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a08632 boster mad2 antibody  (Boster Bio)


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    Structured Review

    Boster Bio a08632 boster mad2 antibody
    A08632 Boster Mad2 Antibody, supplied by Boster Bio, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/a08632 boster mad2 antibody/product/Boster Bio
    Average 93 stars, based on 2 article reviews
    a08632 boster mad2 antibody - by Bioz Stars, 2026-03
    93/100 stars

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    Pan-Cancer Analysis of <t>SGO2</t> Expression ( A ) SGO2 expression profiles across pan-cancers were analyzed using data from the TCGA database. Tumor samples (represented as red boxes) were compared against normal samples (represented as blue boxes) via the Mann-Whitney U test to assess expression differences. ( B ) SGO2 expression patterns across pan-cancers were interrogated utilizing the GEPIA web platform. Tumor samples (depicted as red dots) were contrasted with normal samples (depicted as green dots), with statistical testing following GEPIA’s default analytical pipeline (*p < 0.05, **p < 0.01,***p < 0.001).
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    Pan-Cancer Analysis of <t>SGO2</t> Expression ( A ) SGO2 expression profiles across pan-cancers were analyzed using data from the TCGA database. Tumor samples (represented as red boxes) were compared against normal samples (represented as blue boxes) via the Mann-Whitney U test to assess expression differences. ( B ) SGO2 expression patterns across pan-cancers were interrogated utilizing the GEPIA web platform. Tumor samples (depicted as red dots) were contrasted with normal samples (depicted as green dots), with statistical testing following GEPIA’s default analytical pipeline (*p < 0.05, **p < 0.01,***p < 0.001).
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    Thermo Fisher sgo2
    (A) Heatmap showing canonical protein abundance profile for experimentally validated APC/C recognition motifs in both Time Course and Mitotic Exit datasets. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). Degradation motifs are indicated with different colours. Proteins not detected are shown with a dashed box. (B) The proportion of CCD proteins with experimentally validated APC/C recognition motifs and established degradation mechanisms (purple) versus those without a known mechanism (light grey). Proteins found to contain unstable peptides in a global peptide stability dataset are also shown in dark grey. (C) Heatmap showing protein abundance changes for CCD proteins predicted to contain a degradation motif with high confidence and selected for validations. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). (D) Representative western blot analysis (n=3) of predicted mitotic APC/C substrates degradation in Hela Kyoto cells during the override of a mitotic checkpoint arrest by the CDK1 inhibitor RO-3306 in the presence and absence of ANAPC4. <t>SGO2,</t> GTSE1, MELK, FAM38D and known APC/C substrates (CCNB1) are stabilised by proteasome inhibition with MG132.
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    sgo2  (Bethyl)
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    (A) Heatmap showing canonical protein abundance profile for experimentally validated APC/C recognition motifs in both Time Course and Mitotic Exit datasets. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). Degradation motifs are indicated with different colours. Proteins not detected are shown with a dashed box. (B) The proportion of CCD proteins with experimentally validated APC/C recognition motifs and established degradation mechanisms (purple) versus those without a known mechanism (light grey). Proteins found to contain unstable peptides in a global peptide stability dataset are also shown in dark grey. (C) Heatmap showing protein abundance changes for CCD proteins predicted to contain a degradation motif with high confidence and selected for validations. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). (D) Representative western blot analysis (n=3) of predicted mitotic APC/C substrates degradation in Hela Kyoto cells during the override of a mitotic checkpoint arrest by the CDK1 inhibitor RO-3306 in the presence and absence of ANAPC4. <t>SGO2,</t> GTSE1, MELK, FAM38D and known APC/C substrates (CCNB1) are stabilised by proteasome inhibition with MG132.
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    CH Instruments antibodies against sgo2
    (A) Heatmap showing canonical protein abundance profile for experimentally validated APC/C recognition motifs in both Time Course and Mitotic Exit datasets. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). Degradation motifs are indicated with different colours. Proteins not detected are shown with a dashed box. (B) The proportion of CCD proteins with experimentally validated APC/C recognition motifs and established degradation mechanisms (purple) versus those without a known mechanism (light grey). Proteins found to contain unstable peptides in a global peptide stability dataset are also shown in dark grey. (C) Heatmap showing protein abundance changes for CCD proteins predicted to contain a degradation motif with high confidence and selected for validations. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). (D) Representative western blot analysis (n=3) of predicted mitotic APC/C substrates degradation in Hela Kyoto cells during the override of a mitotic checkpoint arrest by the CDK1 inhibitor RO-3306 in the presence and absence of ANAPC4. <t>SGO2,</t> GTSE1, MELK, FAM38D and known APC/C substrates (CCNB1) are stabilised by proteasome inhibition with MG132.
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    Thermo Fisher sgo2 coding sequence
    (A) Heatmap showing canonical protein abundance profile for experimentally validated APC/C recognition motifs in both Time Course and Mitotic Exit datasets. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). Degradation motifs are indicated with different colours. Proteins not detected are shown with a dashed box. (B) The proportion of CCD proteins with experimentally validated APC/C recognition motifs and established degradation mechanisms (purple) versus those without a known mechanism (light grey). Proteins found to contain unstable peptides in a global peptide stability dataset are also shown in dark grey. (C) Heatmap showing protein abundance changes for CCD proteins predicted to contain a degradation motif with high confidence and selected for validations. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). (D) Representative western blot analysis (n=3) of predicted mitotic APC/C substrates degradation in Hela Kyoto cells during the override of a mitotic checkpoint arrest by the CDK1 inhibitor RO-3306 in the presence and absence of ANAPC4. <t>SGO2,</t> GTSE1, MELK, FAM38D and known APC/C substrates (CCNB1) are stabilised by proteasome inhibition with MG132.
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    Image Search Results


    Pan-Cancer Analysis of SGO2 Expression ( A ) SGO2 expression profiles across pan-cancers were analyzed using data from the TCGA database. Tumor samples (represented as red boxes) were compared against normal samples (represented as blue boxes) via the Mann-Whitney U test to assess expression differences. ( B ) SGO2 expression patterns across pan-cancers were interrogated utilizing the GEPIA web platform. Tumor samples (depicted as red dots) were contrasted with normal samples (depicted as green dots), with statistical testing following GEPIA’s default analytical pipeline (*p < 0.05, **p < 0.01,***p < 0.001).

    Journal: Scientific Reports

    Article Title: Elevated SGO2 expression in lung adenocarcinoma promotes migration and invasion via MAD2 and correlates with poor prognosis

    doi: 10.1038/s41598-025-10993-0

    Figure Lengend Snippet: Pan-Cancer Analysis of SGO2 Expression ( A ) SGO2 expression profiles across pan-cancers were analyzed using data from the TCGA database. Tumor samples (represented as red boxes) were compared against normal samples (represented as blue boxes) via the Mann-Whitney U test to assess expression differences. ( B ) SGO2 expression patterns across pan-cancers were interrogated utilizing the GEPIA web platform. Tumor samples (depicted as red dots) were contrasted with normal samples (depicted as green dots), with statistical testing following GEPIA’s default analytical pipeline (*p < 0.05, **p < 0.01,***p < 0.001).

    Article Snippet: SGO2 antibody , 1:1000 , A08632 , Boster.

    Techniques: Expressing, MANN-WHITNEY

    Investigation of SGO2 Expression in LUAD. ( A ) Paired comparison: SGO2 expression in tumor vs. matched adjacent normal tissues from LUAD patients (paired t-test). ( B ) Unpaired comparison: SGO2 expression in tumor vs. normal tissues (unpaired t-test). ( C ) Immunohistochemical validation: Immunohistochemical analysis assessed SGO2 expression in LUAD tumor tissues and adjacent peri-tumor tissues from 21 patients (n = 21). Comparison of relative SGO2 expression levels (top) and positive staining area percentages (bottom) between tumor and peri-tumor tissues used paired t-test. ( D ) Clinical stage-related analysis: Based on the TCGA database, SGO2 expression was analyzed across subgroups of T stage, N stage, M stage, and pathological stage. Statistical method: One-way ANOVA with Bonferroni post-hoc test. (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001).

    Journal: Scientific Reports

    Article Title: Elevated SGO2 expression in lung adenocarcinoma promotes migration and invasion via MAD2 and correlates with poor prognosis

    doi: 10.1038/s41598-025-10993-0

    Figure Lengend Snippet: Investigation of SGO2 Expression in LUAD. ( A ) Paired comparison: SGO2 expression in tumor vs. matched adjacent normal tissues from LUAD patients (paired t-test). ( B ) Unpaired comparison: SGO2 expression in tumor vs. normal tissues (unpaired t-test). ( C ) Immunohistochemical validation: Immunohistochemical analysis assessed SGO2 expression in LUAD tumor tissues and adjacent peri-tumor tissues from 21 patients (n = 21). Comparison of relative SGO2 expression levels (top) and positive staining area percentages (bottom) between tumor and peri-tumor tissues used paired t-test. ( D ) Clinical stage-related analysis: Based on the TCGA database, SGO2 expression was analyzed across subgroups of T stage, N stage, M stage, and pathological stage. Statistical method: One-way ANOVA with Bonferroni post-hoc test. (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001).

    Article Snippet: SGO2 antibody , 1:1000 , A08632 , Boster.

    Techniques: Expressing, Comparison, Immunohistochemical staining, Biomarker Discovery, Staining

    Elevated SGO2 expression was associated with poor prognosis in LUAD patients. ( A-C ) Kaplan-Meier survival analyses (via log-rank test) from TCGA database comparing LUAD patients with high vs. low SGO2 expression (stratified by median). ( A ) OS: High-expression group (n = 265) showed significantly worse prognosis than low-expression group (n = 265) (HR = 1.64, p < 0.001). ( B ) DSS: High-expression group (n = 247) had poorer outcomes than low-expression group (n = 248) (HR = 1.87, p < 0.001). ( C ) PFS: High-expression group (n = 265) exhibited shorter PFS than low-expression group (n = 265) (HR = 1.47, p = 0.005). ( D-E ) Validation in GEO datasets (log-rank test): ( D ) GSE13213 : High-expression group (n = 75) had significantly reduced survival vs. low-expression group (n = 42) (p < 0.01). ( E ) GSE31210 : High-expression group (n=84) showed worse prognosis compared to low-expression group (n = 120) (p = 0.005). HR: Hazard ratio.

    Journal: Scientific Reports

    Article Title: Elevated SGO2 expression in lung adenocarcinoma promotes migration and invasion via MAD2 and correlates with poor prognosis

    doi: 10.1038/s41598-025-10993-0

    Figure Lengend Snippet: Elevated SGO2 expression was associated with poor prognosis in LUAD patients. ( A-C ) Kaplan-Meier survival analyses (via log-rank test) from TCGA database comparing LUAD patients with high vs. low SGO2 expression (stratified by median). ( A ) OS: High-expression group (n = 265) showed significantly worse prognosis than low-expression group (n = 265) (HR = 1.64, p < 0.001). ( B ) DSS: High-expression group (n = 247) had poorer outcomes than low-expression group (n = 248) (HR = 1.87, p < 0.001). ( C ) PFS: High-expression group (n = 265) exhibited shorter PFS than low-expression group (n = 265) (HR = 1.47, p = 0.005). ( D-E ) Validation in GEO datasets (log-rank test): ( D ) GSE13213 : High-expression group (n = 75) had significantly reduced survival vs. low-expression group (n = 42) (p < 0.01). ( E ) GSE31210 : High-expression group (n=84) showed worse prognosis compared to low-expression group (n = 120) (p = 0.005). HR: Hazard ratio.

    Article Snippet: SGO2 antibody , 1:1000 , A08632 , Boster.

    Techniques: Expressing, Biomarker Discovery

    The diagnostic ROC curve for SGO2. ( A ) Receiver operating characteristic (ROC) curve evaluating SGO2 expression as a diagnostic biomarker for LUAD. The area under the curve (AUC) was 0.873 (95% CI: 0.843-0.903), indicating high discriminatory power.

    Journal: Scientific Reports

    Article Title: Elevated SGO2 expression in lung adenocarcinoma promotes migration and invasion via MAD2 and correlates with poor prognosis

    doi: 10.1038/s41598-025-10993-0

    Figure Lengend Snippet: The diagnostic ROC curve for SGO2. ( A ) Receiver operating characteristic (ROC) curve evaluating SGO2 expression as a diagnostic biomarker for LUAD. The area under the curve (AUC) was 0.873 (95% CI: 0.843-0.903), indicating high discriminatory power.

    Article Snippet: SGO2 antibody , 1:1000 , A08632 , Boster.

    Techniques: Diagnostic Assay, Expressing, Biomarker Discovery

    SGO2 expression in LUAD cell lines relative to normal Beas-2B cells. ( A ) Combined subpanels showing relative SGO2 mRNA expression: ( a-c ) Relative SGO2 mRNA expression in A549 ( a ), H1975( b ) and H1299 ( c ) cells, normalized to Beas-2B. (n = 3, Student’s t-test). ( B-C ) Representative western blot ( B ) and quantitative analysis ( C ) of SGO2 protein expression in the same cell lines. \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\beta$$\end{document} -actin served as the loading control (n = 3, one-way ANOVA with Tukey’s post hoc test). Original blots are shown in Fig. . (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001).

    Journal: Scientific Reports

    Article Title: Elevated SGO2 expression in lung adenocarcinoma promotes migration and invasion via MAD2 and correlates with poor prognosis

    doi: 10.1038/s41598-025-10993-0

    Figure Lengend Snippet: SGO2 expression in LUAD cell lines relative to normal Beas-2B cells. ( A ) Combined subpanels showing relative SGO2 mRNA expression: ( a-c ) Relative SGO2 mRNA expression in A549 ( a ), H1975( b ) and H1299 ( c ) cells, normalized to Beas-2B. (n = 3, Student’s t-test). ( B-C ) Representative western blot ( B ) and quantitative analysis ( C ) of SGO2 protein expression in the same cell lines. \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\beta$$\end{document} -actin served as the loading control (n = 3, one-way ANOVA with Tukey’s post hoc test). Original blots are shown in Fig. . (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001).

    Article Snippet: SGO2 antibody , 1:1000 , A08632 , Boster.

    Techniques: Expressing, Western Blot, Control

    SGO2 knockdown suppressed malignant behaviors in LUAD cells. ( A-B ) Validation of siRNA-mediated SGO2 knockdown efficiency by ( A ) qPCR and ( B ) Western blot. (n = 3, one-way ANOVA with Tukey’s post hoc test). ( C-E ) Proliferation (CCK-8), migration (wound healing), and invasion (Matrigel) assays in SGO2-depleted H1299 cells. (n = 3, Student’s t-test). ( F ) Western blot analysis of EMT markers (N-cadherin, E-cadherin, Vimentin) in SGO2-knockdown H1299 cells with \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\beta$$\end{document} -actin served as loading control. (n = 3, Student’s t-test). Original blots are shown in Fig. . (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001).

    Journal: Scientific Reports

    Article Title: Elevated SGO2 expression in lung adenocarcinoma promotes migration and invasion via MAD2 and correlates with poor prognosis

    doi: 10.1038/s41598-025-10993-0

    Figure Lengend Snippet: SGO2 knockdown suppressed malignant behaviors in LUAD cells. ( A-B ) Validation of siRNA-mediated SGO2 knockdown efficiency by ( A ) qPCR and ( B ) Western blot. (n = 3, one-way ANOVA with Tukey’s post hoc test). ( C-E ) Proliferation (CCK-8), migration (wound healing), and invasion (Matrigel) assays in SGO2-depleted H1299 cells. (n = 3, Student’s t-test). ( F ) Western blot analysis of EMT markers (N-cadherin, E-cadherin, Vimentin) in SGO2-knockdown H1299 cells with \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\beta$$\end{document} -actin served as loading control. (n = 3, Student’s t-test). Original blots are shown in Fig. . (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001).

    Article Snippet: SGO2 antibody , 1:1000 , A08632 , Boster.

    Techniques: Knockdown, Biomarker Discovery, Western Blot, CCK-8 Assay, Migration, Control

    Knockdown of SGO2 affected the cell cycle in LUAD cells. ( A ) Flow cytometry analysis of cell cycle distribution (G1, S, G2/M phases) in si-SGO2 and si-NC groups. (n = 3, two-way ANOVA with Sidak’s test). ( B ) Western blot of cell cycle proteins (Cyclin B1, Cyclin D1). \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\beta$$\end{document} -actin served as control (n = 3, Student’s t-test). Original blots are shown in Fig. . (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001).

    Journal: Scientific Reports

    Article Title: Elevated SGO2 expression in lung adenocarcinoma promotes migration and invasion via MAD2 and correlates with poor prognosis

    doi: 10.1038/s41598-025-10993-0

    Figure Lengend Snippet: Knockdown of SGO2 affected the cell cycle in LUAD cells. ( A ) Flow cytometry analysis of cell cycle distribution (G1, S, G2/M phases) in si-SGO2 and si-NC groups. (n = 3, two-way ANOVA with Sidak’s test). ( B ) Western blot of cell cycle proteins (Cyclin B1, Cyclin D1). \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\beta$$\end{document} -actin served as control (n = 3, Student’s t-test). Original blots are shown in Fig. . (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001).

    Article Snippet: SGO2 antibody , 1:1000 , A08632 , Boster.

    Techniques: Knockdown, Flow Cytometry, Western Blot, Control

    SGO2 regulated LUAD cell migration and invasion via MAD2. ( A ) GO and KEGG enrichment analysis of genes associated with SGO2. (The use permission from Kanehisa Laboratories has been obtained.) ( B ) Correlation analysis between SGO2 and MAD2 expression (Pearson’s R = 0.62, p < 0.001). ( C-D ) Verification of SGO2 overexpression efficiency using qPCR and Western blot, and analysis of MAD2 expression following SGO2 knockdown or overexpression (n = 3, Student’s t-test). ( E ) Invasion and migration assays of H1299 cells in three groups: SGO2 overexpression (OE-SGO2), control (OE-SGO2-NC), and SGO2-OE with MAD2 inhibitor (OE-M2I-1) (n = 3, one-way ANOVA with Tukey’s post hoc test). Original blots are shown in Fig. . (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001).

    Journal: Scientific Reports

    Article Title: Elevated SGO2 expression in lung adenocarcinoma promotes migration and invasion via MAD2 and correlates with poor prognosis

    doi: 10.1038/s41598-025-10993-0

    Figure Lengend Snippet: SGO2 regulated LUAD cell migration and invasion via MAD2. ( A ) GO and KEGG enrichment analysis of genes associated with SGO2. (The use permission from Kanehisa Laboratories has been obtained.) ( B ) Correlation analysis between SGO2 and MAD2 expression (Pearson’s R = 0.62, p < 0.001). ( C-D ) Verification of SGO2 overexpression efficiency using qPCR and Western blot, and analysis of MAD2 expression following SGO2 knockdown or overexpression (n = 3, Student’s t-test). ( E ) Invasion and migration assays of H1299 cells in three groups: SGO2 overexpression (OE-SGO2), control (OE-SGO2-NC), and SGO2-OE with MAD2 inhibitor (OE-M2I-1) (n = 3, one-way ANOVA with Tukey’s post hoc test). Original blots are shown in Fig. . (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001).

    Article Snippet: SGO2 antibody , 1:1000 , A08632 , Boster.

    Techniques: Migration, Expressing, Over Expression, Western Blot, Knockdown, Control

    (A) Heatmap showing canonical protein abundance profile for experimentally validated APC/C recognition motifs in both Time Course and Mitotic Exit datasets. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). Degradation motifs are indicated with different colours. Proteins not detected are shown with a dashed box. (B) The proportion of CCD proteins with experimentally validated APC/C recognition motifs and established degradation mechanisms (purple) versus those without a known mechanism (light grey). Proteins found to contain unstable peptides in a global peptide stability dataset are also shown in dark grey. (C) Heatmap showing protein abundance changes for CCD proteins predicted to contain a degradation motif with high confidence and selected for validations. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). (D) Representative western blot analysis (n=3) of predicted mitotic APC/C substrates degradation in Hela Kyoto cells during the override of a mitotic checkpoint arrest by the CDK1 inhibitor RO-3306 in the presence and absence of ANAPC4. SGO2, GTSE1, MELK, FAM38D and known APC/C substrates (CCNB1) are stabilised by proteasome inhibition with MG132.

    Journal: bioRxiv

    Article Title: High resolution profiling of cell cycle-dependent protein and phosphorylation abundance changes in non-transformed cells

    doi: 10.1101/2024.06.20.599917

    Figure Lengend Snippet: (A) Heatmap showing canonical protein abundance profile for experimentally validated APC/C recognition motifs in both Time Course and Mitotic Exit datasets. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). Degradation motifs are indicated with different colours. Proteins not detected are shown with a dashed box. (B) The proportion of CCD proteins with experimentally validated APC/C recognition motifs and established degradation mechanisms (purple) versus those without a known mechanism (light grey). Proteins found to contain unstable peptides in a global peptide stability dataset are also shown in dark grey. (C) Heatmap showing protein abundance changes for CCD proteins predicted to contain a degradation motif with high confidence and selected for validations. Protein changes are coloured according to their abundance (log 2 palbociclib arrest normalised values). (D) Representative western blot analysis (n=3) of predicted mitotic APC/C substrates degradation in Hela Kyoto cells during the override of a mitotic checkpoint arrest by the CDK1 inhibitor RO-3306 in the presence and absence of ANAPC4. SGO2, GTSE1, MELK, FAM38D and known APC/C substrates (CCNB1) are stabilised by proteasome inhibition with MG132.

    Article Snippet: After 1 h blocking with 5% milk in TBST at room temperature (RT) for 1 h, membranes were incubated overnight at 4°C with the following primary antibodies: CCND1 (Santa Cruz Biotechnology, sc-2004), CCND3 (Santa Cruz Biotechnology, sc-6283), CCNE2 (Santa Cruz Biotechnology, sc-248), CCNA (Santa Cruz Biotechnology, sc-271682), CCNA (Santa Cruz Biotechnology, sc-596), CCNB1 (Santa Cruz Biotechnology, sc-245), GAPDH (Santa Cruz Biotechnology, sc-51907), CDK1 pT161 (Cell Signalling Technology, 9114), CDK1 pY15 (Cell Signalling Technology, 9111), Alpha Tubulin (Abcam, ab52866), PLK1(Millipore, 05-844), CDK2 (Santa Cruz Biotechnology, sc-163), CDK1 (Abcam, ab32094), CDC20 (Santa Cruz Biotechnology, sc-13162), UBR7 (Thermo Fisher Scientific, A304-130A), UBE2S (Cell Signalling Technology, 11878), CDKN1B (Dako, M7203), CDKN1B pS10 (Santa Cruz Biotechnology, sc-12939), NCL (Abcam, ab22758), NCL pT76 (Abcam, ab168363), CCNB1 (Santa Cruz Biotechnology, sc-245), SGO2 (Thermo Fisher Scientific, A301-261A), GTSE1 (Abnova, H00051512-B01P), MELK (Thermo Fisher Scientific, A303-136A), FAM83D (Custom antibody from Erich Nigg), ANAPC4 (Thermo Fisher Scientific, A301-175A), Phospho-CDK substrate motif [(K/H)pSP] (Cell Signalling Technology, 9477), JUNB (Proteintech, 10486-1-AP), CHAF1B (Thermo Fisher Scientific, A301-085A), Histone H3 pS10 (Cell Signalling Technology, 3377), Actin (Sigma-Aldrich, A5441).

    Techniques: Western Blot, Inhibition