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rabbit polyclonal anti rictor antibody  (Bethyl)


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    Bethyl rabbit polyclonal anti rictor antibody
    Rabbit Polyclonal Anti Rictor Antibody, supplied by Bethyl, used in various techniques. Bioz Stars score: 93/100, based on 189 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 189 article reviews
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    (A) Comparison of C6nc/C6 ratios for the two SILAC replicates. Depleted proteins that met a 2-fold cutoff in both replicates are highlighted in blue. (B) As in (A) except for enriched proteins (red). (C) Extracts from HEK293 cells were subject to IP with a <t>polyclonal</t> antibody against WDR5 or an immunoglobulin G (IgG) control. IP samples were probed with antibodies against the indicated endogenous proteins. Inputs are 2% for WDR5 and RBBP5 and 0.3% for others. n = 3 biological replicates. (D) As in (C) but for different candidate proteins. Inputs are 5% for WDR5, RBBP5, and UBR5 and 0.3% for others. n = 3 biological replicates. (E) HEK293 cells stably expressing FLAG-tagged WDR5 were treated for 4 h with 30 μM C6 or C6nc prior to lysis and subsequent FLAG IP. For ethidium bromide (EtBr) treatment, 200 μg/mL EtBr was added to the lysate for the duration of the experiment. Candidate WDR5 interaction partners were probed by IB. Inputs are 5% for WDR5 and RBBP5, 0.1% for SYRC and SYIC, and 1% for all others; n = 3 biological replicates. (F) HEK293 cells stably expressing FLAG-tagged WDR5 were treated for 4 h with 30 mM C6 or C6nc prior to lysis and subsequent FLAG IP in buffer using CHAPS detergent. IP samples were probed with antibodies against the indicated proteins. Inputs are 10% for WDR5 and RBBP5 and 1% for others; n = 3 biological replicates. (G) HEK293 cells stably expressing FLAG-tagged WDR5 proteins were treated for 4 h with 30 μM C6 (where indicated) prior to lysis and FLAG IP. IP samples were probed with antibodies against the indicated proteins. Inputs are 10% for WDR5 and 1% for others; n = 3 biological replicates. See also .
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    (A) Comparison of C6nc/C6 ratios for the two SILAC replicates. Depleted proteins that met a 2-fold cutoff in both replicates are highlighted in blue. (B) As in (A) except for enriched proteins (red). (C) Extracts from HEK293 cells were subject to IP with a <t>polyclonal</t> antibody against WDR5 or an immunoglobulin G (IgG) control. IP samples were probed with antibodies against the indicated endogenous proteins. Inputs are 2% for WDR5 and RBBP5 and 0.3% for others. n = 3 biological replicates. (D) As in (C) but for different candidate proteins. Inputs are 5% for WDR5, RBBP5, and UBR5 and 0.3% for others. n = 3 biological replicates. (E) HEK293 cells stably expressing FLAG-tagged WDR5 were treated for 4 h with 30 μM C6 or C6nc prior to lysis and subsequent FLAG IP. For ethidium bromide (EtBr) treatment, 200 μg/mL EtBr was added to the lysate for the duration of the experiment. Candidate WDR5 interaction partners were probed by IB. Inputs are 5% for WDR5 and RBBP5, 0.1% for SYRC and SYIC, and 1% for all others; n = 3 biological replicates. (F) HEK293 cells stably expressing FLAG-tagged WDR5 were treated for 4 h with 30 mM C6 or C6nc prior to lysis and subsequent FLAG IP in buffer using CHAPS detergent. IP samples were probed with antibodies against the indicated proteins. Inputs are 10% for WDR5 and RBBP5 and 1% for others; n = 3 biological replicates. (G) HEK293 cells stably expressing FLAG-tagged WDR5 proteins were treated for 4 h with 30 μM C6 (where indicated) prior to lysis and FLAG IP. IP samples were probed with antibodies against the indicated proteins. Inputs are 10% for WDR5 and 1% for others; n = 3 biological replicates. See also .
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    (A) Comparison of C6nc/C6 ratios for the two SILAC replicates. Depleted proteins that met a 2-fold cutoff in both replicates are highlighted in blue. (B) As in (A) except for enriched proteins (red). (C) Extracts from HEK293 cells were subject to IP with a <t>polyclonal</t> antibody against WDR5 or an immunoglobulin G (IgG) control. IP samples were probed with antibodies against the indicated endogenous proteins. Inputs are 2% for WDR5 and RBBP5 and 0.3% for others. n = 3 biological replicates. (D) As in (C) but for different candidate proteins. Inputs are 5% for WDR5, RBBP5, and UBR5 and 0.3% for others. n = 3 biological replicates. (E) HEK293 cells stably expressing FLAG-tagged WDR5 were treated for 4 h with 30 μM C6 or C6nc prior to lysis and subsequent FLAG IP. For ethidium bromide (EtBr) treatment, 200 μg/mL EtBr was added to the lysate for the duration of the experiment. Candidate WDR5 interaction partners were probed by IB. Inputs are 5% for WDR5 and RBBP5, 0.1% for SYRC and SYIC, and 1% for all others; n = 3 biological replicates. (F) HEK293 cells stably expressing FLAG-tagged WDR5 were treated for 4 h with 30 mM C6 or C6nc prior to lysis and subsequent FLAG IP in buffer using CHAPS detergent. IP samples were probed with antibodies against the indicated proteins. Inputs are 10% for WDR5 and RBBP5 and 1% for others; n = 3 biological replicates. (G) HEK293 cells stably expressing FLAG-tagged WDR5 proteins were treated for 4 h with 30 μM C6 (where indicated) prior to lysis and FLAG IP. IP samples were probed with antibodies against the indicated proteins. Inputs are 10% for WDR5 and 1% for others; n = 3 biological replicates. See also .
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    Cell Signaling Technology Inc rictor rabbit polyclonal
    Striatal homogenates (H) and synaptosomes (S) of WT and R6/1 injected with AAV-shCtr ( n = 6 WT and n = 6 R6/1) or AAV-shRTP801 ( n = 6 WT and n = 7 R6/1) were subjected to WB. Membranes were probed against a P-mTOR (Ser2448), b P-S6 (Ser235/236), c P-Akt (Ser273), d <t>Rictor,</t> and e PHLPP1. Total mTOR, S6, Akt, and actin were used as loading controls. Graphs show the densitometric quantification. Values are shown as a mean ± SEM. Homogenates and synaptosomes data were analyzed with two-way ANOVA followed by Bonferroni’s multiple comparisons test for post hoc analyses (* P < 0.05, ** P < 0.01, ** P < 0.010 vs. WT AAV-shCtr; $ P < 0.05 vs. WT AAV-shRTP801; # P < 0.05, ## P < 0.01 vs. R6/1 AAV-shCtr).
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    Image Search Results


    key resources table

    Journal: Cell reports

    Article Title: Non-cell-autonomous regulation of mTORC2 by Hedgehog signaling maintains lipid homeostasis

    doi: 10.1016/j.celrep.2024.115191

    Figure Lengend Snippet: key resources table

    Article Snippet: Rabbit polyclonal anti-Rictor , Cell Signaling Technology , Cat# 2140; RRID:AB_2179961.

    Techniques: Virus, Recombinant, SYBR Green Assay, Transfection, DC Protein Assay, Mutagenesis, CRISPR, Plasmid Preparation, Software

    (A) Comparison of C6nc/C6 ratios for the two SILAC replicates. Depleted proteins that met a 2-fold cutoff in both replicates are highlighted in blue. (B) As in (A) except for enriched proteins (red). (C) Extracts from HEK293 cells were subject to IP with a polyclonal antibody against WDR5 or an immunoglobulin G (IgG) control. IP samples were probed with antibodies against the indicated endogenous proteins. Inputs are 2% for WDR5 and RBBP5 and 0.3% for others. n = 3 biological replicates. (D) As in (C) but for different candidate proteins. Inputs are 5% for WDR5, RBBP5, and UBR5 and 0.3% for others. n = 3 biological replicates. (E) HEK293 cells stably expressing FLAG-tagged WDR5 were treated for 4 h with 30 μM C6 or C6nc prior to lysis and subsequent FLAG IP. For ethidium bromide (EtBr) treatment, 200 μg/mL EtBr was added to the lysate for the duration of the experiment. Candidate WDR5 interaction partners were probed by IB. Inputs are 5% for WDR5 and RBBP5, 0.1% for SYRC and SYIC, and 1% for all others; n = 3 biological replicates. (F) HEK293 cells stably expressing FLAG-tagged WDR5 were treated for 4 h with 30 mM C6 or C6nc prior to lysis and subsequent FLAG IP in buffer using CHAPS detergent. IP samples were probed with antibodies against the indicated proteins. Inputs are 10% for WDR5 and RBBP5 and 1% for others; n = 3 biological replicates. (G) HEK293 cells stably expressing FLAG-tagged WDR5 proteins were treated for 4 h with 30 μM C6 (where indicated) prior to lysis and FLAG IP. IP samples were probed with antibodies against the indicated proteins. Inputs are 10% for WDR5 and 1% for others; n = 3 biological replicates. See also .

    Journal: Cell reports

    Article Title: Impact of WIN site inhibitor on the WDR5 interactome

    doi: 10.1016/j.celrep.2020.108636

    Figure Lengend Snippet: (A) Comparison of C6nc/C6 ratios for the two SILAC replicates. Depleted proteins that met a 2-fold cutoff in both replicates are highlighted in blue. (B) As in (A) except for enriched proteins (red). (C) Extracts from HEK293 cells were subject to IP with a polyclonal antibody against WDR5 or an immunoglobulin G (IgG) control. IP samples were probed with antibodies against the indicated endogenous proteins. Inputs are 2% for WDR5 and RBBP5 and 0.3% for others. n = 3 biological replicates. (D) As in (C) but for different candidate proteins. Inputs are 5% for WDR5, RBBP5, and UBR5 and 0.3% for others. n = 3 biological replicates. (E) HEK293 cells stably expressing FLAG-tagged WDR5 were treated for 4 h with 30 μM C6 or C6nc prior to lysis and subsequent FLAG IP. For ethidium bromide (EtBr) treatment, 200 μg/mL EtBr was added to the lysate for the duration of the experiment. Candidate WDR5 interaction partners were probed by IB. Inputs are 5% for WDR5 and RBBP5, 0.1% for SYRC and SYIC, and 1% for all others; n = 3 biological replicates. (F) HEK293 cells stably expressing FLAG-tagged WDR5 were treated for 4 h with 30 mM C6 or C6nc prior to lysis and subsequent FLAG IP in buffer using CHAPS detergent. IP samples were probed with antibodies against the indicated proteins. Inputs are 10% for WDR5 and RBBP5 and 1% for others; n = 3 biological replicates. (G) HEK293 cells stably expressing FLAG-tagged WDR5 proteins were treated for 4 h with 30 μM C6 (where indicated) prior to lysis and FLAG IP. IP samples were probed with antibodies against the indicated proteins. Inputs are 10% for WDR5 and 1% for others; n = 3 biological replicates. See also .

    Article Snippet: Rabbit polyclonal anti-Rictor Antibody (anti-RICTR) , Bethyl Laboratories , Cat# A300–459A RRID:AB_2179967.

    Techniques: Comparison, Multiplex sample analysis, Control, Stable Transfection, Expressing, Lysis

    KEY RESOURCES TABLE

    Journal: Cell reports

    Article Title: Impact of WIN site inhibitor on the WDR5 interactome

    doi: 10.1016/j.celrep.2020.108636

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: Rabbit polyclonal anti-Rictor Antibody (anti-RICTR) , Bethyl Laboratories , Cat# A300–459A RRID:AB_2179967.

    Techniques: Western Blot, Virus, Recombinant, Protease Inhibitor, Multiplex sample analysis, Staining, Cloning, Expressing, Transfection, Mass Spectrometry, Plasmid Preparation, Mutagenesis, CRISPR, Amplification, Modification, Software, Hybridization, Membrane

    Striatal homogenates (H) and synaptosomes (S) of WT and R6/1 injected with AAV-shCtr ( n = 6 WT and n = 6 R6/1) or AAV-shRTP801 ( n = 6 WT and n = 7 R6/1) were subjected to WB. Membranes were probed against a P-mTOR (Ser2448), b P-S6 (Ser235/236), c P-Akt (Ser273), d Rictor, and e PHLPP1. Total mTOR, S6, Akt, and actin were used as loading controls. Graphs show the densitometric quantification. Values are shown as a mean ± SEM. Homogenates and synaptosomes data were analyzed with two-way ANOVA followed by Bonferroni’s multiple comparisons test for post hoc analyses (* P < 0.05, ** P < 0.01, ** P < 0.010 vs. WT AAV-shCtr; $ P < 0.05 vs. WT AAV-shRTP801; # P < 0.05, ## P < 0.01 vs. R6/1 AAV-shCtr).

    Journal: Cell Death & Disease

    Article Title: Synaptic RTP801 contributes to motor-learning dysfunction in Huntington’s disease

    doi: 10.1038/s41419-020-02775-5

    Figure Lengend Snippet: Striatal homogenates (H) and synaptosomes (S) of WT and R6/1 injected with AAV-shCtr ( n = 6 WT and n = 6 R6/1) or AAV-shRTP801 ( n = 6 WT and n = 7 R6/1) were subjected to WB. Membranes were probed against a P-mTOR (Ser2448), b P-S6 (Ser235/236), c P-Akt (Ser273), d Rictor, and e PHLPP1. Total mTOR, S6, Akt, and actin were used as loading controls. Graphs show the densitometric quantification. Values are shown as a mean ± SEM. Homogenates and synaptosomes data were analyzed with two-way ANOVA followed by Bonferroni’s multiple comparisons test for post hoc analyses (* P < 0.05, ** P < 0.01, ** P < 0.010 vs. WT AAV-shCtr; $ P < 0.05 vs. WT AAV-shRTP801; # P < 0.05, ## P < 0.01 vs. R6/1 AAV-shCtr).

    Article Snippet: The following primary antibodies were used: Akt rabbit polyclonal (1:1000, Cell Signaling, #4691), Akt-phospho-Ser473 rabbit polyclonal (1:1000, Cell Signaling, #4060), GFP rabbit polyclonal (1:1000, Santa Cruz Biotechnology, #sc-8334), GluA1 rabbit polyclonal (1:1000, Merck Millipore, #ABN241), mTOR rabbit polyclonal (1:1000, Cell Signaling, #2971), mTOR-phospho Ser2448 (1:1000, Cell Signaling, #2972), anti-NR1 mouse monoclonal (1:1000, Chemicon, #MAB363), p75 NTR rabbit polyclonal (1:1000, Promega, #G323A), PHLPP1 rabbit polyclonal (1:500, Cayman Chemical, #10007191), PSD-95 mouse monoclonal (1:1000, Thermo Fisher Scientific, #MA1-045), Rictor rabbit polyclonal (1:1000, Cell Signaling, #2140), RTP801 (1:500, Proteintech Group Inc., #10638-1-AP), RPS6 mouse monoclonal (1:500, Cell Signaling, #2317), RPS6-phospho-Ser235/236 rabbit polyclonal (1:1000, Cell Signaling, #4858), SV2A mouse monoclonal (1:1000, Santa Cruz Biotechnology, #sc-376234) and TrkB mouse monoclonal (1:1000, BD Biosciences, #610102).

    Techniques: Injection

    In comparison to WT mice, R6/1 mice display increased RTP801 at the striatal synapse along with increased Rictor and P-Akt (Ser473) and motor-learning deficits. RTP801 silencing preserves corticostriatal motor-learning function by decreasing the levels of Rictor and P-Akt Ser473 and enhancing postsynaptic signaling by increasing GluA1 and TrkB receptors.

    Journal: Cell Death & Disease

    Article Title: Synaptic RTP801 contributes to motor-learning dysfunction in Huntington’s disease

    doi: 10.1038/s41419-020-02775-5

    Figure Lengend Snippet: In comparison to WT mice, R6/1 mice display increased RTP801 at the striatal synapse along with increased Rictor and P-Akt (Ser473) and motor-learning deficits. RTP801 silencing preserves corticostriatal motor-learning function by decreasing the levels of Rictor and P-Akt Ser473 and enhancing postsynaptic signaling by increasing GluA1 and TrkB receptors.

    Article Snippet: The following primary antibodies were used: Akt rabbit polyclonal (1:1000, Cell Signaling, #4691), Akt-phospho-Ser473 rabbit polyclonal (1:1000, Cell Signaling, #4060), GFP rabbit polyclonal (1:1000, Santa Cruz Biotechnology, #sc-8334), GluA1 rabbit polyclonal (1:1000, Merck Millipore, #ABN241), mTOR rabbit polyclonal (1:1000, Cell Signaling, #2971), mTOR-phospho Ser2448 (1:1000, Cell Signaling, #2972), anti-NR1 mouse monoclonal (1:1000, Chemicon, #MAB363), p75 NTR rabbit polyclonal (1:1000, Promega, #G323A), PHLPP1 rabbit polyclonal (1:500, Cayman Chemical, #10007191), PSD-95 mouse monoclonal (1:1000, Thermo Fisher Scientific, #MA1-045), Rictor rabbit polyclonal (1:1000, Cell Signaling, #2140), RTP801 (1:500, Proteintech Group Inc., #10638-1-AP), RPS6 mouse monoclonal (1:500, Cell Signaling, #2317), RPS6-phospho-Ser235/236 rabbit polyclonal (1:1000, Cell Signaling, #4858), SV2A mouse monoclonal (1:1000, Santa Cruz Biotechnology, #sc-376234) and TrkB mouse monoclonal (1:1000, BD Biosciences, #610102).

    Techniques: Comparison