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  • 91
    MedChemExpress hy13404
    Hy13404, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Proteintech pdp2
    Pdp2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cell Signaling Technology Inc α rad17 ps635
    Identification of <t>RAD17</t> as an SMG7-binding protein. ( a ) Verification of SMG7-binding proteins identified from complex purification. The total cell lysates and α-Flag/HA immunoprecipitated materials from H1299 and H1299-FH-SMG7 cells were assayed by western blot analysis using <t>α-RAD17,</t> α-UPF1, α-SMG5, and α-HA (SMG7) antibodies. ( b ) Schematic presentation of the RAD17 domain structure containing P-loop, Walker B, Sensor 1, Sensor 2 and C-terminal highlighted SQ motifs. ( c ) As in ( a ), the total cell lysates and α-Flag immunoprecipitates from H1299 and H1299-FH-SMG7 cells were assayed by western blot analysis using α-RAD17, α-RAD17-pS645, α-SMG7, α-RFC2 and α-RFC3 antibodies. ( d ) H1299 cells were transfected with SMG7- and RAD17-expressing plasmid DNA, and the cell extracts and α-Flag immunoprecipitated materials were analyzed by western blot with α-RAD17 and α-HA (SMG7) antibodies. ( e ) The total cell extracts and α-Flag immunoprecipitated materials from H1299 cells transfected with empty vector or FH-RAD17-expression plasmid DNA were examined by western blot analysis using α-SMG7 and α-RAD17 antibodies. ( f – g ) SMG7 direct binding to RAD17 in vitro. GST, full-length GST-RAD17 ( f ), or truncated GST-RAD17 fragment ( g ) fusion proteins were used in pulldown assays with purified FH-SMG7 proteins. FH-SMG7 was detected by western blot analysis using α-SMG7 antibody, and GST proteins visualized by Ponceau S staining in ( f ) and Supplementary Fig. d.
    α Rad17 Ps635, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Proteintech rabbit polyclonal pdp2 antibody
    (A) GST pull-down demonstrating that purified GST-Rheb binds endogenous PDP1 in the brain (A, top panel) and <t>PDP2</t> in the liver (A, middle panel).
    Rabbit Polyclonal Pdp2 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    MathWorks Inc 13 404 405 simulation 406 matlab simulations
    (A) GST pull-down demonstrating that purified GST-Rheb binds endogenous PDP1 in the brain (A, top panel) and <t>PDP2</t> in the liver (A, middle panel).
    13 404 405 Simulation 406 Matlab Simulations, supplied by MathWorks Inc, 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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    Image Search Results


    Identification of RAD17 as an SMG7-binding protein. ( a ) Verification of SMG7-binding proteins identified from complex purification. The total cell lysates and α-Flag/HA immunoprecipitated materials from H1299 and H1299-FH-SMG7 cells were assayed by western blot analysis using α-RAD17, α-UPF1, α-SMG5, and α-HA (SMG7) antibodies. ( b ) Schematic presentation of the RAD17 domain structure containing P-loop, Walker B, Sensor 1, Sensor 2 and C-terminal highlighted SQ motifs. ( c ) As in ( a ), the total cell lysates and α-Flag immunoprecipitates from H1299 and H1299-FH-SMG7 cells were assayed by western blot analysis using α-RAD17, α-RAD17-pS645, α-SMG7, α-RFC2 and α-RFC3 antibodies. ( d ) H1299 cells were transfected with SMG7- and RAD17-expressing plasmid DNA, and the cell extracts and α-Flag immunoprecipitated materials were analyzed by western blot with α-RAD17 and α-HA (SMG7) antibodies. ( e ) The total cell extracts and α-Flag immunoprecipitated materials from H1299 cells transfected with empty vector or FH-RAD17-expression plasmid DNA were examined by western blot analysis using α-SMG7 and α-RAD17 antibodies. ( f – g ) SMG7 direct binding to RAD17 in vitro. GST, full-length GST-RAD17 ( f ), or truncated GST-RAD17 fragment ( g ) fusion proteins were used in pulldown assays with purified FH-SMG7 proteins. FH-SMG7 was detected by western blot analysis using α-SMG7 antibody, and GST proteins visualized by Ponceau S staining in ( f ) and Supplementary Fig. d.

    Journal: Scientific Reports

    Article Title: Critical role of SMG7 in activation of the ATR-CHK1 axis in response to genotoxic stress

    doi: 10.1038/s41598-021-86957-x

    Figure Lengend Snippet: Identification of RAD17 as an SMG7-binding protein. ( a ) Verification of SMG7-binding proteins identified from complex purification. The total cell lysates and α-Flag/HA immunoprecipitated materials from H1299 and H1299-FH-SMG7 cells were assayed by western blot analysis using α-RAD17, α-UPF1, α-SMG5, and α-HA (SMG7) antibodies. ( b ) Schematic presentation of the RAD17 domain structure containing P-loop, Walker B, Sensor 1, Sensor 2 and C-terminal highlighted SQ motifs. ( c ) As in ( a ), the total cell lysates and α-Flag immunoprecipitates from H1299 and H1299-FH-SMG7 cells were assayed by western blot analysis using α-RAD17, α-RAD17-pS645, α-SMG7, α-RFC2 and α-RFC3 antibodies. ( d ) H1299 cells were transfected with SMG7- and RAD17-expressing plasmid DNA, and the cell extracts and α-Flag immunoprecipitated materials were analyzed by western blot with α-RAD17 and α-HA (SMG7) antibodies. ( e ) The total cell extracts and α-Flag immunoprecipitated materials from H1299 cells transfected with empty vector or FH-RAD17-expression plasmid DNA were examined by western blot analysis using α-SMG7 and α-RAD17 antibodies. ( f – g ) SMG7 direct binding to RAD17 in vitro. GST, full-length GST-RAD17 ( f ), or truncated GST-RAD17 fragment ( g ) fusion proteins were used in pulldown assays with purified FH-SMG7 proteins. FH-SMG7 was detected by western blot analysis using α-SMG7 antibody, and GST proteins visualized by Ponceau S staining in ( f ) and Supplementary Fig. d.

    Article Snippet: The following antibodies were from Cell Signaling Technology: α-ATM-pS1981 (5883, 1:1000), α-ATM (2873, 1:1000), α-CHK1-pS345 (2348, 1:1000), α-CHK2-pT68 (2661, 1:1000), α-CHK2 (2662, 1:1000), α-RAD17-pS635 (13404S, 1:1000), α-RAD17 (8561, 1:1000), α-RPA32 (2208S, IF 1:1000), α-Histone H3 (3638, 1:2000), α-rabbit IgG-HRP (7074, 1:5000).

    Techniques: Binding Assay, Purification, Immunoprecipitation, Western Blot, Transfection, Expressing, Plasmid Preparation, In Vitro, Staining

    SMG7 maintains normal attenuation of the ATR-CHK1 axis during recovery from replication stress. ( a ) Wild type and SMG7 −/− HCT116 cells were pulsed with 25 μm BrdU followed by treatment with 5 mM HU for 6 h. After HU treatment, cells were released into fresh normal media, and harvested at the indicated time points. Cells were then fixed, stained with α-BrdU antibody (y-axis) and 7-AAD (x-axis) and analyzed by flow cytometry. The BrdU-positive fractions containing G 1 -DNA content from total populations are circled (4, 6 and 8 h after HU removal). ( b – d ) Cells treated as in ( a ) were released into fresh media containing 1 μg/mL nocodazole for different hours. Cells were then fixed and stained with α-BrdU (BU1/75) (green) and α-Histone H3-pS10 (red) antibodies, and imaged using a fluorescence microscope. Representative images of cells 8 h after HU removal are shown in ( b ). Cells were counted using ImageJ, and the percentage of BrdU/H3-pS10 double positive ( c ) cells were quantified. Data are presented as Mean ± SD (n = 3) and analyzed by one-way ANOVA (**** P < 0.0001). ( d ) BrdU-negative/H3-pS10-positive cells were quantified. Data are presented as Mean ± SEM (n = 3) and analyzed by Student’s t-test; P < 0.01. ( e ) Total cell extracts from wild type and SMG7 −/− cells treated as in ( b – d ) were examined by western blot analysis using α-SMG7, α-CHK1-pS345, α-CHK1, α-RPA32-pS33, α-RPA32, α-RAD17 and α-RAD17-pS635 antibodies.

    Journal: Scientific Reports

    Article Title: Critical role of SMG7 in activation of the ATR-CHK1 axis in response to genotoxic stress

    doi: 10.1038/s41598-021-86957-x

    Figure Lengend Snippet: SMG7 maintains normal attenuation of the ATR-CHK1 axis during recovery from replication stress. ( a ) Wild type and SMG7 −/− HCT116 cells were pulsed with 25 μm BrdU followed by treatment with 5 mM HU for 6 h. After HU treatment, cells were released into fresh normal media, and harvested at the indicated time points. Cells were then fixed, stained with α-BrdU antibody (y-axis) and 7-AAD (x-axis) and analyzed by flow cytometry. The BrdU-positive fractions containing G 1 -DNA content from total populations are circled (4, 6 and 8 h after HU removal). ( b – d ) Cells treated as in ( a ) were released into fresh media containing 1 μg/mL nocodazole for different hours. Cells were then fixed and stained with α-BrdU (BU1/75) (green) and α-Histone H3-pS10 (red) antibodies, and imaged using a fluorescence microscope. Representative images of cells 8 h after HU removal are shown in ( b ). Cells were counted using ImageJ, and the percentage of BrdU/H3-pS10 double positive ( c ) cells were quantified. Data are presented as Mean ± SD (n = 3) and analyzed by one-way ANOVA (**** P < 0.0001). ( d ) BrdU-negative/H3-pS10-positive cells were quantified. Data are presented as Mean ± SEM (n = 3) and analyzed by Student’s t-test; P < 0.01. ( e ) Total cell extracts from wild type and SMG7 −/− cells treated as in ( b – d ) were examined by western blot analysis using α-SMG7, α-CHK1-pS345, α-CHK1, α-RPA32-pS33, α-RPA32, α-RAD17 and α-RAD17-pS635 antibodies.

    Article Snippet: The following antibodies were from Cell Signaling Technology: α-ATM-pS1981 (5883, 1:1000), α-ATM (2873, 1:1000), α-CHK1-pS345 (2348, 1:1000), α-CHK2-pT68 (2661, 1:1000), α-CHK2 (2662, 1:1000), α-RAD17-pS635 (13404S, 1:1000), α-RAD17 (8561, 1:1000), α-RPA32 (2208S, IF 1:1000), α-Histone H3 (3638, 1:2000), α-rabbit IgG-HRP (7074, 1:5000).

    Techniques: Staining, Flow Cytometry, Fluorescence, Microscopy, Western Blot

    SMG7 promotes chromatin recruitment of RAD9 upon DNA damage. ( a ) Cell extracts from DLD1 SMG7 −/− cells expressing FH-SMG7 and the α-Flag immunoprecipitates were examined by western blot analysis using α-SMG7, α-RAD17, α-ATR, α-TOPBP1, α-CHK1 and α-Tubulin antibodies. ( b , c ) Wild type and SMG7 −/− cells were treated with ionizing radiation (10 Gy, 1 h), pre-extracted, and immunostained in ( b ) with α-RPA32 (green) and α-γH2AX (red) antibodies and in ( c ) with α-RPA32 (green) and α-RAD9 (sc-74464, red). Nuclei were stained with DAPI. Representative images from immunofluorescence microscopy are shown. Wider fields of view at are shown in Fig. S4b-c. ( d ) Quantification of yH2AX-, yH2AX/RPA- and RPA/RAD9- foci-positive cells from experiments represented in ( b , c ). Data are presented as Mean ± SEM (n = 3 independent experiments containing pooled data) and were analyzed by one-way ANOVA with Tukey post-test. **** indicates P < 0.001. ( e ) Wild type and SMG7 −/− DLD1 cells were subjected to fractionation, and the total cells extracts, soluble nuclear and chromatin fractions were analyzed by western blot using α-SMG7 and α-RAD17 antibodies. α-alpha-Tubulin and α-Histone H3 antibodies were used as cytoplasmic and chromatin markers, respectively. Relative levels of chromatin-bound SMG7 and RAD17 are quantitated in Fig. S4d. ( f ) As in ( e ), the chromatin-bound fractions from the control and irradiated cells were isolated and examined by western blot analysis using α-SMG7, α-RAD17, α-RAD17-pS645, α-RAD9 (A300-890A) and α-H3 antibodies. Relative levels of chromatin-bound RAD9 are quantitated in Fig. S4f.

    Journal: Scientific Reports

    Article Title: Critical role of SMG7 in activation of the ATR-CHK1 axis in response to genotoxic stress

    doi: 10.1038/s41598-021-86957-x

    Figure Lengend Snippet: SMG7 promotes chromatin recruitment of RAD9 upon DNA damage. ( a ) Cell extracts from DLD1 SMG7 −/− cells expressing FH-SMG7 and the α-Flag immunoprecipitates were examined by western blot analysis using α-SMG7, α-RAD17, α-ATR, α-TOPBP1, α-CHK1 and α-Tubulin antibodies. ( b , c ) Wild type and SMG7 −/− cells were treated with ionizing radiation (10 Gy, 1 h), pre-extracted, and immunostained in ( b ) with α-RPA32 (green) and α-γH2AX (red) antibodies and in ( c ) with α-RPA32 (green) and α-RAD9 (sc-74464, red). Nuclei were stained with DAPI. Representative images from immunofluorescence microscopy are shown. Wider fields of view at are shown in Fig. S4b-c. ( d ) Quantification of yH2AX-, yH2AX/RPA- and RPA/RAD9- foci-positive cells from experiments represented in ( b , c ). Data are presented as Mean ± SEM (n = 3 independent experiments containing pooled data) and were analyzed by one-way ANOVA with Tukey post-test. **** indicates P < 0.001. ( e ) Wild type and SMG7 −/− DLD1 cells were subjected to fractionation, and the total cells extracts, soluble nuclear and chromatin fractions were analyzed by western blot using α-SMG7 and α-RAD17 antibodies. α-alpha-Tubulin and α-Histone H3 antibodies were used as cytoplasmic and chromatin markers, respectively. Relative levels of chromatin-bound SMG7 and RAD17 are quantitated in Fig. S4d. ( f ) As in ( e ), the chromatin-bound fractions from the control and irradiated cells were isolated and examined by western blot analysis using α-SMG7, α-RAD17, α-RAD17-pS645, α-RAD9 (A300-890A) and α-H3 antibodies. Relative levels of chromatin-bound RAD9 are quantitated in Fig. S4f.

    Article Snippet: The following antibodies were from Cell Signaling Technology: α-ATM-pS1981 (5883, 1:1000), α-ATM (2873, 1:1000), α-CHK1-pS345 (2348, 1:1000), α-CHK2-pT68 (2661, 1:1000), α-CHK2 (2662, 1:1000), α-RAD17-pS635 (13404S, 1:1000), α-RAD17 (8561, 1:1000), α-RPA32 (2208S, IF 1:1000), α-Histone H3 (3638, 1:2000), α-rabbit IgG-HRP (7074, 1:5000).

    Techniques: Expressing, Western Blot, Staining, Immunofluorescence, Microscopy, Fractionation, Irradiation, Isolation

    ATR-dependent RAD17 phosphorylation at S635 enhances SMG7 interaction. ( a ) The FH-SMG7-H1299 cells were treated for 4 h with 10 µM ATM (KU-55933) or ATR (VE-822) inhibitor. The total cell lysates and α-Flag immunoprecipitates were analyzed by western blot using α-SMG7, α-RAD17 and α-RAD17-pS635 antibodies. Relative levels of immunoprecipitated RAD17 are quantitated in Fig. S3a. ( b ) Cells treated with or without ATR inhibitor (VE-822, 10 µM for 4 h) were exposed to 10 Gy IR and harvested 1 h later. The total cell lysates and α-Flag immunoprecipitates were analyzed by western blot using α-SMG7, α-RAD17 and α-RAD17-pS635 antibodies as in ( a ). Relative levels of immunoprecipitated RAD17 and RAD17-pS635 are quantitated in Fig. S3b. ( c ) GST and GST-SMG7 fragment fusion proteins were incubated with lysates from 293FT cells transiently expressing HA-RAD17, and RAD17 pulled down by the GST proteins was analyzed by western blot with α-RAD17 antibody. ( d ) Alignment of the amino acid sequences adjacent to the serine residues within the SQ motif of RAD17, UPF1 and p53 (top). The FH-RAD17 and FH-RAD17-S635A proteins purified from transfected 293FT cells were analyzed by western blot using α-RAD17-pS635 and α-RAD17 antibodies (bottom). ( e ) GST or GST-SMG7 fragments were incubated with purified FH-RAD17 or FH-RAD17-S635A protein from ( d ) in GST pull-down assays. RAD17 and RAD17-pS635 were detected by western blotting with the antibodies indicated. Relative levels of RAD17 binding and RAD17-pS635 binding are quantitated in Fig. S3f. ( f ) H1299 cells were co-transfected with plasmids expressing FH-SMG7 and HA-RAD17 WT, S635A, S645A or S635/645A, and the total cell extracts and α-Flag immunoprecipitated materials were examined by western blot analysis using α-SMG7, α-RAD17 and α-RAD17-pS635 antibodies. Relative levels of RAD17 and RAD17-pS635 binding to FH-SMG7 are quantitated in Fig. S3g.

    Journal: Scientific Reports

    Article Title: Critical role of SMG7 in activation of the ATR-CHK1 axis in response to genotoxic stress

    doi: 10.1038/s41598-021-86957-x

    Figure Lengend Snippet: ATR-dependent RAD17 phosphorylation at S635 enhances SMG7 interaction. ( a ) The FH-SMG7-H1299 cells were treated for 4 h with 10 µM ATM (KU-55933) or ATR (VE-822) inhibitor. The total cell lysates and α-Flag immunoprecipitates were analyzed by western blot using α-SMG7, α-RAD17 and α-RAD17-pS635 antibodies. Relative levels of immunoprecipitated RAD17 are quantitated in Fig. S3a. ( b ) Cells treated with or without ATR inhibitor (VE-822, 10 µM for 4 h) were exposed to 10 Gy IR and harvested 1 h later. The total cell lysates and α-Flag immunoprecipitates were analyzed by western blot using α-SMG7, α-RAD17 and α-RAD17-pS635 antibodies as in ( a ). Relative levels of immunoprecipitated RAD17 and RAD17-pS635 are quantitated in Fig. S3b. ( c ) GST and GST-SMG7 fragment fusion proteins were incubated with lysates from 293FT cells transiently expressing HA-RAD17, and RAD17 pulled down by the GST proteins was analyzed by western blot with α-RAD17 antibody. ( d ) Alignment of the amino acid sequences adjacent to the serine residues within the SQ motif of RAD17, UPF1 and p53 (top). The FH-RAD17 and FH-RAD17-S635A proteins purified from transfected 293FT cells were analyzed by western blot using α-RAD17-pS635 and α-RAD17 antibodies (bottom). ( e ) GST or GST-SMG7 fragments were incubated with purified FH-RAD17 or FH-RAD17-S635A protein from ( d ) in GST pull-down assays. RAD17 and RAD17-pS635 were detected by western blotting with the antibodies indicated. Relative levels of RAD17 binding and RAD17-pS635 binding are quantitated in Fig. S3f. ( f ) H1299 cells were co-transfected with plasmids expressing FH-SMG7 and HA-RAD17 WT, S635A, S645A or S635/645A, and the total cell extracts and α-Flag immunoprecipitated materials were examined by western blot analysis using α-SMG7, α-RAD17 and α-RAD17-pS635 antibodies. Relative levels of RAD17 and RAD17-pS635 binding to FH-SMG7 are quantitated in Fig. S3g.

    Article Snippet: The following antibodies were from Cell Signaling Technology: α-ATM-pS1981 (5883, 1:1000), α-ATM (2873, 1:1000), α-CHK1-pS345 (2348, 1:1000), α-CHK2-pT68 (2661, 1:1000), α-CHK2 (2662, 1:1000), α-RAD17-pS635 (13404S, 1:1000), α-RAD17 (8561, 1:1000), α-RPA32 (2208S, IF 1:1000), α-Histone H3 (3638, 1:2000), α-rabbit IgG-HRP (7074, 1:5000).

    Techniques: Western Blot, Immunoprecipitation, Incubation, Expressing, Purification, Transfection, Binding Assay

    (A) GST pull-down demonstrating that purified GST-Rheb binds endogenous PDP1 in the brain (A, top panel) and PDP2 in the liver (A, middle panel).

    Journal: Developmental cell

    Article Title: Rheb mediates neuronal-activity-induced mitochondrial energetics through mTORC1-independent PDH activation

    doi: 10.1016/j.devcel.2021.02.022

    Figure Lengend Snippet: (A) GST pull-down demonstrating that purified GST-Rheb binds endogenous PDP1 in the brain (A, top panel) and PDP2 in the liver (A, middle panel).

    Article Snippet: Rabbit polyclonal PDP2 antibody , Proteintech , Cat#13404–1-AP.

    Techniques: Purification

    (A and B) GST pull-down (A) and quantification (B) comparing GST-Rheb pull-down of PDP2 and PDH-E1α from liver of Rheb KO versus mTor KO mice. Despite equivalent amounts of PDP2, less PDH-E1α is pulled down from Rheb KO. N = 3 independent experiments, PDP2, p = 0.8183; PDH-E1α, p = 0.0034.

    Journal: Developmental cell

    Article Title: Rheb mediates neuronal-activity-induced mitochondrial energetics through mTORC1-independent PDH activation

    doi: 10.1016/j.devcel.2021.02.022

    Figure Lengend Snippet: (A and B) GST pull-down (A) and quantification (B) comparing GST-Rheb pull-down of PDP2 and PDH-E1α from liver of Rheb KO versus mTor KO mice. Despite equivalent amounts of PDP2, less PDH-E1α is pulled down from Rheb KO. N = 3 independent experiments, PDP2, p = 0.8183; PDH-E1α, p = 0.0034.

    Article Snippet: Rabbit polyclonal PDP2 antibody , Proteintech , Cat#13404–1-AP.

    Techniques:

    KEY RESOURCES TABLE

    Journal: Developmental cell

    Article Title: Rheb mediates neuronal-activity-induced mitochondrial energetics through mTORC1-independent PDH activation

    doi: 10.1016/j.devcel.2021.02.022

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: Rabbit polyclonal PDP2 antibody , Proteintech , Cat#13404–1-AP.

    Techniques: Recombinant, ATP Assay, Isolation, Activity Assay, Phosphatase Assay, In Situ, Pyruvate Assay, Lactate Assay, Enzyme-linked Immunosorbent Assay, Real-time Polymerase Chain Reaction, Sequencing, Software