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monoclonal anti eif4e antibody  (R&D Systems)


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    R&D Systems monoclonal anti eif4e antibody
    Fig. 4 | Compound 4 inhibits <t>eIF4G:eIF4E</t> binding and cap-dependent transla- tion in cell lysate assays. a Lysates from SW620 cells were incubated with 1–100 µM compound 4 or 5 or positive control peptide (RIIY) for 30 min. Endo- genous eIF4E was immunoprecipitated and immunoblotted for eIF4G, 4E-BP1 and eIF4E. Quantitation of 4E-BP1 (b) or eIF4G (c) with endogenous eIF4E in SW620 and HeLa cell lysates, determined by the electro-chemiluminescent binding assay fol- lowing incubation for 30 min with DMSO vehicle (Cont), 100 µM compound 4 or 100 µM RIIY peptide. Complexes were immobilised by an eIF4E antibody and captured eIF4E, eIF4G and 4E-BP1 detected by their respective secondary anti- bodies. Values represent ratios of 4E-BP1:eIF4E or eIF4G:eIF4E electro- chemiluminescence relative to DMSO control (n = 2 biological replicates). d Electro-chemiluminescent assay for binding of eIF4G or 4E-BP1 with eIF4E in SW620 (n = 2 biological replicates), or (e) in HeLa lysates (n = 3 biological replicates, mean ± SD) following incubation for 30 min with compound 4 or 5. Results are expressed as luminescence signals relative to DMSO control. f Quantification of eIF4E:eIF4G interaction in H1299 cells by electro-chemiluminescent assay. Cell lysates treated with RIIY 4E-BP1 derived peptide or RIIG negative control peptide at 0.1–100 µM for 30 min (n = 2 biological replicates). g Quantification of the endo- genous eIF4E:eIF4G interaction in H1299 cell lysates at 0.1–100 µM (for 6 h) of compound 4 or 5, as measured by electro-chemiluminescent assay (mean ± SD from n = 3 biological replicates). h HeLa cell lysates for in vitro translation were incubated for 30 min with 1, 10, 100 µM of compound 4 or 5. Results are expressed as firefly or renilla luminescence signal normalized to DMSO control and expressed as % (mean ± SD from n = 3 biological replicates). Significance was determined using two-sided unpaired t-test comparing compound 4 to compound 5 at each concentration. Statistically significant p-values (p < 0.05) are shown on the plot and source data is located in the Source Data file.
    Monoclonal Anti Eif4e Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/monoclonal+anti+eif4e+antibody/Human%2FMouse%2FRat+eIF4E+Antibody/pm40016190-349-0-3
    Average 94 stars, based on 11 article reviews
    monoclonal anti eif4e antibody - by Bioz Stars, 2026-09
    94/100 stars

    Images

    1) Product Images from "Integrating fragment-based screening with targeted protein degradation and genetic rescue to explore eIF4E function."

    Article Title: Integrating fragment-based screening with targeted protein degradation and genetic rescue to explore eIF4E function.

    Journal: Nature communications

    doi: 10.1038/s41467-024-54356-1

    Fig. 4 | Compound 4 inhibits eIF4G:eIF4E binding and cap-dependent transla- tion in cell lysate assays. a Lysates from SW620 cells were incubated with 1–100 µM compound 4 or 5 or positive control peptide (RIIY) for 30 min. Endo- genous eIF4E was immunoprecipitated and immunoblotted for eIF4G, 4E-BP1 and eIF4E. Quantitation of 4E-BP1 (b) or eIF4G (c) with endogenous eIF4E in SW620 and HeLa cell lysates, determined by the electro-chemiluminescent binding assay fol- lowing incubation for 30 min with DMSO vehicle (Cont), 100 µM compound 4 or 100 µM RIIY peptide. Complexes were immobilised by an eIF4E antibody and captured eIF4E, eIF4G and 4E-BP1 detected by their respective secondary anti- bodies. Values represent ratios of 4E-BP1:eIF4E or eIF4G:eIF4E electro- chemiluminescence relative to DMSO control (n = 2 biological replicates). d Electro-chemiluminescent assay for binding of eIF4G or 4E-BP1 with eIF4E in SW620 (n = 2 biological replicates), or (e) in HeLa lysates (n = 3 biological replicates, mean ± SD) following incubation for 30 min with compound 4 or 5. Results are expressed as luminescence signals relative to DMSO control. f Quantification of eIF4E:eIF4G interaction in H1299 cells by electro-chemiluminescent assay. Cell lysates treated with RIIY 4E-BP1 derived peptide or RIIG negative control peptide at 0.1–100 µM for 30 min (n = 2 biological replicates). g Quantification of the endo- genous eIF4E:eIF4G interaction in H1299 cell lysates at 0.1–100 µM (for 6 h) of compound 4 or 5, as measured by electro-chemiluminescent assay (mean ± SD from n = 3 biological replicates). h HeLa cell lysates for in vitro translation were incubated for 30 min with 1, 10, 100 µM of compound 4 or 5. Results are expressed as firefly or renilla luminescence signal normalized to DMSO control and expressed as % (mean ± SD from n = 3 biological replicates). Significance was determined using two-sided unpaired t-test comparing compound 4 to compound 5 at each concentration. Statistically significant p-values (p < 0.05) are shown on the plot and source data is located in the Source Data file.
    Figure Legend Snippet: Fig. 4 | Compound 4 inhibits eIF4G:eIF4E binding and cap-dependent transla- tion in cell lysate assays. a Lysates from SW620 cells were incubated with 1–100 µM compound 4 or 5 or positive control peptide (RIIY) for 30 min. Endo- genous eIF4E was immunoprecipitated and immunoblotted for eIF4G, 4E-BP1 and eIF4E. Quantitation of 4E-BP1 (b) or eIF4G (c) with endogenous eIF4E in SW620 and HeLa cell lysates, determined by the electro-chemiluminescent binding assay fol- lowing incubation for 30 min with DMSO vehicle (Cont), 100 µM compound 4 or 100 µM RIIY peptide. Complexes were immobilised by an eIF4E antibody and captured eIF4E, eIF4G and 4E-BP1 detected by their respective secondary anti- bodies. Values represent ratios of 4E-BP1:eIF4E or eIF4G:eIF4E electro- chemiluminescence relative to DMSO control (n = 2 biological replicates). d Electro-chemiluminescent assay for binding of eIF4G or 4E-BP1 with eIF4E in SW620 (n = 2 biological replicates), or (e) in HeLa lysates (n = 3 biological replicates, mean ± SD) following incubation for 30 min with compound 4 or 5. Results are expressed as luminescence signals relative to DMSO control. f Quantification of eIF4E:eIF4G interaction in H1299 cells by electro-chemiluminescent assay. Cell lysates treated with RIIY 4E-BP1 derived peptide or RIIG negative control peptide at 0.1–100 µM for 30 min (n = 2 biological replicates). g Quantification of the endo- genous eIF4E:eIF4G interaction in H1299 cell lysates at 0.1–100 µM (for 6 h) of compound 4 or 5, as measured by electro-chemiluminescent assay (mean ± SD from n = 3 biological replicates). h HeLa cell lysates for in vitro translation were incubated for 30 min with 1, 10, 100 µM of compound 4 or 5. Results are expressed as firefly or renilla luminescence signal normalized to DMSO control and expressed as % (mean ± SD from n = 3 biological replicates). Significance was determined using two-sided unpaired t-test comparing compound 4 to compound 5 at each concentration. Statistically significant p-values (p < 0.05) are shown on the plot and source data is located in the Source Data file.

    Techniques Used: Binding Assay, Incubation, Positive Control, Immunoprecipitation, Quantitation Assay, Control, Derivative Assay, Negative Control, In Vitro, Concentration Assay

    Related Articles

    Magnetic Beads:

    Article Title: Integrating fragment-based screening with targeted protein degradation and genetic rescue to explore eIF4E function
    Article Snippet: .. Monoclonal anti-eIF4E antibody (R&D Systems, Cat# MAB3228, RRID:AB_2097694) was biotinylated using the Lightning-Link kit (R&D Systems Inc. Cat# 371-0010) according to the manufacturer instructions and 20 μg used to coat 1 ml streptavidin magnetic beads (Pierce Cat# 88817) for 1 hr at room temperature (RT) with rotatory shaking. ..



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    A. Western blot of total cell lysates from MM6 cells grown in suspension demonstrated knockdown of Ezrin (siEZR) or eIF4E (siEIF4E) compared to RNAi to luciferase (siLUC) used as a negative control. b-Actin is provided as a loading control. Other proteins of the Ezrin-CD44-HA axis are also shown. Quantification for these is shown in with 3-6 biological replicates for each protein. B. Adhesion and invasion capacity of MM6 cells onto/through HS-5 bone marrow stroma. Fold change relative to siLUC is shown. Each symbol represents a biological replicate performed independently with replicates. Bars represent the mean, shown with standard deviations and p-values (one-way ANOVA). C. Western blot of eIF4E and Ezrin immunoprecipitations (IPs) using total cell lysates from MM6 cells in suspension. SN, supernatant after immunoprecipitation, IgG, negative control. Representative of three biological replicates. IPs of total cell lysates from THP-1 cells in suspension are provided in . D. IPs from MM6 cells in suspension using the rRNA antibody Y10b. LC indicates antibody light chain. Representative of three biological replicates. E. RNA immunoprecipitations (RIPs) from MM6 total cell lysates grown in suspension using anti-Ezrin (Ezrin RIP) or anti-eIF4E (eIF4E RIP) antibodies. Data are from RT-qPCR and represented relative to input. Each symbol represents a biological replicate performed independently with triplicates. Bars represent the mean, shown with standard deviations and p-values (two tailed Welch’s t test). F. Western blots of eIF4E and Ezrin IPs from the cytoplasmic fractions of MM6 cells in suspension or G . After invasion through HS-5 bone marrow stroma (invaded). Fractionation controls are provided in . H. RIPs from MM6 cytoplasmic fraction from invaded cells using anti-eIF4E (eIF4E RIP) or anti-Ezrin (Ezrin RIP) antibodies. Data are from RT-qPCR represented relative to input. Each symbol represents a biological replicate performed independently with triplicates. Bars represent the mean, shown with standard deviations and p-values (two tailed Welch’s t test). I. Count of the number of pseudopods observed in suspension and invaded MM6 cells represented as a fraction relative to the total cells counted. Each symbol represents a biological replicate. Bars represent the mean, shown with standard deviations and p-values (two-way ANOVA). J . Immunofluorescence and confocal microscopy demonstrating eIF4E, Ezrin, CD44 and rRNA are localized to the same pseudopods (white arrows). All confocal micrographs represent a single section through the plane of the cell. Scale bar = 10 µm

    Journal: bioRxiv

    Article Title: eIF4E and Ezrin cooperate in pseudopods to drive a localized migratory translation program in acute myeloid leukemia

    doi: 10.64898/2026.02.21.707190

    Figure Lengend Snippet: A. Western blot of total cell lysates from MM6 cells grown in suspension demonstrated knockdown of Ezrin (siEZR) or eIF4E (siEIF4E) compared to RNAi to luciferase (siLUC) used as a negative control. b-Actin is provided as a loading control. Other proteins of the Ezrin-CD44-HA axis are also shown. Quantification for these is shown in with 3-6 biological replicates for each protein. B. Adhesion and invasion capacity of MM6 cells onto/through HS-5 bone marrow stroma. Fold change relative to siLUC is shown. Each symbol represents a biological replicate performed independently with replicates. Bars represent the mean, shown with standard deviations and p-values (one-way ANOVA). C. Western blot of eIF4E and Ezrin immunoprecipitations (IPs) using total cell lysates from MM6 cells in suspension. SN, supernatant after immunoprecipitation, IgG, negative control. Representative of three biological replicates. IPs of total cell lysates from THP-1 cells in suspension are provided in . D. IPs from MM6 cells in suspension using the rRNA antibody Y10b. LC indicates antibody light chain. Representative of three biological replicates. E. RNA immunoprecipitations (RIPs) from MM6 total cell lysates grown in suspension using anti-Ezrin (Ezrin RIP) or anti-eIF4E (eIF4E RIP) antibodies. Data are from RT-qPCR and represented relative to input. Each symbol represents a biological replicate performed independently with triplicates. Bars represent the mean, shown with standard deviations and p-values (two tailed Welch’s t test). F. Western blots of eIF4E and Ezrin IPs from the cytoplasmic fractions of MM6 cells in suspension or G . After invasion through HS-5 bone marrow stroma (invaded). Fractionation controls are provided in . H. RIPs from MM6 cytoplasmic fraction from invaded cells using anti-eIF4E (eIF4E RIP) or anti-Ezrin (Ezrin RIP) antibodies. Data are from RT-qPCR represented relative to input. Each symbol represents a biological replicate performed independently with triplicates. Bars represent the mean, shown with standard deviations and p-values (two tailed Welch’s t test). I. Count of the number of pseudopods observed in suspension and invaded MM6 cells represented as a fraction relative to the total cells counted. Each symbol represents a biological replicate. Bars represent the mean, shown with standard deviations and p-values (two-way ANOVA). J . Immunofluorescence and confocal microscopy demonstrating eIF4E, Ezrin, CD44 and rRNA are localized to the same pseudopods (white arrows). All confocal micrographs represent a single section through the plane of the cell. Scale bar = 10 µm

    Article Snippet: Antibodies for immunoblotting: mouse monoclonal anti-eIF4E (cat# 610270, BD Biosciences), mouse monoclonal anti-β-Actin (cat# A5441, Sigma Aldrich), rabbit polyclonal anti-Mcl-1 (S-19) (cat# sc-819, Santa Cruz), mouse monoclonal anti-HSP90α/β (F-8) (cat# sc-13119, Santa Cruz), rabbit polyclonal anti-Myc (cat# ab32072, Abcam), Mouse monoclonal anti-CD44 antibody (cat# 156–3 C11, Cell Signaling Technology), rabbit polyclonal anti-CD44 (cat# A12410, Abclonal), rabbit polyclonal anti-HAS3 antibody (cat# ab154104, Abcam), rabbit polyclonal anti-phosphoglucomutase 5 (cat# AI14638, Abgent), rabbit polyclonal anti-Lamin A (C-terminal) (cat# L1293, Sigma Aldrich), rabbit polyclonal anti-GAPDH (FL-335) (cat# sc-25778, Santa Cruz), rabbit polyclonal anti-UGDH (cat#AP12613b-EV, Abgent), rabbit monoclonal anti-Hexokinase II (cat# 2867, Cell Signaling Technology), rabbit monoclonal anti-UAP1 antibody (cat# 2716, GenuinBiotech), mouse monoclonal anti-RPL17 (C-8, cat# sc-515904, Santa Cruz), mouse monoclonal anti-RPS16 (D-8, cat# sc-518206; Santa Cruz), mouse monoclonal anti-RPS6 (C-8, cat# sc-74459, Santa Cruz), mouse monoclonal anti-eIF3e (G-7, cat# sc-390413, Santa Cruz), mouse monoclonal anti-eIF3p110 (B-6, cat# sc-74507, Santa Cruz), mouse monoclonal anti-eIF3b (A-7, cat# sc-374156, Santa Cruz), mouse monoclonal anti-eIF4AI/II (H-5, cat# sc-377315, Santa Cruz), mouse monoclonal anti-eIF4G (A-10, cat# sc-133155, Santa Cruz), mouse monoclonal anti-Nopp140 (E-7, cat# sc-374033, Santa Cruz), rabbit monoclonal anti-histone H3 acetyl K27 (cat# ab177178, Abcam), rabbit polyclonal Calreticulin (cat# AW5211, ABCEPTA), rabbit polyclonal anti-Calnexin (cat# ab22595, Abcam), rabbit polyclonal anti-Ezrin antibody (cat# PA5-80603, Invitrogen), mouse monoclonal anti-Ezrin (CPTC-Ezrin-1, cat# AB_2100318, DSHB), mouse monoclonal anti-MEK-1 (H-8, sc-6250, Santa Cruz), and mouse monoclonal anti-cytochrome c (A-8, cat# sc-13156, Santa Cruz).

    Techniques: Western Blot, Suspension, Knockdown, Luciferase, Negative Control, Control, Immunoprecipitation, Quantitative RT-PCR, Two Tailed Test, Fractionation, Immunofluorescence, Confocal Microscopy

    HCT116 cells are CLNS1A-independent until PRMT5 activity is decreased (A) Western blot analyses of HA (CLNSIA), SDMA (methyl-SmB), and HSP90 as loading control in HCT116 dTag-CLNS1A #1 ( Left ) and #2 ( Right ) maintained in 1 μM dTag-13 for the indicated number of days. (B) Representative Western blot analysis of CLNS1A, SDMA (methyl-SmB), and loading control GAPDH levels in HCT116 sgCtrl and four sgCLNS1A clones ( n = 4 biological replicates). (C) Relative proliferation of HCT116 sgCtrl and four sgCLNS1A clones through analyses of cumulative population doubling over a 6-day period. Data represent mean ± SD of 10 technical replicates. (D) Relative viability of HCT116 sgCtrl and indicated sgCLNS1A clones treated with the PRMT5i JNJ-64619178 for 6 days. Data represent mean ± SD of 3 technical replicates. (E–G) HCT116 parental or two dTag-CLNS1A clones treated with or without 1μM dTag-13 in combination with the indicated concentrations of JNJ-64619178 (PRMT5i). (E) Relative viability was assessed after treatment for 6 days. Data represent mean ± SD of 3 technical replicates. Red markings correspond to the critical PRMT5i doses used in F and 5G. (F) Western blot analyses of HA (CLNS1A), SDMA, and loading control HSP90 after treatment with the critical indicated PRMT5i doses for 3 days (G) Relative levels of a representative DI in EIF4E were assessed by qRT-PCR after treatment with the critical indicated PRMT5i doses for 3 days. Data represent mean ± SD of 3 technical replicates. For all panels, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001, Student’s t test.

    Journal: iScience

    Article Title: The PRMT5-splicing axis is a critical oncogenic vulnerability that regulates detained intron splicing

    doi: 10.1016/j.isci.2025.112965

    Figure Lengend Snippet: HCT116 cells are CLNS1A-independent until PRMT5 activity is decreased (A) Western blot analyses of HA (CLNSIA), SDMA (methyl-SmB), and HSP90 as loading control in HCT116 dTag-CLNS1A #1 ( Left ) and #2 ( Right ) maintained in 1 μM dTag-13 for the indicated number of days. (B) Representative Western blot analysis of CLNS1A, SDMA (methyl-SmB), and loading control GAPDH levels in HCT116 sgCtrl and four sgCLNS1A clones ( n = 4 biological replicates). (C) Relative proliferation of HCT116 sgCtrl and four sgCLNS1A clones through analyses of cumulative population doubling over a 6-day period. Data represent mean ± SD of 10 technical replicates. (D) Relative viability of HCT116 sgCtrl and indicated sgCLNS1A clones treated with the PRMT5i JNJ-64619178 for 6 days. Data represent mean ± SD of 3 technical replicates. (E–G) HCT116 parental or two dTag-CLNS1A clones treated with or without 1μM dTag-13 in combination with the indicated concentrations of JNJ-64619178 (PRMT5i). (E) Relative viability was assessed after treatment for 6 days. Data represent mean ± SD of 3 technical replicates. Red markings correspond to the critical PRMT5i doses used in F and 5G. (F) Western blot analyses of HA (CLNS1A), SDMA, and loading control HSP90 after treatment with the critical indicated PRMT5i doses for 3 days (G) Relative levels of a representative DI in EIF4E were assessed by qRT-PCR after treatment with the critical indicated PRMT5i doses for 3 days. Data represent mean ± SD of 3 technical replicates. For all panels, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001, Student’s t test.

    Article Snippet: Rabbit anti-eIF4E Monoclonal Antibody , Cell Signaling Technology , Cat#2067; RRID: AB_2097675.

    Techniques: Activity Assay, Western Blot, Control, Clone Assay, Quantitative RT-PCR

    Fig. 4 | Compound 4 inhibits eIF4G:eIF4E binding and cap-dependent transla- tion in cell lysate assays. a Lysates from SW620 cells were incubated with 1–100 µM compound 4 or 5 or positive control peptide (RIIY) for 30 min. Endo- genous eIF4E was immunoprecipitated and immunoblotted for eIF4G, 4E-BP1 and eIF4E. Quantitation of 4E-BP1 (b) or eIF4G (c) with endogenous eIF4E in SW620 and HeLa cell lysates, determined by the electro-chemiluminescent binding assay fol- lowing incubation for 30 min with DMSO vehicle (Cont), 100 µM compound 4 or 100 µM RIIY peptide. Complexes were immobilised by an eIF4E antibody and captured eIF4E, eIF4G and 4E-BP1 detected by their respective secondary anti- bodies. Values represent ratios of 4E-BP1:eIF4E or eIF4G:eIF4E electro- chemiluminescence relative to DMSO control (n = 2 biological replicates). d Electro-chemiluminescent assay for binding of eIF4G or 4E-BP1 with eIF4E in SW620 (n = 2 biological replicates), or (e) in HeLa lysates (n = 3 biological replicates, mean ± SD) following incubation for 30 min with compound 4 or 5. Results are expressed as luminescence signals relative to DMSO control. f Quantification of eIF4E:eIF4G interaction in H1299 cells by electro-chemiluminescent assay. Cell lysates treated with RIIY 4E-BP1 derived peptide or RIIG negative control peptide at 0.1–100 µM for 30 min (n = 2 biological replicates). g Quantification of the endo- genous eIF4E:eIF4G interaction in H1299 cell lysates at 0.1–100 µM (for 6 h) of compound 4 or 5, as measured by electro-chemiluminescent assay (mean ± SD from n = 3 biological replicates). h HeLa cell lysates for in vitro translation were incubated for 30 min with 1, 10, 100 µM of compound 4 or 5. Results are expressed as firefly or renilla luminescence signal normalized to DMSO control and expressed as % (mean ± SD from n = 3 biological replicates). Significance was determined using two-sided unpaired t-test comparing compound 4 to compound 5 at each concentration. Statistically significant p-values (p < 0.05) are shown on the plot and source data is located in the Source Data file.

    Journal: Nature communications

    Article Title: Integrating fragment-based screening with targeted protein degradation and genetic rescue to explore eIF4E function.

    doi: 10.1038/s41467-024-54356-1

    Figure Lengend Snippet: Fig. 4 | Compound 4 inhibits eIF4G:eIF4E binding and cap-dependent transla- tion in cell lysate assays. a Lysates from SW620 cells were incubated with 1–100 µM compound 4 or 5 or positive control peptide (RIIY) for 30 min. Endo- genous eIF4E was immunoprecipitated and immunoblotted for eIF4G, 4E-BP1 and eIF4E. Quantitation of 4E-BP1 (b) or eIF4G (c) with endogenous eIF4E in SW620 and HeLa cell lysates, determined by the electro-chemiluminescent binding assay fol- lowing incubation for 30 min with DMSO vehicle (Cont), 100 µM compound 4 or 100 µM RIIY peptide. Complexes were immobilised by an eIF4E antibody and captured eIF4E, eIF4G and 4E-BP1 detected by their respective secondary anti- bodies. Values represent ratios of 4E-BP1:eIF4E or eIF4G:eIF4E electro- chemiluminescence relative to DMSO control (n = 2 biological replicates). d Electro-chemiluminescent assay for binding of eIF4G or 4E-BP1 with eIF4E in SW620 (n = 2 biological replicates), or (e) in HeLa lysates (n = 3 biological replicates, mean ± SD) following incubation for 30 min with compound 4 or 5. Results are expressed as luminescence signals relative to DMSO control. f Quantification of eIF4E:eIF4G interaction in H1299 cells by electro-chemiluminescent assay. Cell lysates treated with RIIY 4E-BP1 derived peptide or RIIG negative control peptide at 0.1–100 µM for 30 min (n = 2 biological replicates). g Quantification of the endo- genous eIF4E:eIF4G interaction in H1299 cell lysates at 0.1–100 µM (for 6 h) of compound 4 or 5, as measured by electro-chemiluminescent assay (mean ± SD from n = 3 biological replicates). h HeLa cell lysates for in vitro translation were incubated for 30 min with 1, 10, 100 µM of compound 4 or 5. Results are expressed as firefly or renilla luminescence signal normalized to DMSO control and expressed as % (mean ± SD from n = 3 biological replicates). Significance was determined using two-sided unpaired t-test comparing compound 4 to compound 5 at each concentration. Statistically significant p-values (p < 0.05) are shown on the plot and source data is located in the Source Data file.

    Article Snippet: Monoclonal anti-eIF4E antibody (R&D Systems, Cat#MAB3228, RRID:AB_2097694) was biotinylated using the Lightning-Link kit (R&D Systems Inc. Cat# 371-0010) according to the manufacturer instructions and 20μg used to coat 1ml streptavidinmagnetic beads (Pierce Cat# 88817) for 1 hr at room temperature (RT) with rotatory shaking.

    Techniques: Binding Assay, Incubation, Positive Control, Immunoprecipitation, Quantitation Assay, Control, Derivative Assay, Negative Control, In Vitro, Concentration Assay