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selective erbb2 inhibitor  (Selleck Chemicals)


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    Selleck Chemicals selective erbb2 inhibitor
    Selective Erbb2 Inhibitor, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 96/100, based on 341 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/selective+erbb2+inhibitor/Lapatinib/us11933781-122-42-46
    Average 96 stars, based on 341 article reviews
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    Article Snippet: .. Inhibitors used and HBEC inhibitor treatment: The following compounds were utilized to assess modulation of cellular speed: Tyrphostin AG-1478 (Millipore Sigma, Burlington, MAT4182-5MG, 100 nM) and Erlotinib (Selleckchem, Houston, Texas, 57786, 100 nM) selective EGFR inhibitors; Mubritinib (Selleckchem, S2216, 100 nM) a selective ERBB2 inhibitor; Lapatinib (Selleckchem, Houston, Texas, S2111, 100 nM) an EGFR/ERBB2 dual inhibitor; OSU-03012 (Selleckchem, Houston, Texas, S1106, 1 μM) and GSK2334470 (Selleckchem, Houston, Texas, S7087, 1 μM) selective PDK1 inhibitor; LY294002 (Selleckchem, Houston, Texas, S1105, 5 μM) a selective PI3K inhibitor; MK-2206 (Selleckchem, Houston, Texas, S1078, 1 μM) a selective ATK1/2/3 inhibitor; Staltic (Selleckchem, Houston, Texas, S7024, 5 μM) a selective STAT3 inhibitor; Ruxolitinib (Selleckchem, Houston, Texas, S1378, 5 μM) a selective JAK1/2 inhibitor; Sotrastaurin (Selleckchem, Houston, Texas, S2791, 1 μM) a selective PKC inhibitor; Verteporfin (Tocris Bioscience, Bristol, UK, 5305, 1 μM) a selective YAP inhibitor; XMU-MP-1 (Tocris Bioscience, Bristol, UK, 6482, 1 μM) a selective MST1/2 inhibitor; SB431542 (Tocris Bioscience, Bristol, UK, 1614, 5 μM) a selective TGFBRI inhibitor; Amphiregulin neutralizing antibody (R&D Systems, Minneapolis, Minnesota, MAB262, 30 μg/ml), Recombinant AREG (R&D Systems, Minneapolis, Minnesota 262-AR), EGF (R&D Systems, Minneapolis, Minnesota 263-EG), and TGF-α (R&D Systems, Minneapolis, Minnesota, 239-A-100) EGFR agonists. ..



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    ( A , B ) Schematic representation of the ErbB signaling pathway. Ligands are all produced as membrane-bound precursor proteins that are cleaved by cell-surface sheddases to yield the active growth factor species. Binding of the soluble form of the ligand induces ErbB receptor homodimerization or heterodimerization, converting the receptor to an active dimeric conformation ( A ). Ligands are grouped in four rows according to their receptor specificity (top; arrows); the six ligands for which ectodomain shedding is primarily mediated by ADAM17 appear in black characters, and the remaining five are in grey characters ( B ). ( C – K ) Resting CBF ( C , F , I ) and CBF responses to whisker stimulation ( D , G , J ) or topical application of adenosine ( E , H , K ) were evaluated before and after superfusion of various inhibitors of the ErbB signaling pathway, including the ErbB1/ErbB4 inhibitor AG1478 (10 and 20 µM); the <t>ErbB2</t> inhibitor <t>AG825</t> (50 and 200 µM) ( C – E ), the soluble ErbB receptor traps (ErbB1-Fc, 66.7 nM; ErbB3-Fc, 71.4 nM; ErbB4-Fc, 71.4 nM) and the respective control IgG1-Fc and IgG2-Fc fragments (286 nM) ( F – H ), heparin and the synthetic peptide p21 (12 µM) and the control inactive peptide p21-mut (12 µM) ( I – K ). None of these compounds affected resting CBF, except ErbB4-Fc, which produced a slight increase. ( C – K ) Significance was determined by one-way ANOVA followed by Tukey’s post-hoc test (*p<0.05, **p<0.01, ***p<0.001 compared to vehicle; n = 5/group). Error bars indicate SEM. DOI: http://dx.doi.org/10.7554/eLife.17536.015 10.7554/eLife.17536.016 Figure 3—source data 1. Reagents used for . DOI: http://dx.doi.org/10.7554/eLife.17536.016 10.7554/eLife.17536.017 Figure 3—source data 2. Main physiological variables of mice studied in . DOI: http://dx.doi.org/10.7554/eLife.17536.017 10.7554/eLife.17536.018 Figure 3—source data 3. Numerical data that were used to generate the bar charts in . DOI: http://dx.doi.org/10.7554/eLife.17536.018
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    ( A , B ) Schematic representation of the ErbB signaling pathway. Ligands are all produced as membrane-bound precursor proteins that are cleaved by cell-surface sheddases to yield the active growth factor species. Binding of the soluble form of the ligand induces ErbB receptor homodimerization or heterodimerization, converting the receptor to an active dimeric conformation ( A ). Ligands are grouped in four rows according to their receptor specificity (top; arrows); the six ligands for which ectodomain shedding is primarily mediated by ADAM17 appear in black characters, and the remaining five are in grey characters ( B ). ( C – K ) Resting CBF ( C , F , I ) and CBF responses to whisker stimulation ( D , G , J ) or topical application of adenosine ( E , H , K ) were evaluated before and after superfusion of various inhibitors of the ErbB signaling pathway, including the ErbB1/ErbB4 inhibitor AG1478 (10 and 20 µM); the <t>ErbB2</t> inhibitor <t>AG825</t> (50 and 200 µM) ( C – E ), the soluble ErbB receptor traps (ErbB1-Fc, 66.7 nM; ErbB3-Fc, 71.4 nM; ErbB4-Fc, 71.4 nM) and the respective control IgG1-Fc and IgG2-Fc fragments (286 nM) ( F – H ), heparin and the synthetic peptide p21 (12 µM) and the control inactive peptide p21-mut (12 µM) ( I – K ). None of these compounds affected resting CBF, except ErbB4-Fc, which produced a slight increase. ( C – K ) Significance was determined by one-way ANOVA followed by Tukey’s post-hoc test (*p<0.05, **p<0.01, ***p<0.001 compared to vehicle; n = 5/group). Error bars indicate SEM. DOI: http://dx.doi.org/10.7554/eLife.17536.015 10.7554/eLife.17536.016 Figure 3—source data 1. Reagents used for . DOI: http://dx.doi.org/10.7554/eLife.17536.016 10.7554/eLife.17536.017 Figure 3—source data 2. Main physiological variables of mice studied in . DOI: http://dx.doi.org/10.7554/eLife.17536.017 10.7554/eLife.17536.018 Figure 3—source data 3. Numerical data that were used to generate the bar charts in . DOI: http://dx.doi.org/10.7554/eLife.17536.018
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    ( A , B ) Schematic representation of the ErbB signaling pathway. Ligands are all produced as membrane-bound precursor proteins that are cleaved by cell-surface sheddases to yield the active growth factor species. Binding of the soluble form of the ligand induces ErbB receptor homodimerization or heterodimerization, converting the receptor to an active dimeric conformation ( A ). Ligands are grouped in four rows according to their receptor specificity (top; arrows); the six ligands for which ectodomain shedding is primarily mediated by ADAM17 appear in black characters, and the remaining five are in grey characters ( B ). ( C – K ) Resting CBF ( C , F , I ) and CBF responses to whisker stimulation ( D , G , J ) or topical application of adenosine ( E , H , K ) were evaluated before and after superfusion of various inhibitors of the ErbB signaling pathway, including the ErbB1/ErbB4 inhibitor AG1478 (10 and 20 µM); the <t>ErbB2</t> inhibitor <t>AG825</t> (50 and 200 µM) ( C – E ), the soluble ErbB receptor traps (ErbB1-Fc, 66.7 nM; ErbB3-Fc, 71.4 nM; ErbB4-Fc, 71.4 nM) and the respective control IgG1-Fc and IgG2-Fc fragments (286 nM) ( F – H ), heparin and the synthetic peptide p21 (12 µM) and the control inactive peptide p21-mut (12 µM) ( I – K ). None of these compounds affected resting CBF, except ErbB4-Fc, which produced a slight increase. ( C – K ) Significance was determined by one-way ANOVA followed by Tukey’s post-hoc test (*p<0.05, **p<0.01, ***p<0.001 compared to vehicle; n = 5/group). Error bars indicate SEM. DOI: http://dx.doi.org/10.7554/eLife.17536.015 10.7554/eLife.17536.016 Figure 3—source data 1. Reagents used for . DOI: http://dx.doi.org/10.7554/eLife.17536.016 10.7554/eLife.17536.017 Figure 3—source data 2. Main physiological variables of mice studied in . DOI: http://dx.doi.org/10.7554/eLife.17536.017 10.7554/eLife.17536.018 Figure 3—source data 3. Numerical data that were used to generate the bar charts in . DOI: http://dx.doi.org/10.7554/eLife.17536.018
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    ( A , B ) Schematic representation of the ErbB signaling pathway. Ligands are all produced as membrane-bound precursor proteins that are cleaved by cell-surface sheddases to yield the active growth factor species. Binding of the soluble form of the ligand induces ErbB receptor homodimerization or heterodimerization, converting the receptor to an active dimeric conformation ( A ). Ligands are grouped in four rows according to their receptor specificity (top; arrows); the six ligands for which ectodomain shedding is primarily mediated by ADAM17 appear in black characters, and the remaining five are in grey characters ( B ). ( C – K ) Resting CBF ( C , F , I ) and CBF responses to whisker stimulation ( D , G , J ) or topical application of adenosine ( E , H , K ) were evaluated before and after superfusion of various inhibitors of the ErbB signaling pathway, including the ErbB1/ErbB4 inhibitor AG1478 (10 and 20 µM); the <t>ErbB2</t> inhibitor <t>AG825</t> (50 and 200 µM) ( C – E ), the soluble ErbB receptor traps (ErbB1-Fc, 66.7 nM; ErbB3-Fc, 71.4 nM; ErbB4-Fc, 71.4 nM) and the respective control IgG1-Fc and IgG2-Fc fragments (286 nM) ( F – H ), heparin and the synthetic peptide p21 (12 µM) and the control inactive peptide p21-mut (12 µM) ( I – K ). None of these compounds affected resting CBF, except ErbB4-Fc, which produced a slight increase. ( C – K ) Significance was determined by one-way ANOVA followed by Tukey’s post-hoc test (*p<0.05, **p<0.01, ***p<0.001 compared to vehicle; n = 5/group). Error bars indicate SEM. DOI: http://dx.doi.org/10.7554/eLife.17536.015 10.7554/eLife.17536.016 Figure 3—source data 1. Reagents used for . DOI: http://dx.doi.org/10.7554/eLife.17536.016 10.7554/eLife.17536.017 Figure 3—source data 2. Main physiological variables of mice studied in . DOI: http://dx.doi.org/10.7554/eLife.17536.017 10.7554/eLife.17536.018 Figure 3—source data 3. Numerical data that were used to generate the bar charts in . DOI: http://dx.doi.org/10.7554/eLife.17536.018
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    ( A , B ) Schematic representation of the ErbB signaling pathway. Ligands are all produced as membrane-bound precursor proteins that are cleaved by cell-surface sheddases to yield the active growth factor species. Binding of the soluble form of the ligand induces ErbB receptor homodimerization or heterodimerization, converting the receptor to an active dimeric conformation ( A ). Ligands are grouped in four rows according to their receptor specificity (top; arrows); the six ligands for which ectodomain shedding is primarily mediated by ADAM17 appear in black characters, and the remaining five are in grey characters ( B ). ( C – K ) Resting CBF ( C , F , I ) and CBF responses to whisker stimulation ( D , G , J ) or topical application of adenosine ( E , H , K ) were evaluated before and after superfusion of various inhibitors of the ErbB signaling pathway, including the ErbB1/ErbB4 inhibitor AG1478 (10 and 20 µM); the ErbB2 inhibitor AG825 (50 and 200 µM) ( C – E ), the soluble ErbB receptor traps (ErbB1-Fc, 66.7 nM; ErbB3-Fc, 71.4 nM; ErbB4-Fc, 71.4 nM) and the respective control IgG1-Fc and IgG2-Fc fragments (286 nM) ( F – H ), heparin and the synthetic peptide p21 (12 µM) and the control inactive peptide p21-mut (12 µM) ( I – K ). None of these compounds affected resting CBF, except ErbB4-Fc, which produced a slight increase. ( C – K ) Significance was determined by one-way ANOVA followed by Tukey’s post-hoc test (*p<0.05, **p<0.01, ***p<0.001 compared to vehicle; n = 5/group). Error bars indicate SEM. DOI: http://dx.doi.org/10.7554/eLife.17536.015 10.7554/eLife.17536.016 Figure 3—source data 1. Reagents used for . DOI: http://dx.doi.org/10.7554/eLife.17536.016 10.7554/eLife.17536.017 Figure 3—source data 2. Main physiological variables of mice studied in . DOI: http://dx.doi.org/10.7554/eLife.17536.017 10.7554/eLife.17536.018 Figure 3—source data 3. Numerical data that were used to generate the bar charts in . DOI: http://dx.doi.org/10.7554/eLife.17536.018

    Journal: eLife

    Article Title: Mechanistic insights into a TIMP3-sensitive pathway constitutively engaged in the regulation of cerebral hemodynamics

    doi: 10.7554/eLife.17536

    Figure Lengend Snippet: ( A , B ) Schematic representation of the ErbB signaling pathway. Ligands are all produced as membrane-bound precursor proteins that are cleaved by cell-surface sheddases to yield the active growth factor species. Binding of the soluble form of the ligand induces ErbB receptor homodimerization or heterodimerization, converting the receptor to an active dimeric conformation ( A ). Ligands are grouped in four rows according to their receptor specificity (top; arrows); the six ligands for which ectodomain shedding is primarily mediated by ADAM17 appear in black characters, and the remaining five are in grey characters ( B ). ( C – K ) Resting CBF ( C , F , I ) and CBF responses to whisker stimulation ( D , G , J ) or topical application of adenosine ( E , H , K ) were evaluated before and after superfusion of various inhibitors of the ErbB signaling pathway, including the ErbB1/ErbB4 inhibitor AG1478 (10 and 20 µM); the ErbB2 inhibitor AG825 (50 and 200 µM) ( C – E ), the soluble ErbB receptor traps (ErbB1-Fc, 66.7 nM; ErbB3-Fc, 71.4 nM; ErbB4-Fc, 71.4 nM) and the respective control IgG1-Fc and IgG2-Fc fragments (286 nM) ( F – H ), heparin and the synthetic peptide p21 (12 µM) and the control inactive peptide p21-mut (12 µM) ( I – K ). None of these compounds affected resting CBF, except ErbB4-Fc, which produced a slight increase. ( C – K ) Significance was determined by one-way ANOVA followed by Tukey’s post-hoc test (*p<0.05, **p<0.01, ***p<0.001 compared to vehicle; n = 5/group). Error bars indicate SEM. DOI: http://dx.doi.org/10.7554/eLife.17536.015 10.7554/eLife.17536.016 Figure 3—source data 1. Reagents used for . DOI: http://dx.doi.org/10.7554/eLife.17536.016 10.7554/eLife.17536.017 Figure 3—source data 2. Main physiological variables of mice studied in . DOI: http://dx.doi.org/10.7554/eLife.17536.017 10.7554/eLife.17536.018 Figure 3—source data 3. Numerical data that were used to generate the bar charts in . DOI: http://dx.doi.org/10.7554/eLife.17536.018

    Article Snippet: Acetylcholine, adenosine, the selective ErbB1/ErbB4 inhibitor tyrphostin AG1478, and the selective ErbB2 inhibitor tyrphostin AG825 ( ) were purchased from Sigma Aldrich (St. Louis, MO).

    Techniques: Produced, Binding Assay, Whisker Assay