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Sino Biological recombinant egfr extracellular domain
EA Directly Binds to the <t>Extracellular</t> Domain of <t>EGFR.</t> (A) SPR sensorgrams showing the binding affinity of EA to the extracellular domain of EGFR. The traces represent real‐time interactions at EA concentrations of 2, 1, 0.5, and 0.2 μM. (B) Three‐dimensional (3D) computer simulation depicting the docking of EA with the extracellular domain of EGFR. (C) 3D docking diagram illustrating EA binding to the extracellular segment of EGFR. (D) Magnified view of the EA binding pocket within EGFR. (E) 3D model of the interaction between EA and EGFR, with green and yellow dotted lines representing hydrogen bonds and hydrophobic interactions, respectively. (F) Two‐dimensional (2D) model of the interaction between EA and EGFR. 2D, two‐dimensional; 3D, three‐dimensional; EA, ellagic acid; EGFR, epidermal growth factor receptor; SPR, surface plasmon resonance.
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EA Directly Binds to the <t>Extracellular</t> Domain of <t>EGFR.</t> (A) SPR sensorgrams showing the binding affinity of EA to the extracellular domain of EGFR. The traces represent real‐time interactions at EA concentrations of 2, 1, 0.5, and 0.2 μM. (B) Three‐dimensional (3D) computer simulation depicting the docking of EA with the extracellular domain of EGFR. (C) 3D docking diagram illustrating EA binding to the extracellular segment of EGFR. (D) Magnified view of the EA binding pocket within EGFR. (E) 3D model of the interaction between EA and EGFR, with green and yellow dotted lines representing hydrogen bonds and hydrophobic interactions, respectively. (F) Two‐dimensional (2D) model of the interaction between EA and EGFR. 2D, two‐dimensional; 3D, three‐dimensional; EA, ellagic acid; EGFR, epidermal growth factor receptor; SPR, surface plasmon resonance.
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MedChemExpress human epidermal growth factor receptor egfr protein
EA Directly Binds to the <t>Extracellular</t> Domain of <t>EGFR.</t> (A) SPR sensorgrams showing the binding affinity of EA to the extracellular domain of EGFR. The traces represent real‐time interactions at EA concentrations of 2, 1, 0.5, and 0.2 μM. (B) Three‐dimensional (3D) computer simulation depicting the docking of EA with the extracellular domain of EGFR. (C) 3D docking diagram illustrating EA binding to the extracellular segment of EGFR. (D) Magnified view of the EA binding pocket within EGFR. (E) 3D model of the interaction between EA and EGFR, with green and yellow dotted lines representing hydrogen bonds and hydrophobic interactions, respectively. (F) Two‐dimensional (2D) model of the interaction between EA and EGFR. 2D, two‐dimensional; 3D, three‐dimensional; EA, ellagic acid; EGFR, epidermal growth factor receptor; SPR, surface plasmon resonance.
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Sino Biological egfr ext
EA Directly Binds to the <t>Extracellular</t> Domain of <t>EGFR.</t> (A) SPR sensorgrams showing the binding affinity of EA to the extracellular domain of EGFR. The traces represent real‐time interactions at EA concentrations of 2, 1, 0.5, and 0.2 μM. (B) Three‐dimensional (3D) computer simulation depicting the docking of EA with the extracellular domain of EGFR. (C) 3D docking diagram illustrating EA binding to the extracellular segment of EGFR. (D) Magnified view of the EA binding pocket within EGFR. (E) 3D model of the interaction between EA and EGFR, with green and yellow dotted lines representing hydrogen bonds and hydrophobic interactions, respectively. (F) Two‐dimensional (2D) model of the interaction between EA and EGFR. 2D, two‐dimensional; 3D, three‐dimensional; EA, ellagic acid; EGFR, epidermal growth factor receptor; SPR, surface plasmon resonance.
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Image Search Results


EA Directly Binds to the Extracellular Domain of EGFR. (A) SPR sensorgrams showing the binding affinity of EA to the extracellular domain of EGFR. The traces represent real‐time interactions at EA concentrations of 2, 1, 0.5, and 0.2 μM. (B) Three‐dimensional (3D) computer simulation depicting the docking of EA with the extracellular domain of EGFR. (C) 3D docking diagram illustrating EA binding to the extracellular segment of EGFR. (D) Magnified view of the EA binding pocket within EGFR. (E) 3D model of the interaction between EA and EGFR, with green and yellow dotted lines representing hydrogen bonds and hydrophobic interactions, respectively. (F) Two‐dimensional (2D) model of the interaction between EA and EGFR. 2D, two‐dimensional; 3D, three‐dimensional; EA, ellagic acid; EGFR, epidermal growth factor receptor; SPR, surface plasmon resonance.

Journal: FASEB BioAdvances

Article Title: Ellagic Acid and Its Nanoparticles Mitigate Atherosclerosis by Elevating Low‐Density Lipoprotein Receptor Levels Through Targeting of the Epidermal Growth Factor Receptor

doi: 10.1096/fba.2025-00178

Figure Lengend Snippet: EA Directly Binds to the Extracellular Domain of EGFR. (A) SPR sensorgrams showing the binding affinity of EA to the extracellular domain of EGFR. The traces represent real‐time interactions at EA concentrations of 2, 1, 0.5, and 0.2 μM. (B) Three‐dimensional (3D) computer simulation depicting the docking of EA with the extracellular domain of EGFR. (C) 3D docking diagram illustrating EA binding to the extracellular segment of EGFR. (D) Magnified view of the EA binding pocket within EGFR. (E) 3D model of the interaction between EA and EGFR, with green and yellow dotted lines representing hydrogen bonds and hydrophobic interactions, respectively. (F) Two‐dimensional (2D) model of the interaction between EA and EGFR. 2D, two‐dimensional; 3D, three‐dimensional; EA, ellagic acid; EGFR, epidermal growth factor receptor; SPR, surface plasmon resonance.

Article Snippet: The recombinant EGFR extracellular domain (Cat: 10001‐H08H) was purchased from Sino Biological (Beijing, China).

Techniques: Binding Assay, SPR Assay

EA Enhances LDLR Expression via the EGFR‐ERK Signaling Pathway. (A) Effect of EA treatment (24 h) on LDLR mRNA levels in HepG2 cells, determined by real‐time quantitative PCR. (B) Impact of EA on LDLR mRNA stability in HepG2 cells, assessed following inhibition of mRNA synthesis with actinomycin D. (C) Effects of EA at concentrations of 10, 20, and 40 μM on phosphorylated ERK (p‐ERK) and phosphorylated EGFR (p‐EGFR) levels in HepG2 cells after 1‐h treatment, as evaluated by Western blotting analysis. (D) Effects of EA on p‐ERK, p‐EGFR, and LDLR levels in HepG2 cells following after 1‐h treatment with or without EGFR pathway blockade by cetuximab, as assessed by Western blotting analysis. Data are presented as mean ± SEM ( n = 3). Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001. EA, ellagic acid; EGFR, epidermal growth factor receptor; ERK, extracellular signal‐regulated kinase; LDLR, low‐density lipoprotein receptor; p‐EGFR, phosphorylated EGFR; p‐ERK, phosphorylated ERK; SEM, standard error of the mean.

Journal: FASEB BioAdvances

Article Title: Ellagic Acid and Its Nanoparticles Mitigate Atherosclerosis by Elevating Low‐Density Lipoprotein Receptor Levels Through Targeting of the Epidermal Growth Factor Receptor

doi: 10.1096/fba.2025-00178

Figure Lengend Snippet: EA Enhances LDLR Expression via the EGFR‐ERK Signaling Pathway. (A) Effect of EA treatment (24 h) on LDLR mRNA levels in HepG2 cells, determined by real‐time quantitative PCR. (B) Impact of EA on LDLR mRNA stability in HepG2 cells, assessed following inhibition of mRNA synthesis with actinomycin D. (C) Effects of EA at concentrations of 10, 20, and 40 μM on phosphorylated ERK (p‐ERK) and phosphorylated EGFR (p‐EGFR) levels in HepG2 cells after 1‐h treatment, as evaluated by Western blotting analysis. (D) Effects of EA on p‐ERK, p‐EGFR, and LDLR levels in HepG2 cells following after 1‐h treatment with or without EGFR pathway blockade by cetuximab, as assessed by Western blotting analysis. Data are presented as mean ± SEM ( n = 3). Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001. EA, ellagic acid; EGFR, epidermal growth factor receptor; ERK, extracellular signal‐regulated kinase; LDLR, low‐density lipoprotein receptor; p‐EGFR, phosphorylated EGFR; p‐ERK, phosphorylated ERK; SEM, standard error of the mean.

Article Snippet: The recombinant EGFR extracellular domain (Cat: 10001‐H08H) was purchased from Sino Biological (Beijing, China).

Techniques: Expressing, Real-time Polymerase Chain Reaction, Inhibition, Western Blot

EA‐NPs Activate the EGFR Pathway to Enhance LDLR Expression in HFD‐Fed ApoE − / − Mice. (A) LDLR mRNA levels in the liver of ApoE − / − mice, determined by real‐time quantitative PCR. (B) Protein levels of LDLR, p‐ERK, and p‐EGFR in the liver of ApoE − / − mice, assessed by Western blotting. Data are presented as mean ± SEM of six biological replicates. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001. Experimental groups: HFD group (high‐fat and high‐cholesterol diet with uncoated EA nanoparticles); HFD + EA‐NPs group (high‐fat and high‐cholesterol diet with coated EA‐NPs). ApoE, apolipoprotein E; EA‐NPs, ellagic acid‐loaded human serum albumin nanoparticles; EGFR, epidermal growth factor receptor; ERK, extracellular signal‐regulated kinase; HFD, high‐fat diet; LDLR, low‐density lipoprotein receptor; p‐EGFR, phosphorylated EGFR; p‐ERK, phosphorylated ERK; SEM, standard error of the mean.

Journal: FASEB BioAdvances

Article Title: Ellagic Acid and Its Nanoparticles Mitigate Atherosclerosis by Elevating Low‐Density Lipoprotein Receptor Levels Through Targeting of the Epidermal Growth Factor Receptor

doi: 10.1096/fba.2025-00178

Figure Lengend Snippet: EA‐NPs Activate the EGFR Pathway to Enhance LDLR Expression in HFD‐Fed ApoE − / − Mice. (A) LDLR mRNA levels in the liver of ApoE − / − mice, determined by real‐time quantitative PCR. (B) Protein levels of LDLR, p‐ERK, and p‐EGFR in the liver of ApoE − / − mice, assessed by Western blotting. Data are presented as mean ± SEM of six biological replicates. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001. Experimental groups: HFD group (high‐fat and high‐cholesterol diet with uncoated EA nanoparticles); HFD + EA‐NPs group (high‐fat and high‐cholesterol diet with coated EA‐NPs). ApoE, apolipoprotein E; EA‐NPs, ellagic acid‐loaded human serum albumin nanoparticles; EGFR, epidermal growth factor receptor; ERK, extracellular signal‐regulated kinase; HFD, high‐fat diet; LDLR, low‐density lipoprotein receptor; p‐EGFR, phosphorylated EGFR; p‐ERK, phosphorylated ERK; SEM, standard error of the mean.

Article Snippet: The recombinant EGFR extracellular domain (Cat: 10001‐H08H) was purchased from Sino Biological (Beijing, China).

Techniques: Expressing, Real-time Polymerase Chain Reaction, Western Blot