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A Mutations introduced to disrupt Sm-x-x-x-Sm dimerization motifs40 in the <t>EGFR</t> TM domain. The three Sm-x-x-x-Sm motifs are marked, where Sm is any small amino acid (red): T-g-m-v-G; G-m-v-g-A; and A-l-g-i-G. All Sm residues were replaced with valine in TM3X. B SPT data for wild type EGFR (gray) and a variant with the TM3X TM domain shown in A (blue). Unliganded receptors were tracked using QD-HA (open diamonds), and ligand-bound receptors were tracked using 200 pM QD-EGF (filled diamonds). EGF induces a similar slow-down for wild type EGFR (n = 40 cells without ligand, 42 with; P = 6.7 × 10−6) and the TM3X variant (n = 45 without ligand, 46 with; P = 1.9 × 10−7). Unpaired two-sided Welch’s t-tests were used to calculate P values (**P < 1×10−3; ***P < 1×10−6). See also Table S2. C pEGFR immunoblots of wild type and TM3X EGFR activated with 16 nM EGF for 5 min and probed <t>with</t> <t>anti-pY1173</t> (upper), anti-EGFR (middle) and anti-GRB2 (lower) as loading control. Representative of three biological repeats.

Total Egfr, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 68 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+total+egfr/pmc10835193-567-20-22?v=R%26D+Systems
Average 93 stars, based on 68 article reviews

total egfr - by Bioz Stars, 2026-08

93/100 stars

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1) Product Images from "Distinct interactions stabilize EGFR dimers and higher-order oligomers in cell membranes"

Article Title: Distinct interactions stabilize EGFR dimers and higher-order oligomers in cell membranes

Journal: Cell reports

doi: 10.1016/j.celrep.2023.113603

A Mutations introduced to disrupt Sm-x-x-x-Sm dimerization motifs40 in the EGFR TM domain. The three Sm-x-x-x-Sm motifs are marked, where Sm is any small amino acid (red): T-g-m-v-G; G-m-v-g-A; and A-l-g-i-G. All Sm residues were replaced with valine in TM3X. B SPT data for wild type EGFR (gray) and a variant with the TM3X TM domain shown in A (blue). Unliganded receptors were tracked using QD-HA (open diamonds), and ligand-bound receptors were tracked using 200 pM QD-EGF (filled diamonds). EGF induces a similar slow-down for wild type EGFR (n = 40 cells without ligand, 42 with; P = 6.7 × 10−6) and the TM3X variant (n = 45 without ligand, 46 with; P = 1.9 × 10−7). Unpaired two-sided Welch’s t-tests were used to calculate P values (**P < 1×10−3; ***P < 1×10−6). See also Table S2. C pEGFR immunoblots of wild type and TM3X EGFR activated with 16 nM EGF for 5 min and probed with anti-pY1173 (upper), anti-EGFR (middle) and anti-GRB2 (lower) as loading control. Representative of three biological repeats.

Figure Legend Snippet: A Mutations introduced to disrupt Sm-x-x-x-Sm dimerization motifs40 in the EGFR TM domain. The three Sm-x-x-x-Sm motifs are marked, where Sm is any small amino acid (red): T-g-m-v-G; G-m-v-g-A; and A-l-g-i-G. All Sm residues were replaced with valine in TM3X. B SPT data for wild type EGFR (gray) and a variant with the TM3X TM domain shown in A (blue). Unliganded receptors were tracked using QD-HA (open diamonds), and ligand-bound receptors were tracked using 200 pM QD-EGF (filled diamonds). EGF induces a similar slow-down for wild type EGFR (n = 40 cells without ligand, 42 with; P = 6.7 × 10−6) and the TM3X variant (n = 45 without ligand, 46 with; P = 1.9 × 10−7). Unpaired two-sided Welch’s t-tests were used to calculate P values (**P < 1×10−3; ***P < 1×10−6). See also Table S2. C pEGFR immunoblots of wild type and TM3X EGFR activated with 16 nM EGF for 5 min and probed with anti-pY1173 (upper), anti-EGFR (middle) and anti-GRB2 (lower) as loading control. Representative of three biological repeats.

Techniques Used: Variant Assay, Western Blot

Figure Legend Snippet: Key resources table

Techniques Used: Polymer, Plasmid Preparation, Affinity Purification, Virus, Recombinant, Expressing, Software, Imaging

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Journal: Cell reports

Article Title: Distinct interactions stabilize EGFR dimers and higher-order oligomers in cell membranes

doi: 10.1016/j.celrep.2023.113603

Figure Lengend Snippet: A Mutations introduced to disrupt Sm-x-x-x-Sm dimerization motifs40 in the EGFR TM domain. The three Sm-x-x-x-Sm motifs are marked, where Sm is any small amino acid (red): T-g-m-v-G; G-m-v-g-A; and A-l-g-i-G. All Sm residues were replaced with valine in TM3X. B SPT data for wild type EGFR (gray) and a variant with the TM3X TM domain shown in A (blue). Unliganded receptors were tracked using QD-HA (open diamonds), and ligand-bound receptors were tracked using 200 pM QD-EGF (filled diamonds). EGF induces a similar slow-down for wild type EGFR (n = 40 cells without ligand, 42 with; P = 6.7 × 10−6) and the TM3X variant (n = 45 without ligand, 46 with; P = 1.9 × 10−7). Unpaired two-sided Welch’s t-tests were used to calculate P values (**P < 1×10−3; ***P < 1×10−6). See also Table S2. C pEGFR immunoblots of wild type and TM3X EGFR activated with 16 nM EGF for 5 min and probed with anti-pY1173 (upper), anti-EGFR (middle) and anti-GRB2 (lower) as loading control. Representative of three biological repeats.

Article Snippet: 73 For signaling studies, primary antibodies were all used at a 1:1,000 dilution as follows: for phosphorylated EGFR (pY1173: CST#4407), total EGFR (R&D AF231) and ERK1/2 (pT202/pY204: CST #9106; total ERK: CST#4696).

Techniques: Variant Assay, Western Blot

Journal: Cell reports

Article Title: Distinct interactions stabilize EGFR dimers and higher-order oligomers in cell membranes

doi: 10.1016/j.celrep.2023.113603

Figure Lengend Snippet: Key resources table

Techniques: Polymer, Plasmid Preparation, Affinity Purification, Virus, Recombinant, Expressing, Software, Imaging

EGF receptor tyrosine kinase inhibitor erlotinib inhibits EGF-mediated phosphorylation of EGFR and the TSH-induced increase of thyroid-specific genes in thyrocytes. (A) Erlotinib and AG1478 inhibit phosphorylation of EGFR stimulated by EGF in thyrocytes. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Erlotinib and AG1478, EGF receptor tyrosine kinase inhibitors were then added at the indicated doses for a 20-minute pretreatment followed by a stimulation by EGF at 30 ng/mL for 5 minutes. Cell lysates were analyzed for phospho-EGFR (pEGFR) by ELISA. Data are expressed as mean ± SD, n = 2 patient donors. (B) EGF receptor tyrosine kinase inhibitor erlotinib inhibits TSH-induced upregulation of TG, TPO, DIO2, NIS, and TSHR mRNAs. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Erlotinib was then added at 5 µM alone or in combination with 1 mU/mL TSH for 48 hours. Cell lysates were analyzed for TG, TPO, DIO2, NIS, and TSHR mRNAs by RT-qPCR. Each experiment contained biological duplicates. Data are expressed as mean ± SEM, n = 3 patient donors.

Journal: Endocrinology

Article Title: Opposing Effects of EGF Receptor Signaling on Proliferation and Differentiation Initiated by EGF or TSH/EGF Receptor Transactivation

doi: 10.1210/endocr/bqac136

Figure Lengend Snippet: EGF receptor tyrosine kinase inhibitor erlotinib inhibits EGF-mediated phosphorylation of EGFR and the TSH-induced increase of thyroid-specific genes in thyrocytes. (A) Erlotinib and AG1478 inhibit phosphorylation of EGFR stimulated by EGF in thyrocytes. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Erlotinib and AG1478, EGF receptor tyrosine kinase inhibitors were then added at the indicated doses for a 20-minute pretreatment followed by a stimulation by EGF at 30 ng/mL for 5 minutes. Cell lysates were analyzed for phospho-EGFR (pEGFR) by ELISA. Data are expressed as mean ± SD, n = 2 patient donors. (B) EGF receptor tyrosine kinase inhibitor erlotinib inhibits TSH-induced upregulation of TG, TPO, DIO2, NIS, and TSHR mRNAs. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Erlotinib was then added at 5 µM alone or in combination with 1 mU/mL TSH for 48 hours. Cell lysates were analyzed for TG, TPO, DIO2, NIS, and TSHR mRNAs by RT-qPCR. Each experiment contained biological duplicates. Data are expressed as mean ± SEM, n = 3 patient donors.

Article Snippet: Human Phospho-EGFR DuoSet IC enzyme-linked immunosorbent assay (ELISA) (Cat # DYC1095B, RRID:AB_2922827), Human Total EGFR DuoSet IC ELISA (Cat # DYC1854, RRID:AB_2922828), EGF Quantikine ELISA (Cat # DEG00, RRID:AB_2922829), Human/Mouse/Rat Phospho-AKT (protein kinase B) (S473), and Pan Specific DuoSet IC ELISA (Cat # DYC887B, RRID:AB_292282) were purchased from R&D Systems (Minneapolis, MN).

Techniques: Phospho-proteomics, Enzyme-linked Immunosorbent Assay, Quantitative RT-PCR

EGFR-blocking antibodies cetuximab and panitumumab inhibit EGF-stimulated phospho-EGFR but have no effect on TSH regulation of TG, TPO, DIO2, NIS, and TSHR mRNAs (EGFR transactivation). (A) EGFR-blocking antibodies inhibit phospho-EGFR levels stimulated by EGF in thyrocytes. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Cetuximab and panitumumab were then added at the indicated doses for a 20-minute pretreatment followed by a stimulation by EGF at 30 ng/mL for 5 minutes. Cell lysates were analyzed for pEGFR by ELISA. Data are expressed as mean ± SD, n = 2 patient donors. (B) Cetuximab and panitumumab have no effect on TSH-mediated upregulation of thyroid gene mRNAs. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Cetuximab or panitumumab were then added at 10 µM alone or in combination with 1 mU/mL TSH for 48 hours. Cell lysates were analyzed for TG, TPO, DIO2, NIS, and TSHR mRNAs by RT-qPCR. Each experiment contained biological duplicates. Data are expressed as mean ± SEM, n = 3 patient donors.

Journal: Endocrinology

Article Title: Opposing Effects of EGF Receptor Signaling on Proliferation and Differentiation Initiated by EGF or TSH/EGF Receptor Transactivation

doi: 10.1210/endocr/bqac136

Figure Lengend Snippet: EGFR-blocking antibodies cetuximab and panitumumab inhibit EGF-stimulated phospho-EGFR but have no effect on TSH regulation of TG, TPO, DIO2, NIS, and TSHR mRNAs (EGFR transactivation). (A) EGFR-blocking antibodies inhibit phospho-EGFR levels stimulated by EGF in thyrocytes. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Cetuximab and panitumumab were then added at the indicated doses for a 20-minute pretreatment followed by a stimulation by EGF at 30 ng/mL for 5 minutes. Cell lysates were analyzed for pEGFR by ELISA. Data are expressed as mean ± SD, n = 2 patient donors. (B) Cetuximab and panitumumab have no effect on TSH-mediated upregulation of thyroid gene mRNAs. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Cetuximab or panitumumab were then added at 10 µM alone or in combination with 1 mU/mL TSH for 48 hours. Cell lysates were analyzed for TG, TPO, DIO2, NIS, and TSHR mRNAs by RT-qPCR. Each experiment contained biological duplicates. Data are expressed as mean ± SEM, n = 3 patient donors.

Techniques: Blocking Assay, Enzyme-linked Immunosorbent Assay, Quantitative RT-PCR

TSH, unlike EGF, does not stimulate phosphorylation nor downregulation of EGFR. (A) TSH, unlike EGF, does not lead to EGFR phosphorylation. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Cells were then stimulated by TSH (1 or 100 mU/mL) or EGF (1 or 100 ng/mL) for 5 minutes. Cell lysates were analyzed for phospho-EGFR by ELISA. The difference between groups was analyzed using unpaired Student’s t-test. The differences between basal (untreated) wells and 1 and 100 mU/mL TSH-treated wells were not statistically significant. Basal vs EGF 1 ng/mL and 100 ng/mL were highly significant (P < .0001 for both conditions). Each experiment contained biological duplicates. Data are expressed as mean ± SEM, n = 3 patient donors. (B) TSH, unlike EGF, does not cause downregulation of EGFR. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Cells were then stimulated by TSH (1 or 100 mU/mL) or EGF (1 or 100 ng/mL) for 48 hours. Cell lysates were analyzed for total EGFR by ELISA. The difference between groups was analyzed using unpaired Student’s t-test. The differences between basal (untreated) wells and 1 or 100 mU/mL TSH-treated wells were not statistically significant. Basal vs EGF 1 ng/mL and 100 ng/mL were significant (P < .0120 and 0.0082, respectively). Each experiment contained biological duplicates. Data are expressed as mean ± SEM, n = 3 patient donors.

Journal: Endocrinology

Article Title: Opposing Effects of EGF Receptor Signaling on Proliferation and Differentiation Initiated by EGF or TSH/EGF Receptor Transactivation

doi: 10.1210/endocr/bqac136

Figure Lengend Snippet: TSH, unlike EGF, does not stimulate phosphorylation nor downregulation of EGFR. (A) TSH, unlike EGF, does not lead to EGFR phosphorylation. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Cells were then stimulated by TSH (1 or 100 mU/mL) or EGF (1 or 100 ng/mL) for 5 minutes. Cell lysates were analyzed for phospho-EGFR by ELISA. The difference between groups was analyzed using unpaired Student’s t-test. The differences between basal (untreated) wells and 1 and 100 mU/mL TSH-treated wells were not statistically significant. Basal vs EGF 1 ng/mL and 100 ng/mL were highly significant (P < .0001 for both conditions). Each experiment contained biological duplicates. Data are expressed as mean ± SEM, n = 3 patient donors. (B) TSH, unlike EGF, does not cause downregulation of EGFR. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. Cells were then stimulated by TSH (1 or 100 mU/mL) or EGF (1 or 100 ng/mL) for 48 hours. Cell lysates were analyzed for total EGFR by ELISA. The difference between groups was analyzed using unpaired Student’s t-test. The differences between basal (untreated) wells and 1 or 100 mU/mL TSH-treated wells were not statistically significant. Basal vs EGF 1 ng/mL and 100 ng/mL were significant (P < .0120 and 0.0082, respectively). Each experiment contained biological duplicates. Data are expressed as mean ± SEM, n = 3 patient donors.

Techniques: Phospho-proteomics, Enzyme-linked Immunosorbent Assay

TSH stimulates phospho-AKT formation in an EGFR-dependent manner, and TSH and EGF synergistically stimulate phospho-AKT formation. (A) EGFR kinase inhibitor AG1478 inhibits TSH-mediated AKT phosphorylation. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. AG1478 (5 µM) was added for a 20-minute pretreatment followed by a stimulation by TSH (1 or 100 mU/mL) for 10 minutes. Cell lysates were analyzed for phospho-AKT by ELISA. The difference between groups was analyzed using unpaired Student’s t-test. The differences between DMSO basal (untreated) wells and 1 and 100 mU/mL TSH-treated wells were highly statistically significant (P < .0001 for both conditions). AG1478-treated Basal vs TSH 1 mU/mL was not significant. For AG1478-treated Basal vs TSH 100 mU/mL P = .0160. The difference between Control DMSO- and AG1478-treated cells was insignificant: P = .6356. Each experiment contained biological duplicates or triplicates. Data are expressed as mean ± SEM, n = 3 patient donors. (B) TSH and EGF synergistically potentiate AKT phosphorylation. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested overnight in 0.1% BSA-containing DMEM. Cells were stimulated by EGF (100 ng/mL) or TSH (1 mU/mL) or both for 10 minutes. Cell lysates were analyzed for phospho-AKT by ELISA. The difference between groups was analyzed using unpaired Student’s t-test. The differences between basal (untreated) wells and 1 mU/mL TSH-treated wells as well as 100 ng/mL EGF-treated wells were statistically significant (P = .0229 and P < .0001, respectively). The difference between EGF and EGF + TSH was highly significant (P < .0007). Each experiment contained biological duplicates or triplicates. Data are expressed as mean ± SEM, n = 3 patient donors. The dotted line represents the additive level of phospho-AKT independently stimulated by TSH and EGF.

Journal: Endocrinology

Article Title: Opposing Effects of EGF Receptor Signaling on Proliferation and Differentiation Initiated by EGF or TSH/EGF Receptor Transactivation

doi: 10.1210/endocr/bqac136

Figure Lengend Snippet: TSH stimulates phospho-AKT formation in an EGFR-dependent manner, and TSH and EGF synergistically stimulate phospho-AKT formation. (A) EGFR kinase inhibitor AG1478 inhibits TSH-mediated AKT phosphorylation. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested in 0.1% BSA-containing DMEM for 24 hours. AG1478 (5 µM) was added for a 20-minute pretreatment followed by a stimulation by TSH (1 or 100 mU/mL) for 10 minutes. Cell lysates were analyzed for phospho-AKT by ELISA. The difference between groups was analyzed using unpaired Student’s t-test. The differences between DMSO basal (untreated) wells and 1 and 100 mU/mL TSH-treated wells were highly statistically significant (P < .0001 for both conditions). AG1478-treated Basal vs TSH 1 mU/mL was not significant. For AG1478-treated Basal vs TSH 100 mU/mL P = .0160. The difference between Control DMSO- and AG1478-treated cells was insignificant: P = .6356. Each experiment contained biological duplicates or triplicates. Data are expressed as mean ± SEM, n = 3 patient donors. (B) TSH and EGF synergistically potentiate AKT phosphorylation. Human thyrocytes were seeded at 1 × 105 cells per well, allowed to attach overnight, then arrested overnight in 0.1% BSA-containing DMEM. Cells were stimulated by EGF (100 ng/mL) or TSH (1 mU/mL) or both for 10 minutes. Cell lysates were analyzed for phospho-AKT by ELISA. The difference between groups was analyzed using unpaired Student’s t-test. The differences between basal (untreated) wells and 1 mU/mL TSH-treated wells as well as 100 ng/mL EGF-treated wells were statistically significant (P = .0229 and P < .0001, respectively). The difference between EGF and EGF + TSH was highly significant (P < .0007). Each experiment contained biological duplicates or triplicates. Data are expressed as mean ± SEM, n = 3 patient donors. The dotted line represents the additive level of phospho-AKT independently stimulated by TSH and EGF.

Techniques: Phospho-proteomics, Enzyme-linked Immunosorbent Assay, Control

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