eif4g (Proteintech)
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Proteintech
eif4g
Eif4g, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/eif4g/EIF4G1+Fusion+Protein/pmc12841665-134-13-14
Average 94 stars, based on 3 article reviews
Eif4g, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/eif4g/EIF4G1+Fusion+Protein/pmc12841665-134-13-14
Average 94 stars, based on 3 article reviews
eif4g - by Bioz Stars,
2026-09
94/100 stars
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other:Article Title: DDX3 Regulates the Cap‐Independent Translation of the Japanese Encephalitis Virus via Its Interactions with PABP1 and the Untranslated Regions of the Viral Genome Article Snippet: Mouse anti‐DDX3, mouse anti‐PABP1, mouse anti‐eIF4G, mouse anti‐rpS6, rabbit anti‐eIF5, and rabbit Article Title: Baicalein suppresses Coxsackievirus B3 replication by inhibiting caspase-1 and viral protease 2A Article Snippet: Antibodies against GAPDH, EGFP, eIF4G, β-tubulin, β-actin, caspase-1, HRP-conjugated goat anti-mouse IgG (H + L), and SDS Page:Article Title: Structural and mechanistic insights into translation initiation on the enterovirus Type 1 IRES Article Snippet: Eluate was adjusted to a KCl concentration of 100 mM before application to a Capto HiRes S 10/100 column (Cytiva) equilibrated in buffer D. A linear KCl gradient from 100 mM to 1.0 M (30 CV) was used to elute eIF3-containing fractions, which were pooled and layered onto a 10-30% (w/v) sucrose gradient in buffer E (20 mM Tris-HCl pH 7.5, 400 mM KCl, 2.0 mM DTT, 0.1 mM EDTA, 10% w/v glycerol). .. Ultracentrifugation in an SW-41 rotor (287,000 x g, 4°C, 22 h) was performed to separate eIF3 from Western Blot:Article Title: Structural and mechanistic insights into translation initiation on the enterovirus Type 1 IRES Article Snippet: Eluate was adjusted to a KCl concentration of 100 mM before application to a Capto HiRes S 10/100 column (Cytiva) equilibrated in buffer D. A linear KCl gradient from 100 mM to 1.0 M (30 CV) was used to elute eIF3-containing fractions, which were pooled and layered onto a 10-30% (w/v) sucrose gradient in buffer E (20 mM Tris-HCl pH 7.5, 400 mM KCl, 2.0 mM DTT, 0.1 mM EDTA, 10% w/v glycerol). .. Ultracentrifugation in an SW-41 rotor (287,000 x g, 4°C, 22 h) was performed to separate eIF3 from Incubation:Article Title: The Translational Landscape Revealed the Sequential Treatment Containing ATRA plus PI3K/AKT Inhibitors as an Efficient Strategy for AML Therapy Article Snippet: Then, the separated protein was transferred onto methanol-activated PVDF membranes (Millipore, Boston, MA, USA). .. After being blocked with 5% defatted milk for 2 h at room temperature, the membranes were then incubated with the appropriate diluted antibodies against eIF4E, eIF4A, |
![A , Western blot showing indicated proteins expression levels in YUMM1.1 cells expressing a shRNA control or targeting ASS1. HSP90 serves as a loading control. B , Western blot showing indicated proteins expression levels in YUMM1.7 cells expressing a shRNA control or targeting ASS1. HSP90 serves as a loading control. C , Western blot showing indicated proteins expression levels in YUMM2.1 cells expressing an ectopic empty vector or containing the open reading frame of ASS1. HSP90 serves as a loading control. D , Renilla over Firefly luminescent ratio quantification in YUMM1.1 cells expressing a shRNA control or targeting ASS1 (n=4; mean ± SEM). E , Renilla over Firefly luminescent ratio quantification in YUMM1.7 cells expressing a shRNA control or targeting ASS1 (n=3; mean ± SEM). F , Renilla over Firefly luminescent ratio quantification in YUMM2.1 cells expressing an ectopic empty vector or containing the open reading frame of ASS1 (n=3; mean ± SEM). G , Protein synthesis rates were determined in YUMM1.1 cells expressing a shRNA control or targeting ASS1. Cells were then pulsed for 30 min with [ 35 S]Cys/Met, and the incorporation of 35 S into proteins was quantified and normalized to the total protein amount. Cells treated 30 minutes with 100µg/mL of cycloheximide (CHX) are used as a positive control. The data are presented as the mean (n = 4). H , Protein synthesis rates were determined in YUMM1.7 cells expressing a shRNA control or targeting ASS1. Cells were then pulsed for 30 min with [ 35 S]Cys/Met, and the incorporation of 35 S into proteins was quantified and normalized to the total protein amount. Cells treated 30 minutes with 100µg/mL of cycloheximide (CHX) are used as a positive control. The data are presented as the mean (n = 3). I , Protein synthesis rates were determined in YUMM2.1 cells expressing an ectopic empty vector or containing the open reading frame of ASS1. Cells were then pulsed for 30 min with [ 35 S]Cys/Met, and the incorporation of 35 S into proteins was quantified and normalized to the total protein amount. Cells treated 30 minutes with 100µg/mL of cycloheximide (CHX) are used as a positive control. The data are presented as the mean (n = 3). J , Proximity Ligation Assay showing eiF4E/eiF4G interactions in YUMM1.1 cells expressing a shRNA control or targeting ASS1. Representative images are presented in the left panel, and quantifications are presented in the right panel. K , Proximity Ligation Assay showing eiF4E/eiF4G interactions in YUMM1.7 cells expressing a shRNA control or targeting ASS1. Representative images are presented in the left panel, and quantifications are presented in the right panel.](https://bio-rxiv-images-cdn.bioz.com/dois_ending_with_79/10__64898_slash_2026__03__17__712479/10__64898_slash_2026__03__17__712479___F3.large.jpg)
![Chronic stress pre-incubated cells fail to respond to form SGs by acute stress (A) U2OS cells were subjected to treatment with SA (10, 50, 100, and 500 μM) at each time (0, 1, 4, 12, and 24 h). Cells were examined for the presence of the core SG markers G3BP1 (green), eIF4G (red), and eIF3b (blue). Scale bars represent 10 μm. All positive cells were quantified. p values were assessed using a one-way ANOVA (vs. NT; p ∗∗∗∗ <0.0001). Results are mean ± S.E.M. ( n = 3). (B) Schematic illustration of the experimental timeline. (C–F) U2OS cells were subjected to treatment with 100 μM SA for 1 h after pre-incubation with 10 μM SA, 30 μM Mena (menadione), 2 μM Drb (doxorubicin), 1 μM Tg (thapsigargin), 25 μg/mL Tun (tunicamycin), 25 μg/mL BA (brefeldin A), 60 μM CCCP (carbonyl cyanide m -chlorophenyl hydrazone), 60 mM 2DG (2-deoxy-D-glucose), or HBSS for 24 h. Unstressed cells (NT) were used as a control. (C) Cells were examined for the presence of the core SG markers G3BP1, eIF4G, and eIF3B. (D) Representative images of U2OS cells stained with G3BP1 (green), eIF4G (red), and eIF3B (blue) after the cells had been subjected to specific stresses. Scale bars represent 20 μm. (E) Cells were examined for the presence of the core SG marker G3BP1 and poly (A) mRNAs (FISH using oligo[dT] probe). (F) Representative images of U2OS cells stained with G3BP1 (green) and oligo(dT) (red) after the cells had been subjected to specific stresses. Scale bars represent 20 μm. (C and E) p values were assessed using a one-way ANOVA (vs. 1 h SA; p ∗∗∗∗ <0.0001). Results are mean ± S.E.M. ( n = 3). All experiments were done for each of the three biological replicates (independent experiments).](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_8549/pmc12828549/pmc12828549__gr1.jpg)
