phosphorylated p egfr tyr992 Search Results


phosphorylated p egfr tyr992  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc phosphorylated p egfr tyr992
<t>EGFR,</t> <t>p-EGFR</t> <t>(Tyr992),</t> SYK, EGF, and AREG protein expression in APL patient samples. (A) Western blotting analysis of EGFR, p-EGFR (Tyr992), SYK, and β-actin protein levels in CD34 + cells isolated from normal BM of one healthy adult volunteer and 10 representative primary APL samples collected at diagnosis. HeLa cells served as a positive control to assess EGFR and p-EGFR (Tyr992) expression, and MV4-11 cell extracts were used as a positive control for SYK expression. EGFR and p-EGFR (Tyr992) were detectable when exposed for 180 seconds (sec). (B) EGF levels in BM plasma samples from healthy donors (n=15) and APL patients at diagnosis (n=16). (C) Plasma AREG levels in BM from healthy donors (n=20) and APL patients at diagnosis (n=17). (**) p < 0.01 (Mann-Whitney U-test).
Phosphorylated P Egfr Tyr992, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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phosphorylated p egfr tyr845  (Cell Signaling Technology Inc)
94
Cell Signaling Technology Inc phosphorylated p egfr tyr845
<t>EGFR,</t> <t>p-EGFR</t> <t>(Tyr992),</t> SYK, EGF, and AREG protein expression in APL patient samples. (A) Western blotting analysis of EGFR, p-EGFR (Tyr992), SYK, and β-actin protein levels in CD34 + cells isolated from normal BM of one healthy adult volunteer and 10 representative primary APL samples collected at diagnosis. HeLa cells served as a positive control to assess EGFR and p-EGFR (Tyr992) expression, and MV4-11 cell extracts were used as a positive control for SYK expression. EGFR and p-EGFR (Tyr992) were detectable when exposed for 180 seconds (sec). (B) EGF levels in BM plasma samples from healthy donors (n=15) and APL patients at diagnosis (n=16). (C) Plasma AREG levels in BM from healthy donors (n=20) and APL patients at diagnosis (n=17). (**) p < 0.01 (Mann-Whitney U-test).
Phosphorylated P Egfr Tyr845, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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antibodies against total egfr  (Cell Signaling Technology Inc)
98
Cell Signaling Technology Inc antibodies against total egfr
<t>EGFR,</t> <t>p-EGFR</t> <t>(Tyr992),</t> SYK, EGF, and AREG protein expression in APL patient samples. (A) Western blotting analysis of EGFR, p-EGFR (Tyr992), SYK, and β-actin protein levels in CD34 + cells isolated from normal BM of one healthy adult volunteer and 10 representative primary APL samples collected at diagnosis. HeLa cells served as a positive control to assess EGFR and p-EGFR (Tyr992) expression, and MV4-11 cell extracts were used as a positive control for SYK expression. EGFR and p-EGFR (Tyr992) were detectable when exposed for 180 seconds (sec). (B) EGF levels in BM plasma samples from healthy donors (n=15) and APL patients at diagnosis (n=16). (C) Plasma AREG levels in BM from healthy donors (n=20) and APL patients at diagnosis (n=17). (**) p < 0.01 (Mann-Whitney U-test).
Antibodies Against Total Egfr, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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egfr antibody 4267  (Cell Signaling Technology Inc)
90
Cell Signaling Technology Inc egfr antibody 4267
<t>EGFR,</t> <t>p-EGFR</t> <t>(Tyr992),</t> SYK, EGF, and AREG protein expression in APL patient samples. (A) Western blotting analysis of EGFR, p-EGFR (Tyr992), SYK, and β-actin protein levels in CD34 + cells isolated from normal BM of one healthy adult volunteer and 10 representative primary APL samples collected at diagnosis. HeLa cells served as a positive control to assess EGFR and p-EGFR (Tyr992) expression, and MV4-11 cell extracts were used as a positive control for SYK expression. EGFR and p-EGFR (Tyr992) were detectable when exposed for 180 seconds (sec). (B) EGF levels in BM plasma samples from healthy donors (n=15) and APL patients at diagnosis (n=16). (C) Plasma AREG levels in BM from healthy donors (n=20) and APL patients at diagnosis (n=17). (**) p < 0.01 (Mann-Whitney U-test).
Egfr Antibody 4267, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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antibodies against egfr  (Cell Signaling Technology Inc)
98
Cell Signaling Technology Inc antibodies against egfr
<t>EGFR,</t> <t>p-EGFR</t> <t>(Tyr992),</t> SYK, EGF, and AREG protein expression in APL patient samples. (A) Western blotting analysis of EGFR, p-EGFR (Tyr992), SYK, and β-actin protein levels in CD34 + cells isolated from normal BM of one healthy adult volunteer and 10 representative primary APL samples collected at diagnosis. HeLa cells served as a positive control to assess EGFR and p-EGFR (Tyr992) expression, and MV4-11 cell extracts were used as a positive control for SYK expression. EGFR and p-EGFR (Tyr992) were detectable when exposed for 180 seconds (sec). (B) EGF levels in BM plasma samples from healthy donors (n=15) and APL patients at diagnosis (n=16). (C) Plasma AREG levels in BM from healthy donors (n=20) and APL patients at diagnosis (n=17). (**) p < 0.01 (Mann-Whitney U-test).
Antibodies Against Egfr, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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tyr1068  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc tyr1068
<t>EGFR,</t> <t>p-EGFR</t> <t>(Tyr992),</t> SYK, EGF, and AREG protein expression in APL patient samples. (A) Western blotting analysis of EGFR, p-EGFR (Tyr992), SYK, and β-actin protein levels in CD34 + cells isolated from normal BM of one healthy adult volunteer and 10 representative primary APL samples collected at diagnosis. HeLa cells served as a positive control to assess EGFR and p-EGFR (Tyr992) expression, and MV4-11 cell extracts were used as a positive control for SYK expression. EGFR and p-EGFR (Tyr992) were detectable when exposed for 180 seconds (sec). (B) EGF levels in BM plasma samples from healthy donors (n=15) and APL patients at diagnosis (n=16). (C) Plasma AREG levels in BM from healthy donors (n=20) and APL patients at diagnosis (n=17). (**) p < 0.01 (Mann-Whitney U-test).
Tyr1068, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti-gm3 igm (cat. no. 303-06541; 1:200)  (FUJIFILM)
90
FUJIFILM anti-gm3 igm (cat. no. 303-06541; 1:200)
<t>EGFR,</t> <t>p-EGFR</t> <t>(Tyr992),</t> SYK, EGF, and AREG protein expression in APL patient samples. (A) Western blotting analysis of EGFR, p-EGFR (Tyr992), SYK, and β-actin protein levels in CD34 + cells isolated from normal BM of one healthy adult volunteer and 10 representative primary APL samples collected at diagnosis. HeLa cells served as a positive control to assess EGFR and p-EGFR (Tyr992) expression, and MV4-11 cell extracts were used as a positive control for SYK expression. EGFR and p-EGFR (Tyr992) were detectable when exposed for 180 seconds (sec). (B) EGF levels in BM plasma samples from healthy donors (n=15) and APL patients at diagnosis (n=16). (C) Plasma AREG levels in BM from healthy donors (n=20) and APL patients at diagnosis (n=17). (**) p < 0.01 (Mann-Whitney U-test).
Anti Gm3 Igm (Cat. No. 303 06541; 1:200), supplied by FUJIFILM, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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gapdh antibody  (Cell Signaling Technology Inc)
99
Cell Signaling Technology Inc gapdh antibody
Migfilin up-regulates the expression of EGFR and forms a complex with EGFR in glioma cells. A, panel a, expression of EGFR was analyzed by Western blotting in Migfilin-transfected and Migfilin siRNA-transfected cells. Protein expression levels were normalized with actin. A, panel b, bar chart shows the relative expression of EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus FLAG or Control-siRNA. B, quantification of changes of EGFR mRNA levels in Migfilin-transfected and Migfilin siRNA-transfected cells. mRNA expression levels were normalized with <t>GAPDH.</t> *, p < 0.05 versus FLAG or Control-siRNA. C, panels a and b, immunoprecipitation of Migfilin and EGFR. Lysates of human U-87 MG cells were mixed with rabbit anti-EGFR antibody ( panel a ) or mouse anti-Migfilin mAb ( panel b ). The immunoprecipitates or the control precipitates were analyzed by Western blotting with anti-Migfilin and EGFR antibodies, respectively. Panel c, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin fusion protein or GST. GST-Migfilin and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. D, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin mutant fusion proteins or GST. GST-Migfilin mutant fusion proteins and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. E, panel a, ectopic expression of mutant Migfilin in U-87 MG cells lines was analyzed by Western blotting using <t>an</t> <t>anti-GFP</t> antibody; The expression of EGFR was analyzed by Western blotting in U-87 MG cells transfected Migfilin mutant plasmids. Protein expression levels were normalized with actin; panel b, bar chart shows the relative expression of GFP and EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus GFP.
Gapdh Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pplc γ1  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc pplc γ1
Migfilin up-regulates the expression of EGFR and forms a complex with EGFR in glioma cells. A, panel a, expression of EGFR was analyzed by Western blotting in Migfilin-transfected and Migfilin siRNA-transfected cells. Protein expression levels were normalized with actin. A, panel b, bar chart shows the relative expression of EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus FLAG or Control-siRNA. B, quantification of changes of EGFR mRNA levels in Migfilin-transfected and Migfilin siRNA-transfected cells. mRNA expression levels were normalized with <t>GAPDH.</t> *, p < 0.05 versus FLAG or Control-siRNA. C, panels a and b, immunoprecipitation of Migfilin and EGFR. Lysates of human U-87 MG cells were mixed with rabbit anti-EGFR antibody ( panel a ) or mouse anti-Migfilin mAb ( panel b ). The immunoprecipitates or the control precipitates were analyzed by Western blotting with anti-Migfilin and EGFR antibodies, respectively. Panel c, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin fusion protein or GST. GST-Migfilin and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. D, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin mutant fusion proteins or GST. GST-Migfilin mutant fusion proteins and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. E, panel a, ectopic expression of mutant Migfilin in U-87 MG cells lines was analyzed by Western blotting using <t>an</t> <t>anti-GFP</t> antibody; The expression of EGFR was analyzed by Western blotting in U-87 MG cells transfected Migfilin mutant plasmids. Protein expression levels were normalized with actin; panel b, bar chart shows the relative expression of GFP and EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus GFP.
Pplc γ1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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plc 1 antibody  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc plc 1 antibody
Migfilin up-regulates the expression of EGFR and forms a complex with EGFR in glioma cells. A, panel a, expression of EGFR was analyzed by Western blotting in Migfilin-transfected and Migfilin siRNA-transfected cells. Protein expression levels were normalized with actin. A, panel b, bar chart shows the relative expression of EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus FLAG or Control-siRNA. B, quantification of changes of EGFR mRNA levels in Migfilin-transfected and Migfilin siRNA-transfected cells. mRNA expression levels were normalized with <t>GAPDH.</t> *, p < 0.05 versus FLAG or Control-siRNA. C, panels a and b, immunoprecipitation of Migfilin and EGFR. Lysates of human U-87 MG cells were mixed with rabbit anti-EGFR antibody ( panel a ) or mouse anti-Migfilin mAb ( panel b ). The immunoprecipitates or the control precipitates were analyzed by Western blotting with anti-Migfilin and EGFR antibodies, respectively. Panel c, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin fusion protein or GST. GST-Migfilin and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. D, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin mutant fusion proteins or GST. GST-Migfilin mutant fusion proteins and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. E, panel a, ectopic expression of mutant Migfilin in U-87 MG cells lines was analyzed by Western blotting using <t>an</t> <t>anti-GFP</t> antibody; The expression of EGFR was analyzed by Western blotting in U-87 MG cells transfected Migfilin mutant plasmids. Protein expression levels were normalized with actin; panel b, bar chart shows the relative expression of GFP and EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus GFP.
Plc 1 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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actin antibody  (Cell Signaling Technology Inc)
99
Cell Signaling Technology Inc actin antibody
Migfilin up-regulates the expression of EGFR and forms a complex with EGFR in glioma cells. A, panel a, expression of EGFR was analyzed by Western blotting in Migfilin-transfected and Migfilin siRNA-transfected cells. Protein expression levels were normalized with actin. A, panel b, bar chart shows the relative expression of EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus FLAG or Control-siRNA. B, quantification of changes of EGFR mRNA levels in Migfilin-transfected and Migfilin siRNA-transfected cells. mRNA expression levels were normalized with <t>GAPDH.</t> *, p < 0.05 versus FLAG or Control-siRNA. C, panels a and b, immunoprecipitation of Migfilin and EGFR. Lysates of human U-87 MG cells were mixed with rabbit anti-EGFR antibody ( panel a ) or mouse anti-Migfilin mAb ( panel b ). The immunoprecipitates or the control precipitates were analyzed by Western blotting with anti-Migfilin and EGFR antibodies, respectively. Panel c, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin fusion protein or GST. GST-Migfilin and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. D, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin mutant fusion proteins or GST. GST-Migfilin mutant fusion proteins and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. E, panel a, ectopic expression of mutant Migfilin in U-87 MG cells lines was analyzed by Western blotting using <t>an</t> <t>anti-GFP</t> antibody; The expression of EGFR was analyzed by Western blotting in U-87 MG cells transfected Migfilin mutant plasmids. Protein expression levels were normalized with actin; panel b, bar chart shows the relative expression of GFP and EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus GFP.
Actin Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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actin antibody - by Bioz Stars, 2026-02
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akt  (Cell Signaling Technology Inc)
99
Cell Signaling Technology Inc akt
Migfilin up-regulates the expression of EGFR and forms a complex with EGFR in glioma cells. A, panel a, expression of EGFR was analyzed by Western blotting in Migfilin-transfected and Migfilin siRNA-transfected cells. Protein expression levels were normalized with actin. A, panel b, bar chart shows the relative expression of EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus FLAG or Control-siRNA. B, quantification of changes of EGFR mRNA levels in Migfilin-transfected and Migfilin siRNA-transfected cells. mRNA expression levels were normalized with <t>GAPDH.</t> *, p < 0.05 versus FLAG or Control-siRNA. C, panels a and b, immunoprecipitation of Migfilin and EGFR. Lysates of human U-87 MG cells were mixed with rabbit anti-EGFR antibody ( panel a ) or mouse anti-Migfilin mAb ( panel b ). The immunoprecipitates or the control precipitates were analyzed by Western blotting with anti-Migfilin and EGFR antibodies, respectively. Panel c, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin fusion protein or GST. GST-Migfilin and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. D, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin mutant fusion proteins or GST. GST-Migfilin mutant fusion proteins and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. E, panel a, ectopic expression of mutant Migfilin in U-87 MG cells lines was analyzed by Western blotting using <t>an</t> <t>anti-GFP</t> antibody; The expression of EGFR was analyzed by Western blotting in U-87 MG cells transfected Migfilin mutant plasmids. Protein expression levels were normalized with actin; panel b, bar chart shows the relative expression of GFP and EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus GFP.
Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


EGFR, p-EGFR (Tyr992), SYK, EGF, and AREG protein expression in APL patient samples. (A) Western blotting analysis of EGFR, p-EGFR (Tyr992), SYK, and β-actin protein levels in CD34 + cells isolated from normal BM of one healthy adult volunteer and 10 representative primary APL samples collected at diagnosis. HeLa cells served as a positive control to assess EGFR and p-EGFR (Tyr992) expression, and MV4-11 cell extracts were used as a positive control for SYK expression. EGFR and p-EGFR (Tyr992) were detectable when exposed for 180 seconds (sec). (B) EGF levels in BM plasma samples from healthy donors (n=15) and APL patients at diagnosis (n=16). (C) Plasma AREG levels in BM from healthy donors (n=20) and APL patients at diagnosis (n=17). (**) p < 0.01 (Mann-Whitney U-test).

Journal: Frontiers in Oncology

Article Title: The Combination of Gefitinib With ATRA and ATO Induces Myeloid Differentiation in Acute Promyelocytic Leukemia Resistant Cells

doi: 10.3389/fonc.2021.686445

Figure Lengend Snippet: EGFR, p-EGFR (Tyr992), SYK, EGF, and AREG protein expression in APL patient samples. (A) Western blotting analysis of EGFR, p-EGFR (Tyr992), SYK, and β-actin protein levels in CD34 + cells isolated from normal BM of one healthy adult volunteer and 10 representative primary APL samples collected at diagnosis. HeLa cells served as a positive control to assess EGFR and p-EGFR (Tyr992) expression, and MV4-11 cell extracts were used as a positive control for SYK expression. EGFR and p-EGFR (Tyr992) were detectable when exposed for 180 seconds (sec). (B) EGF levels in BM plasma samples from healthy donors (n=15) and APL patients at diagnosis (n=16). (C) Plasma AREG levels in BM from healthy donors (n=20) and APL patients at diagnosis (n=17). (**) p < 0.01 (Mann-Whitney U-test).

Article Snippet: The proteins were transferred to a polyvinylidene difluoride membrane (Amersham Hybond-P; GE Healthcare, Memphis, TN, USA) that was probed with antibodies against total EGFR (#2232, polyclonal, 1:1000) and phosphorylated (p-)EGFR (Tyr992) (#2235, polyclonal, 1:1000) (both from Cell Signaling Technology, Danvers, MA, USA); SYK (#1240, clone: 4D10, 1:1000; Santa Cruz Biotechnology, Santa Cruz, CA, USA); and β-actin (#A5441, clone: AC-15, 1:60 000; Sigma-Aldrich).

Techniques: Expressing, Western Blot, Isolation, Biomarker Discovery, Positive Control, Clinical Proteomics, MANN-WHITNEY

EGFR, p-EGFR (Tyr992), SYK, EGF, and AREG protein expression in APL patient samples. (A) Western blotting analysis of EGFR, p-EGFR (Tyr992), SYK, and β-actin protein levels in CD34 + cells isolated from normal BM of one healthy adult volunteer and 10 representative primary APL samples collected at diagnosis. HeLa cells served as a positive control to assess EGFR and p-EGFR (Tyr992) expression, and MV4-11 cell extracts were used as a positive control for SYK expression. EGFR and p-EGFR (Tyr992) were detectable when exposed for 180 seconds (sec). (B) EGF levels in BM plasma samples from healthy donors (n=15) and APL patients at diagnosis (n=16). (C) Plasma AREG levels in BM from healthy donors (n=20) and APL patients at diagnosis (n=17). (**) p < 0.01 (Mann-Whitney U-test).

Journal: Frontiers in Oncology

Article Title: The Combination of Gefitinib With ATRA and ATO Induces Myeloid Differentiation in Acute Promyelocytic Leukemia Resistant Cells

doi: 10.3389/fonc.2021.686445

Figure Lengend Snippet: EGFR, p-EGFR (Tyr992), SYK, EGF, and AREG protein expression in APL patient samples. (A) Western blotting analysis of EGFR, p-EGFR (Tyr992), SYK, and β-actin protein levels in CD34 + cells isolated from normal BM of one healthy adult volunteer and 10 representative primary APL samples collected at diagnosis. HeLa cells served as a positive control to assess EGFR and p-EGFR (Tyr992) expression, and MV4-11 cell extracts were used as a positive control for SYK expression. EGFR and p-EGFR (Tyr992) were detectable when exposed for 180 seconds (sec). (B) EGF levels in BM plasma samples from healthy donors (n=15) and APL patients at diagnosis (n=16). (C) Plasma AREG levels in BM from healthy donors (n=20) and APL patients at diagnosis (n=17). (**) p < 0.01 (Mann-Whitney U-test).

Article Snippet: The proteins were transferred to a polyvinylidene difluoride membrane (Amersham Hybond-P; GE Healthcare, Memphis, TN, USA) that was probed with antibodies against total EGFR (#2232, polyclonal, 1:1000) and phosphorylated (p-)EGFR (Tyr992) (#2235, polyclonal, 1:1000) (both from Cell Signaling Technology, Danvers, MA, USA); SYK (#1240, clone: 4D10, 1:1000; Santa Cruz Biotechnology, Santa Cruz, CA, USA); and β-actin (#A5441, clone: AC-15, 1:60 000; Sigma-Aldrich).

Techniques: Expressing, Western Blot, Isolation, Biomarker Discovery, Positive Control, Clinical Proteomics, MANN-WHITNEY

Migfilin up-regulates the expression of EGFR and forms a complex with EGFR in glioma cells. A, panel a, expression of EGFR was analyzed by Western blotting in Migfilin-transfected and Migfilin siRNA-transfected cells. Protein expression levels were normalized with actin. A, panel b, bar chart shows the relative expression of EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus FLAG or Control-siRNA. B, quantification of changes of EGFR mRNA levels in Migfilin-transfected and Migfilin siRNA-transfected cells. mRNA expression levels were normalized with GAPDH. *, p < 0.05 versus FLAG or Control-siRNA. C, panels a and b, immunoprecipitation of Migfilin and EGFR. Lysates of human U-87 MG cells were mixed with rabbit anti-EGFR antibody ( panel a ) or mouse anti-Migfilin mAb ( panel b ). The immunoprecipitates or the control precipitates were analyzed by Western blotting with anti-Migfilin and EGFR antibodies, respectively. Panel c, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin fusion protein or GST. GST-Migfilin and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. D, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin mutant fusion proteins or GST. GST-Migfilin mutant fusion proteins and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. E, panel a, ectopic expression of mutant Migfilin in U-87 MG cells lines was analyzed by Western blotting using an anti-GFP antibody; The expression of EGFR was analyzed by Western blotting in U-87 MG cells transfected Migfilin mutant plasmids. Protein expression levels were normalized with actin; panel b, bar chart shows the relative expression of GFP and EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus GFP.

Journal: The Journal of Biological Chemistry

Article Title: Migfilin Protein Promotes Migration and Invasion in Human Glioma through Epidermal Growth Factor Receptor-mediated Phospholipase C-γ and STAT3 Protein Signaling Pathways *

doi: 10.1074/jbc.M112.393900

Figure Lengend Snippet: Migfilin up-regulates the expression of EGFR and forms a complex with EGFR in glioma cells. A, panel a, expression of EGFR was analyzed by Western blotting in Migfilin-transfected and Migfilin siRNA-transfected cells. Protein expression levels were normalized with actin. A, panel b, bar chart shows the relative expression of EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus FLAG or Control-siRNA. B, quantification of changes of EGFR mRNA levels in Migfilin-transfected and Migfilin siRNA-transfected cells. mRNA expression levels were normalized with GAPDH. *, p < 0.05 versus FLAG or Control-siRNA. C, panels a and b, immunoprecipitation of Migfilin and EGFR. Lysates of human U-87 MG cells were mixed with rabbit anti-EGFR antibody ( panel a ) or mouse anti-Migfilin mAb ( panel b ). The immunoprecipitates or the control precipitates were analyzed by Western blotting with anti-Migfilin and EGFR antibodies, respectively. Panel c, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin fusion protein or GST. GST-Migfilin and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. D, GST fusion protein pulldown assay. Human U-87 MG cell lysates were incubated with GST-Migfilin mutant fusion proteins or GST. GST-Migfilin mutant fusion proteins and GST were precipitated with glutathione beads. EGFR was detected by Western blotting with an anti-EGFR mAb. E, panel a, ectopic expression of mutant Migfilin in U-87 MG cells lines was analyzed by Western blotting using an anti-GFP antibody; The expression of EGFR was analyzed by Western blotting in U-87 MG cells transfected Migfilin mutant plasmids. Protein expression levels were normalized with actin; panel b, bar chart shows the relative expression of GFP and EGFR. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus GFP.

Article Snippet: EGFR antibody (4267), phosphorylated (p) EGFR (pEGFR) antibodies (Tyr-1173, Tyr-845, Tyr-1068, Tyr-1148, Tyr-992, and Ser-1046/1047), protein kinase B (Akt) antibody (2920S), pAkt (serine 473) antibody (4060S), STAT3 antibody (9139S), pSTAT3 (Thr-705) antibody (9145S), extracellular signal-regulated kinases 1/2 (ERK1/2) antibody (9102S), pERK1/2 (threonine 202/tyrosine 204) antibody (4370S), PLC-γ1 antibody (5690S), pPLC-γ1 (tyrosine 783) antibody (2821S), GFP antibody (2956), GAPDH antibody (2118), and β-actin antibody (4970) were purchased from Cell Signaling Technology, Inc. Anti-Migfilin antibody was a kind gift from Dr. Cary Wu (University of Pittsburgh).

Techniques: Expressing, Western Blot, Transfection, Control, Immunoprecipitation, Incubation, Mutagenesis

C-terminal region is essential for Migfilin regulation of the EGFR phosphorylation. A, panel a, endogenous phosphorylation of EGFR was analyzed by Western blotting using anti-pEGFR antibodies in Migfilin-transfected and Migfilin siRNA-transfected cells. Protein expression levels were normalized with GAPDH; A, panel b, bar chart shows the relative expression of proteins. *, p < 0.05 versus FLAG or control-siRNA. B, panel a, ectopic expression of mutant Migfilin in U-87 MG cells lines was analyzed by Western blotting using an anti-GFP antibody ( top panel ). The expression of Tyr-1173 phosphorylation of EGFR was analyzed by Western blotting in U-87 MG cells transfected with Migfilin mutant plasmids ( bottom panel ). Protein expression levels were normalized with GAPDH; B, panel b, bar chart shows the relative expression of proteins. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the GAPDH internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus GFP.

Journal: The Journal of Biological Chemistry

Article Title: Migfilin Protein Promotes Migration and Invasion in Human Glioma through Epidermal Growth Factor Receptor-mediated Phospholipase C-γ and STAT3 Protein Signaling Pathways *

doi: 10.1074/jbc.M112.393900

Figure Lengend Snippet: C-terminal region is essential for Migfilin regulation of the EGFR phosphorylation. A, panel a, endogenous phosphorylation of EGFR was analyzed by Western blotting using anti-pEGFR antibodies in Migfilin-transfected and Migfilin siRNA-transfected cells. Protein expression levels were normalized with GAPDH; A, panel b, bar chart shows the relative expression of proteins. *, p < 0.05 versus FLAG or control-siRNA. B, panel a, ectopic expression of mutant Migfilin in U-87 MG cells lines was analyzed by Western blotting using an anti-GFP antibody ( top panel ). The expression of Tyr-1173 phosphorylation of EGFR was analyzed by Western blotting in U-87 MG cells transfected with Migfilin mutant plasmids ( bottom panel ). Protein expression levels were normalized with GAPDH; B, panel b, bar chart shows the relative expression of proteins. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the GAPDH internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus GFP.

Article Snippet: EGFR antibody (4267), phosphorylated (p) EGFR (pEGFR) antibodies (Tyr-1173, Tyr-845, Tyr-1068, Tyr-1148, Tyr-992, and Ser-1046/1047), protein kinase B (Akt) antibody (2920S), pAkt (serine 473) antibody (4060S), STAT3 antibody (9139S), pSTAT3 (Thr-705) antibody (9145S), extracellular signal-regulated kinases 1/2 (ERK1/2) antibody (9102S), pERK1/2 (threonine 202/tyrosine 204) antibody (4370S), PLC-γ1 antibody (5690S), pPLC-γ1 (tyrosine 783) antibody (2821S), GFP antibody (2956), GAPDH antibody (2118), and β-actin antibody (4970) were purchased from Cell Signaling Technology, Inc. Anti-Migfilin antibody was a kind gift from Dr. Cary Wu (University of Pittsburgh).

Techniques: Phospho-proteomics, Western Blot, Transfection, Expressing, Control, Mutagenesis

C-terminal region is essential for Migfilin regulation of EGFR-mediated PLC-γ and STAT3-signaling pathways in glioma cells. A, panel a, Western blotting analysis of endogenous ERK, PLC-γ1, STAT3, and AKT in Migfilin-transfected and Migfilin siRNA-transfected cells. Protein expression levels were normalized with GAPDH; A, panel b, bar chart shows the relative expression of proteins. *, p < 0.05 versus FLAG or control-siRNA. B, panel a, ectopic expression of mutant Migfilin in U-87 MG cells lines was analyzed by Western blotting using an anti-GFP antibody ( top panel ). The expression of PLC-γ1, p-PLC-γ1, STAT3, and p-STAT3 were analyzed by Western blotting in U-87 MG cells transfected with Migfilin mutant plasmids ( bottom panel ). Protein expression levels were normalized with GAPDH. B, panel b, bar chart shows the relative expression of proteins. *, p < 0.05 versus GFP. C, inhibitor of PLC-γ (U-73122) reduces the Migfilin-induced phosphorylation of PLC-γ, whereas inhibitor of STAT3 (cryptotanshinone) reduces the Migfilin-induced phosphorylation of STAT3. Migfilin-transfected cells were incubated with U-73122 (2 μmol/liter) for 30 min or cryptotanshinone (5 μmol/liter) for 24 h. Panels a, c, and e, Western blotting analysis of Migfilin, PLC-γ1, p-PLC-γ1, STAT3, and p-STAT3; and panels b, d, and f, bar chart shows the relative expression of proteins, and proteins expression levels were normalized with actin or GAPDH. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin or GAPDH internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus FLAG. D and E, effects of U-73122 and cryptotanshinone on Migfilin-mediated migration and invasion in glioma cells. Migfilin-transfected cells were incubated with U-73122 (2 μmol/liter) for 30 min or cryptotanshinone (5 μmol/liter) for 24 h. Representative pictures ( left panel ) and quantification ( right panel ) of penetrated cells were analyzed using the Transwell migrative or invasive assay. The quantification of penetrated cells was represented as the mean of three different experiments. *, p < 0.05 versus control.

Journal: The Journal of Biological Chemistry

Article Title: Migfilin Protein Promotes Migration and Invasion in Human Glioma through Epidermal Growth Factor Receptor-mediated Phospholipase C-γ and STAT3 Protein Signaling Pathways *

doi: 10.1074/jbc.M112.393900

Figure Lengend Snippet: C-terminal region is essential for Migfilin regulation of EGFR-mediated PLC-γ and STAT3-signaling pathways in glioma cells. A, panel a, Western blotting analysis of endogenous ERK, PLC-γ1, STAT3, and AKT in Migfilin-transfected and Migfilin siRNA-transfected cells. Protein expression levels were normalized with GAPDH; A, panel b, bar chart shows the relative expression of proteins. *, p < 0.05 versus FLAG or control-siRNA. B, panel a, ectopic expression of mutant Migfilin in U-87 MG cells lines was analyzed by Western blotting using an anti-GFP antibody ( top panel ). The expression of PLC-γ1, p-PLC-γ1, STAT3, and p-STAT3 were analyzed by Western blotting in U-87 MG cells transfected with Migfilin mutant plasmids ( bottom panel ). Protein expression levels were normalized with GAPDH. B, panel b, bar chart shows the relative expression of proteins. *, p < 0.05 versus GFP. C, inhibitor of PLC-γ (U-73122) reduces the Migfilin-induced phosphorylation of PLC-γ, whereas inhibitor of STAT3 (cryptotanshinone) reduces the Migfilin-induced phosphorylation of STAT3. Migfilin-transfected cells were incubated with U-73122 (2 μmol/liter) for 30 min or cryptotanshinone (5 μmol/liter) for 24 h. Panels a, c, and e, Western blotting analysis of Migfilin, PLC-γ1, p-PLC-γ1, STAT3, and p-STAT3; and panels b, d, and f, bar chart shows the relative expression of proteins, and proteins expression levels were normalized with actin or GAPDH. Protein quantification was obtained by densitometric analysis of the protein absorbance × resulting band area. Protein quantified was relative to the actin or GAPDH internal control. All experiments were performed at least three times with consistent and repeatable results. Each value is expressed as mean ± S.D. ( n = 3). *, p < 0.05 versus FLAG. D and E, effects of U-73122 and cryptotanshinone on Migfilin-mediated migration and invasion in glioma cells. Migfilin-transfected cells were incubated with U-73122 (2 μmol/liter) for 30 min or cryptotanshinone (5 μmol/liter) for 24 h. Representative pictures ( left panel ) and quantification ( right panel ) of penetrated cells were analyzed using the Transwell migrative or invasive assay. The quantification of penetrated cells was represented as the mean of three different experiments. *, p < 0.05 versus control.

Article Snippet: EGFR antibody (4267), phosphorylated (p) EGFR (pEGFR) antibodies (Tyr-1173, Tyr-845, Tyr-1068, Tyr-1148, Tyr-992, and Ser-1046/1047), protein kinase B (Akt) antibody (2920S), pAkt (serine 473) antibody (4060S), STAT3 antibody (9139S), pSTAT3 (Thr-705) antibody (9145S), extracellular signal-regulated kinases 1/2 (ERK1/2) antibody (9102S), pERK1/2 (threonine 202/tyrosine 204) antibody (4370S), PLC-γ1 antibody (5690S), pPLC-γ1 (tyrosine 783) antibody (2821S), GFP antibody (2956), GAPDH antibody (2118), and β-actin antibody (4970) were purchased from Cell Signaling Technology, Inc. Anti-Migfilin antibody was a kind gift from Dr. Cary Wu (University of Pittsburgh).

Techniques: Protein-Protein interactions, Western Blot, Transfection, Expressing, Control, Mutagenesis, Phospho-proteomics, Incubation, Migration