection after Spinal Cord Injury In Vivo

    doi: 10.1371/journal.pone.0042129

    Figure Lengend Snippet: Rat cortical neurons were co-transfected with expression plasmids for ß-galactosidase with, either empty vector or vector expressing E2F1 or CDK1 (A and B). Similarly, ß-galactosidase plasmid was co-transfected along with scrambled, E2F1 or CDK1 shRNAs (C, D and E) and the extent of apoptosis was examined 48 h after transfection, or after an additional 24 h of trophic deprivation (TD) induction post 48 h transfection. A . Neurons transfected with E2F1 vector (0.6 µg DNA/0.5×10 6 neurons) increased basal apoptosis as compared to empty vector. B . Neurons transfected with CDK1 (0.8 µg DNA/0.5×10 6 neurons) vector enhanced TD-induced apoptosis as compared to empty vector transfected cells. C–D . A quantitative assessment of the percentage of nuclei featuring chromatin condensation demonstrates a significant attenuation of TD-induced apoptosis in neurons transfected with two different shRNAs targeting either E2F1 or CDK1. E . Attenuation of TD-induced chromatin condensation in neurons transfected by CDK1 shRNA1 is shown. Representative photomicrographs of the shRNA transfected neurons, which also co-express GFP protein from the separate promoter are shown. In all experiments ß-galactosidase was co-transfected at 0.01 µg DNA/0.5×10 6 neurons to visualize transfected neurons at later apoptotic stage. Neurons with either normal diffuse chromatin morphology or apoptotic condensation of nuclei (after Hoechst 33258 chromatin staining) are indicated by arrowheads or arrows, respectively. Statistical analysis was performed by Kruskal-Wallis one-way ANOVA on ranks, followed by post hoc adjustments using Dunnett's test. For A * p<0.001, vs. vector; For C * p<0.01, vs. TD vector; For D * p<0.05, vs. TD vector; Error bars are ± S.E.M. from three independent experiments.

    Article Snippet: The following antibodies and reagents were obtained from commercial sources: polyclonal rabbit anti-CDK1, cyclin B1, cyclin A, Bim, and c-Myb (Santa Cruz Biotechnology), mouse anti-CDK1 (Santa Cruz Biotechnology), mouse anti-E2F1 (BD pharmingenTM), rabbit anti-phospho(Ser)-CDK substrate, rabbit anti-cleaved caspase 3 (Cell Signaling Technology), anti-pS54-n-myc (Bethyl Laboratories Inc), rabbit anti-β-galactosidase (MP Biomedicals), monoclonal mouse anti-GAPDH and NeuN (Chemicon), mouse anti-fodrin (Affinity Research Products), mouse anti-APC (CC1, Abcam), mouse anti-CD11b (OX42, Serotec), Hoechst 33258 and other reagents and supplies (Sigma).

    Techniques: Transfection, Expressing, Plasmid Preparation, shRNA, Staining

    Cortical neurons were pre-treated with Roscovitine or CR8 (CDK1 inhibitors) or vehicle and then exposed to TD-or campthotecin induced apoptosis. A . Representative photomicrographs of control and trophic deprived neurons treated with the indicated concentrations Roscovitine and CR8 are shown. Upper row presents phase contrast images (Healthy neurons are indicated by larger cell bodies and abundant processes; Apoptotic neurons display shrunken cell bodies and sparse or lost processes). Lower row shows chromatin staining with Hoechst 33258. Arrows and arrowheads indicate surviving and apoptotic neurons, respectively suggesting an attenuation of TD-induced neuronal death in neurons pre-treated with Roscovinine or CR8. B . A quantitative assessment of the percentage of nuclei featuring chromatin condensation demonstrates a significant attenuation of TD-induced apoptosis in neurons pre-treated with Roscovitine (10 µM; * p<0.05, vs. TD vehicle) whereas CR8 at concentrations as low as 1 µM ( *** p<0.001, vs. TD vehicle) almost completely blocked development of apoptotic features in neuronal nuclei. C . Significant attenuation of campthotecin-induced apoptosis in neurons pre-treated with Roscovitine (50 µM; * p<0.001, vs. vehicle) and CR8 at concentrations as low as 1 µM ( *** p<0.001, vs. vehicle).

    Journal: PLoS ONE

    Article Title: Inhibition of E2F1/CDK1 Pathway Attenuates Neuronal Apoptosis In Vitro and Confers Neuroprotection after Spinal Cord Injury In Vivo

    doi: 10.1371/journal.pone.0042129

    Figure Lengend Snippet: Cortical neurons were pre-treated with Roscovitine or CR8 (CDK1 inhibitors) or vehicle and then exposed to TD-or campthotecin induced apoptosis. A . Representative photomicrographs of control and trophic deprived neurons treated with the indicated concentrations Roscovitine and CR8 are shown. Upper row presents phase contrast images (Healthy neurons are indicated by larger cell bodies and abundant processes; Apoptotic neurons display shrunken cell bodies and sparse or lost processes). Lower row shows chromatin staining with Hoechst 33258. Arrows and arrowheads indicate surviving and apoptotic neurons, respectively suggesting an attenuation of TD-induced neuronal death in neurons pre-treated with Roscovinine or CR8. B . A quantitative assessment of the percentage of nuclei featuring chromatin condensation demonstrates a significant attenuation of TD-induced apoptosis in neurons pre-treated with Roscovitine (10 µM; * p<0.05, vs. TD vehicle) whereas CR8 at concentrations as low as 1 µM ( *** p<0.001, vs. TD vehicle) almost completely blocked development of apoptotic features in neuronal nuclei. C . Significant attenuation of campthotecin-induced apoptosis in neurons pre-treated with Roscovitine (50 µM; * p<0.001, vs. vehicle) and CR8 at concentrations as low as 1 µM ( *** p<0.001, vs. vehicle).

    Article Snippet: The following antibodies and reagents were obtained from commercial sources: polyclonal rabbit anti-CDK1, cyclin B1, cyclin A, Bim, and c-Myb (Santa Cruz Biotechnology), mouse anti-CDK1 (Santa Cruz Biotechnology), mouse anti-E2F1 (BD pharmingenTM), rabbit anti-phospho(Ser)-CDK substrate, rabbit anti-cleaved caspase 3 (Cell Signaling Technology), anti-pS54-n-myc (Bethyl Laboratories Inc), rabbit anti-β-galactosidase (MP Biomedicals), monoclonal mouse anti-GAPDH and NeuN (Chemicon), mouse anti-fodrin (Affinity Research Products), mouse anti-APC (CC1, Abcam), mouse anti-CD11b (OX42, Serotec), Hoechst 33258 and other reagents and supplies (Sigma).

    Techniques: Staining

    A . Coronal section in intact spinal cord (a–c) shows that E2F1 was expressed in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of E2F1 (d–f) was increased, and highly expressed by motor neurons. The upregulation of E2F1 was clearly attenuated by CR8 treatment (g–i). B . In intact spinal cord (a–c), CDK1/NeuN was detected in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of CDK1 (d–f) was increased, and highly expressed by motor neurons. CDK1 upregulation was attenuated by CR8 treatment (g–i). All images were taken at 2 mm rostral to epicenter. Scale bar = 100 µm for C–F.

    Journal: PLoS ONE

    Article Title: Inhibition of E2F1/CDK1 Pathway Attenuates Neuronal Apoptosis In Vitro and Confers Neuroprotection after Spinal Cord Injury In Vivo

    doi: 10.1371/journal.pone.0042129

    Figure Lengend Snippet: A . Coronal section in intact spinal cord (a–c) shows that E2F1 was expressed in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of E2F1 (d–f) was increased, and highly expressed by motor neurons. The upregulation of E2F1 was clearly attenuated by CR8 treatment (g–i). B . In intact spinal cord (a–c), CDK1/NeuN was detected in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of CDK1 (d–f) was increased, and highly expressed by motor neurons. CDK1 upregulation was attenuated by CR8 treatment (g–i). All images were taken at 2 mm rostral to epicenter. Scale bar = 100 µm for C–F.

    Article Snippet: The following antibodies and reagents were obtained from commercial sources: polyclonal rabbit anti-CDK1, cyclin B1, cyclin A, Bim, and c-Myb (Santa Cruz Biotechnology), mouse anti-CDK1 (Santa Cruz Biotechnology), mouse anti-E2F1 (BD pharmingenTM), rabbit anti-phospho(Ser)-CDK substrate, rabbit anti-cleaved caspase 3 (Cell Signaling Technology), anti-pS54-n-myc (Bethyl Laboratories Inc), rabbit anti-β-galactosidase (MP Biomedicals), monoclonal mouse anti-GAPDH and NeuN (Chemicon), mouse anti-fodrin (Affinity Research Products), mouse anti-APC (CC1, Abcam), mouse anti-CD11b (OX42, Serotec), Hoechst 33258 and other reagents and supplies (Sigma).

    Techniques:

    Western blot analysis of cdc2 (CDK1) and cdc25C in Abrams OSA cells at day 4 and 5. Both CPFX and ENFX inhibit G 2 checkpoint kinase cdc2 although CPFX showed more potent than ENFX. The level of phospho-cdc25C was increased in both CPFX and ENFX treated canine Abrams OSA cells.

    Journal: PLoS ONE

    Article Title: Fluoroquinolone-Mediated Inhibition of Cell Growth, S-G 2 /M Cell Cycle Arrest, and Apoptosis in Canine Osteosarcoma Cell Lines

    doi: 10.1371/journal.pone.0042960

    Figure Lengend Snippet: Western blot analysis of cdc2 (CDK1) and cdc25C in Abrams OSA cells at day 4 and 5. Both CPFX and ENFX inhibit G 2 checkpoint kinase cdc2 although CPFX showed more potent than ENFX. The level of phospho-cdc25C was increased in both CPFX and ENFX treated canine Abrams OSA cells.

    Article Snippet: Rabbit polyclonal anti-cdc2, mouse monoclonal anti-actin, and anti-p21 were purchased form Santa Cruz Biotechnology.

    Techniques: Western Blot

    (A) BJAB cells transfected with the pA3M vector or pA3M-LANA were treated with nocodazole (200 ng/mL) for 24 hours. The cells were then harvested, total cell lysate were prepared and western blot was performed using antibodies against cyclin B1, Cdc2, Tyr15-phosphorylated Cdc2 [Cdc2 (Tyr15)], and Histone H3 as a protein loading control. (B) BJAB cells transfected with the pA3M vector or pA3M-LANA were grown in 6 well culture plates and treated with nocodazole and observed for colocolaization in a confocal microscope. The result shown is the representative of 3 independent experiments. +, present; −, absent.

    Journal: PLoS ONE

    Article Title: Kaposi Sarcoma Herpes Virus Latency Associated Nuclear Antigen Protein Release the G2/M Cell Cycle Blocks by Modulating ATM/ATR Mediated Checkpoint Pathway

    doi: 10.1371/journal.pone.0100228

    Figure Lengend Snippet: (A) BJAB cells transfected with the pA3M vector or pA3M-LANA were treated with nocodazole (200 ng/mL) for 24 hours. The cells were then harvested, total cell lysate were prepared and western blot was performed using antibodies against cyclin B1, Cdc2, Tyr15-phosphorylated Cdc2 [Cdc2 (Tyr15)], and Histone H3 as a protein loading control. (B) BJAB cells transfected with the pA3M vector or pA3M-LANA were grown in 6 well culture plates and treated with nocodazole and observed for colocolaization in a confocal microscope. The result shown is the representative of 3 independent experiments. +, present; −, absent.

    Article Snippet: Polyclonal rabbit anti-phospho-Tyr15 Cdc2, mouse monoclonal Cdc2, mouse monoclonal cyclin B1, anti-HA rabbit polyclonal antibody, anti-Myc mouse monoclonal antibody, rabbit polyclonal anti-β–actin, HRP conjugated mouse and rabbit polyclonal antibodies were all purchased from Santa Cruz Biotechnology (USA), IMGENEX Corporation (USA) or Cell Signaling Technology, Inc. (USA).

    Techniques: Transfection, Plasmid Preparation, Western Blot, Microscopy

    Nocodazole treatment reduces the level of phosphorylated Cdc2. The viral nuclear antigen LANA binds directly to Chk2, which may result in the phosphorylation of Cdc25c and sequester it in the cytoplasm. Thus, it may be unable to regulate the phosphorylation of nuclear Cdc2 resulting the activation of cyclin B-Cdc2 and progression through the G2/M phase, releasing the nocodozole induced block.

    Journal: PLoS ONE

    Article Title: Kaposi Sarcoma Herpes Virus Latency Associated Nuclear Antigen Protein Release the G2/M Cell Cycle Blocks by Modulating ATM/ATR Mediated Checkpoint Pathway

    doi: 10.1371/journal.pone.0100228

    Figure Lengend Snippet: Nocodazole treatment reduces the level of phosphorylated Cdc2. The viral nuclear antigen LANA binds directly to Chk2, which may result in the phosphorylation of Cdc25c and sequester it in the cytoplasm. Thus, it may be unable to regulate the phosphorylation of nuclear Cdc2 resulting the activation of cyclin B-Cdc2 and progression through the G2/M phase, releasing the nocodozole induced block.

    Article Snippet: Polyclonal rabbit anti-phospho-Tyr15 Cdc2, mouse monoclonal Cdc2, mouse monoclonal cyclin B1, anti-HA rabbit polyclonal antibody, anti-Myc mouse monoclonal antibody, rabbit polyclonal anti-β–actin, HRP conjugated mouse and rabbit polyclonal antibodies were all purchased from Santa Cruz Biotechnology (USA), IMGENEX Corporation (USA) or Cell Signaling Technology, Inc. (USA).

    Techniques: Activation Assay, Blocking Assay

    Journal: Cell Reports

    Article Title: The Arabidopsis F-box protein FBW2 targets AGO1 for degradation to prevent spurious loading of illegitimate small RNA

    doi: 10.1016/j.celrep.2022.110671

    Figure Lengend Snippet:

    Article Snippet: Rabbit polyclonal anti-CDC2 PSTAIRE , Santa Cruz Biotechnology , Cat# sc-53, RRID:AB_2074908.

    Techniques: Recombinant, SYBR Green Assay, Western Blot, Protease Inhibitor, Isolation, Magnetic Beads, Mass Spectrometry, Clone Assay, Sequencing, Software

    Primary and secondary antibodies used for immunohistochemistry.

    Journal: Frontiers in Endocrinology

    Article Title: Selective Depletion of Adult GFAP-Expressing Tanycytes Leads to Hypogonadotropic Hypogonadism in Males

    doi: 10.3389/fendo.2022.869019

    Figure Lengend Snippet: Primary and secondary antibodies used for immunohistochemistry.

    Article Snippet: ERα , Santa Cruz-MC20, rabbit polyclonal, #sc542 , , 1,200 , Donkey anti-rabbit IgG, Alexa 488 , Molecular Probes, #A21206 , 1,600.

    Techniques: Immunohistochemistry

    KEY RESOURCES TABLE

    Journal: Cancer cell

    Article Title: Comprehensive Molecular Characterization Identifies Distinct Genomic and Immune Hallmarks of Renal Medullary Carcinoma

    doi: 10.1016/j.ccell.2020.04.002

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: The following primary antibodies were used: mouse monoclonal anti-SMARCB1 antibody clone 2C2 (Sigma-Aldrich; SAB4200202), rabbit polyclonal anti-phospho-Histone H2A.X at serine 139 (γH2AX; Cell Signaling Technology; 2577), mouse monoclonal anti-c-MYC antibody 9E10 (Santa Cruz Biotechology; sc-40), rabbit polyclonal anti-PARP (Cell Signaling Technology; 9542), goat polyclonal anti-ATR (Santa Cruz Biotechnology; sc-1887), rabbit polyclonal anti-phospho-ATR at serine 428 (Cell Signaling Technology; 2853), mouse monoclonal anti-TP53 (Santa Cruz Biotechnology; sc-126), rabbit polyclonal anti-phospho-TP53 at serine 15 (Cell Signaling Technology; 9284), mouse monoclonal anti-actin (Santa Cruz Biotechnology; sc- 47778), rabbit polyclonal anti-phospho-CDK1 at tyrosine 15 (Cell Signaling Technology; 9111), mouse monoclonal anti-RPA 32 kDa subunit 9H8 (Santa Cruz Biotechology; sc-56770), rabbit polyclonal anti-phospho-RPA32 at serines 4 and 8 (Bethyl Laboratories; A300–245A), mouse monoclonal anti-FANCD2 (Santa Cruz Biotechology; sc-20022).

    Techniques: Recombinant, DNA Methylation Assay, Empire Assay, Imaging, Sequencing, Plasmid Preparation, Software