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goat anti human erbb2 her2 antibody af1129 (R&D Systems)

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R&D Systems goat anti human erbb2 her2 antibody af1129
Goat Anti Human Erbb2 Her2 Antibody Af1129, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+human+erbb2+her2+antibody+af1129/Human+ErbB2%2FHer2+Antibody/pmc12737384-63-0-5
Average 93 stars, based on 34 article reviews

goat anti human erbb2 her2 antibody af1129 - by Bioz Stars, 2026-10

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Article Title: Switchable Retargeting of Lentiviral Vectors Through a VSV-G-Binding Adapter Molecule
Article Snippet: .. Goat anti-human ErbB2/Her2 antibody AF1129 (R&D Systems, Minneapolis, MN, USA) and mouse anti-goat IgG-CFL 555 (Santa Cruz Biotechnology, Dallas, TX, USA) were used for ERBB2 staining on breast cancer cell lines. .. For ERBB2 detection in cell mixtures, trastuzumab (Biocad, Moscow, Russia) conjugated with AlexaFluor 488 (Thermo, Waltham, MA, USA) was utilized.

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a ErbB2-positive breast cancer cells were treated with the HSP90 inhibitor 17-AAG (500 nM) for 4 h or left untreated (control) before immunofluorescence assays to examine ErbB2 localization. Images show representative confocal sections, with triangles pointing to intracellular ErbB2 punctae. Scale bar = 10 μm. b Cultured ErbB2-positive breast cancer cells were subjected to 17-AAG treatment at 500 nM for indicated times and lysed for immunoblotting using two clones of anti-ErbB2 antibodies. Tubulin was probed to show equal loading. Degradation curves show correlating quantification of relative ErbB2 intensities (0 h set as 100%). c SKBR3 cells were treated with 500 nM of 17-AAG for indicated times and harvested for flow cytometric analysis to examine surface levels of ErbB2. d SKBR3 cells were treated with 500 nM of 17-AAG for indicated times and lysed. ErbB2 proteins were immunoprecipitated using mouse anti-ErbB2 antibody (clone 9G6) and analyzed by immunoblotting with anti-ubiquitin antibody, with immunoblotting analysis of cell lysates performed in parallel to examine cellular levels of ErbB2 and Tubulin. e Cultured HeLa cells were treated with 20 ng/ml of EGF for indicated times and lysed. EGFR was immunoprecipitated from each sample and analyzed by immunoblotting with ubiquitin antibody to examine the ubiquitylation of EGFR. Cell lysates were also analyzed by immunoblotting to probe for EGFR and Tubulin. f Relative quantification data of ubiquitin signal after ErbB2 and EGFR normalization from ( d ) and ( e ), respectively. The samples showing highest intensities were considered as 100%, with 0.5 h and 1 h set for EGFR and ErbB2, respectively. All error bars represent standard error of the mean ( n = 3).

Journal: Cell Death and Differentiation

Article Title: The deubiquitylase USP2 maintains ErbB2 abundance via counteracting endocytic degradation and represents a therapeutic target in ErbB2-positive breast cancer

doi: 10.1038/s41418-020-0538-8

Figure Lengend Snippet: a ErbB2-positive breast cancer cells were treated with the HSP90 inhibitor 17-AAG (500 nM) for 4 h or left untreated (control) before immunofluorescence assays to examine ErbB2 localization. Images show representative confocal sections, with triangles pointing to intracellular ErbB2 punctae. Scale bar = 10 μm. b Cultured ErbB2-positive breast cancer cells were subjected to 17-AAG treatment at 500 nM for indicated times and lysed for immunoblotting using two clones of anti-ErbB2 antibodies. Tubulin was probed to show equal loading. Degradation curves show correlating quantification of relative ErbB2 intensities (0 h set as 100%). c SKBR3 cells were treated with 500 nM of 17-AAG for indicated times and harvested for flow cytometric analysis to examine surface levels of ErbB2. d SKBR3 cells were treated with 500 nM of 17-AAG for indicated times and lysed. ErbB2 proteins were immunoprecipitated using mouse anti-ErbB2 antibody (clone 9G6) and analyzed by immunoblotting with anti-ubiquitin antibody, with immunoblotting analysis of cell lysates performed in parallel to examine cellular levels of ErbB2 and Tubulin. e Cultured HeLa cells were treated with 20 ng/ml of EGF for indicated times and lysed. EGFR was immunoprecipitated from each sample and analyzed by immunoblotting with ubiquitin antibody to examine the ubiquitylation of EGFR. Cell lysates were also analyzed by immunoblotting to probe for EGFR and Tubulin. f Relative quantification data of ubiquitin signal after ErbB2 and EGFR normalization from ( d ) and ( e ), respectively. The samples showing highest intensities were considered as 100%, with 0.5 h and 1 h set for EGFR and ErbB2, respectively. All error bars represent standard error of the mean ( n = 3).

Article Snippet: Goat anti-ErbB2 (AF1129) antibody was obtained from R&D systems.

Techniques: Control, Immunofluorescence, Cell Culture, Western Blot, Clone Assay, Immunoprecipitation, Ubiquitin Proteomics, Quantitative Proteomics

a b SKBR3 and HCC1954 cells were treated with 17-AAG at 500 nM for 4 h, before processed for immunofluorescence assays along with untreated control cells. Cells were labeled with anti-ErbB2 antibody together with either anti-EEA1 or anti-LAMP1 antibodies as indicated. Representative confocal sections are shown with magnified insets to illustrate colocalizations of ErbB2 with EEA1 and LAMP1. Scale bar = 10 μm. c SKBR3 and HCC1954 cells were pretreated with 100 μM of chloroquine (CQ) for 30 min before exposed to 17-AAG for 4 h (0 h as untreated controls). Samples were then analyzed by immunofluorescence and confocal microscopy using anti-ErbB2 and anti-LAMP1 antibodies. Micrographs show representative confocal sections, with magnified insets demonstrating colocalizations. Scale bar = 10 μm. d , e SKBR3 and HCC1954 cells were pretreated with chloroquine at 100 μM for 30 min (DMSO as control) prior to 17-AAG addition for indicated times. Cell lysates were analyzed by immunoblotting with antibodies directed against C- and N-termini of ErbB2. Tubulin was probed to show equal loading. Degradation curves show relative quantification of ErbB2 intensities (including truncated version) in corresponding samples. Error bars represent standard error of the mean ( n = 3), with n.s. not significant and ** p < 0.01.

Journal: Cell Death and Differentiation

Article Title: The deubiquitylase USP2 maintains ErbB2 abundance via counteracting endocytic degradation and represents a therapeutic target in ErbB2-positive breast cancer

doi: 10.1038/s41418-020-0538-8

Figure Lengend Snippet: a b SKBR3 and HCC1954 cells were treated with 17-AAG at 500 nM for 4 h, before processed for immunofluorescence assays along with untreated control cells. Cells were labeled with anti-ErbB2 antibody together with either anti-EEA1 or anti-LAMP1 antibodies as indicated. Representative confocal sections are shown with magnified insets to illustrate colocalizations of ErbB2 with EEA1 and LAMP1. Scale bar = 10 μm. c SKBR3 and HCC1954 cells were pretreated with 100 μM of chloroquine (CQ) for 30 min before exposed to 17-AAG for 4 h (0 h as untreated controls). Samples were then analyzed by immunofluorescence and confocal microscopy using anti-ErbB2 and anti-LAMP1 antibodies. Micrographs show representative confocal sections, with magnified insets demonstrating colocalizations. Scale bar = 10 μm. d , e SKBR3 and HCC1954 cells were pretreated with chloroquine at 100 μM for 30 min (DMSO as control) prior to 17-AAG addition for indicated times. Cell lysates were analyzed by immunoblotting with antibodies directed against C- and N-termini of ErbB2. Tubulin was probed to show equal loading. Degradation curves show relative quantification of ErbB2 intensities (including truncated version) in corresponding samples. Error bars represent standard error of the mean ( n = 3), with n.s. not significant and ** p < 0.01.

Article Snippet: Goat anti-ErbB2 (AF1129) antibody was obtained from R&D systems.

Techniques: Immunofluorescence, Control, Labeling, Confocal Microscopy, Western Blot, Quantitative Proteomics

a SKBR3 cell lines with stable knockdown of USP2, AMSH, AMSHLP, and USP8 (two shRNAs per target and empty vector pLKO.1 as control) were treated with 80 nM of 17-AAG or DMSO for 10 h. Cell lysates were subjected to immunoblotting analysis using anti-ErbB2 antibody. GAPDH or Tubulin was probed to confirm equal loading. b quantification data of relative ErbB2 intensities from ( a ). c SKBR3 cells were transfected with constructs expressing GFP, GFP-AMSH, GFP-AMSHLP, GFP-USP8, GFP-USP2, and GFP-USP2(C276A) as indicated. Cells were treated with DMSO or 17-AAG (500 nM) for 4 h and then processed for immunofluorescence analysis using anti-ErbB2 antibody. Nucleus was stained with DAPI. Images show representative confocal sections. GFP-USP2 expressing cell was indicated with solid box. Scale bar = 10 μm. d Intensities of the membrane and intracellular pools of ErbB2 were quantified using results from C with Image Studio software (Version 4.0) and plotted. e SKBR3 cells were treated with 500 nM of 17-AAG for indicated times and lysed. ErbB2 was immunoprecipitated from cell lysates using mouse anti-ErbB2 antibody (clone 9G6). Cell lysates (input) and immunoprecipitation (IP) samples were analyzed by immunoblotting with indicated antibodies. Error bars represent standard error of the mean ( n = 3), with n.s. not significant, * p < 0.05, and ** p < 0.01.

Journal: Cell Death and Differentiation

Article Title: The deubiquitylase USP2 maintains ErbB2 abundance via counteracting endocytic degradation and represents a therapeutic target in ErbB2-positive breast cancer

doi: 10.1038/s41418-020-0538-8

Figure Lengend Snippet: a SKBR3 cell lines with stable knockdown of USP2, AMSH, AMSHLP, and USP8 (two shRNAs per target and empty vector pLKO.1 as control) were treated with 80 nM of 17-AAG or DMSO for 10 h. Cell lysates were subjected to immunoblotting analysis using anti-ErbB2 antibody. GAPDH or Tubulin was probed to confirm equal loading. b quantification data of relative ErbB2 intensities from ( a ). c SKBR3 cells were transfected with constructs expressing GFP, GFP-AMSH, GFP-AMSHLP, GFP-USP8, GFP-USP2, and GFP-USP2(C276A) as indicated. Cells were treated with DMSO or 17-AAG (500 nM) for 4 h and then processed for immunofluorescence analysis using anti-ErbB2 antibody. Nucleus was stained with DAPI. Images show representative confocal sections. GFP-USP2 expressing cell was indicated with solid box. Scale bar = 10 μm. d Intensities of the membrane and intracellular pools of ErbB2 were quantified using results from C with Image Studio software (Version 4.0) and plotted. e SKBR3 cells were treated with 500 nM of 17-AAG for indicated times and lysed. ErbB2 was immunoprecipitated from cell lysates using mouse anti-ErbB2 antibody (clone 9G6). Cell lysates (input) and immunoprecipitation (IP) samples were analyzed by immunoblotting with indicated antibodies. Error bars represent standard error of the mean ( n = 3), with n.s. not significant, * p < 0.05, and ** p < 0.01.

Article Snippet: Goat anti-ErbB2 (AF1129) antibody was obtained from R&D systems.

Techniques: Knockdown, Plasmid Preparation, Control, Western Blot, Transfection, Construct, Expressing, Immunofluorescence, Staining, Membrane, Software, Immunoprecipitation

a , b SKBR3 and HCC1954 cells were treated with cycloheximide (100 μg/ml) in the absence or presence of 10 μM of ML364 for indicated times and lysed. Samples were analyzed by immunoblotting with indicated antibodies. Actin blots show equal loading. Turnover curves show relative quantification of ErbB2 expression at corresponding time points. c AU565 cells were treated with 10 μM of ML364 for indicated times. Cell lysates were prepared and analyzed by immunoblotting using indicated antibodies. Actin was probed to show equal loading. d AU565 cells were treated as in ( c ), and ErbB2 was immunoprecipitated using mouse anti-ErbB2 antibody (clone 9G6) from cell lysates, before immunoblotting assays to probe for ubiquitin and ErbB2. Column chart on the right shows the quantification of relative ubiquitin signal after ErbB2 normalization. e AU565 cells were treated with 17-AAG at 80 nM in the absence or presence of 10 μM of ML364 as indicated for 12 h. ErbB2 was immunoprecipitated using mouse anti-ErbB2 antibody (clone 9G6) from cell lysates and analyzed by immunoblotting to examine the ubiquitylation status of ErbB2 along with cell lysates. Column chart on the right shows the relative quantification of ubiquitin signal detected from immunoprecipitations after ErbB2 normalization. f – h SKBR3, AU565, and HCC1954 cells were treated with ML364, ganetespib, PU-H71, or various combinations at indicated concentrations for 12 h and lysed. Cell lysates were subjected to immunoblotting analysis with indicated antibodies. Actin blots are shown to confirm equal loading. The column charts show corresponding quantification of relative ErbB2 levels. Error bars represent standard error of the mean ( n = 3), with * p < 0.05 and ** p < 0.01.

Journal: Cell Death and Differentiation

Article Title: The deubiquitylase USP2 maintains ErbB2 abundance via counteracting endocytic degradation and represents a therapeutic target in ErbB2-positive breast cancer

doi: 10.1038/s41418-020-0538-8

Figure Lengend Snippet: a , b SKBR3 and HCC1954 cells were treated with cycloheximide (100 μg/ml) in the absence or presence of 10 μM of ML364 for indicated times and lysed. Samples were analyzed by immunoblotting with indicated antibodies. Actin blots show equal loading. Turnover curves show relative quantification of ErbB2 expression at corresponding time points. c AU565 cells were treated with 10 μM of ML364 for indicated times. Cell lysates were prepared and analyzed by immunoblotting using indicated antibodies. Actin was probed to show equal loading. d AU565 cells were treated as in ( c ), and ErbB2 was immunoprecipitated using mouse anti-ErbB2 antibody (clone 9G6) from cell lysates, before immunoblotting assays to probe for ubiquitin and ErbB2. Column chart on the right shows the quantification of relative ubiquitin signal after ErbB2 normalization. e AU565 cells were treated with 17-AAG at 80 nM in the absence or presence of 10 μM of ML364 as indicated for 12 h. ErbB2 was immunoprecipitated using mouse anti-ErbB2 antibody (clone 9G6) from cell lysates and analyzed by immunoblotting to examine the ubiquitylation status of ErbB2 along with cell lysates. Column chart on the right shows the relative quantification of ubiquitin signal detected from immunoprecipitations after ErbB2 normalization. f – h SKBR3, AU565, and HCC1954 cells were treated with ML364, ganetespib, PU-H71, or various combinations at indicated concentrations for 12 h and lysed. Cell lysates were subjected to immunoblotting analysis with indicated antibodies. Actin blots are shown to confirm equal loading. The column charts show corresponding quantification of relative ErbB2 levels. Error bars represent standard error of the mean ( n = 3), with * p < 0.05 and ** p < 0.01.

Article Snippet: Goat anti-ErbB2 (AF1129) antibody was obtained from R&D systems.

Techniques: Western Blot, Quantitative Proteomics, Expressing, Immunoprecipitation, Ubiquitin Proteomics

a Colony formation assays carried out with SKBR3 and HCC1954 cells under the treatment of vehicle, ML364 (10 μM), 17-AAG (100 nM), and the combination of ML364 (10 μM) and 17-AAG (100 nM). b Quantification data from a showing the relative amounts of colonies formed in each group. c SKBR3 and HCC1954 cells were treated as in a for 24 h and then processed for cell cycle analysis. Representative histograms are shown to illustrate cell cycle distributions. Column charts on the right demonstrate quantification data of cells within each stage as indicated. d AU565 and AU565-USP2del cells were treated with 80 nM of 17-AAG for indicated times. Cell lysates were subjected to immunoblotting analysis using indicated antibodies. Degradation curves show the relative quantification of ErbB2 levels at corresponding time points. e Colony formation assays performed using AU565, AU565-USP2del, and AU565-USP2del-CCND1 cells. Column chart shows the relative amounts of colonies formed in each cell line. f AU565 and AU565-USP2del-CCND1 cells were treated with 100 μg/ml of cycloheximide for indicated times and lysed. Samples were analyzed by immunoblotting using indicated antibodies. Actin was probed to confirm equal loading. The turnover curve on the right shows the quantification of relative ErbB2 abundance from immunoblotting assays. Error bars represent standard error of the mean ( n = 3), with * p < 0.05 and ** p < 0.01.

Journal: Cell Death and Differentiation

Article Title: The deubiquitylase USP2 maintains ErbB2 abundance via counteracting endocytic degradation and represents a therapeutic target in ErbB2-positive breast cancer

doi: 10.1038/s41418-020-0538-8

Figure Lengend Snippet: a Colony formation assays carried out with SKBR3 and HCC1954 cells under the treatment of vehicle, ML364 (10 μM), 17-AAG (100 nM), and the combination of ML364 (10 μM) and 17-AAG (100 nM). b Quantification data from a showing the relative amounts of colonies formed in each group. c SKBR3 and HCC1954 cells were treated as in a for 24 h and then processed for cell cycle analysis. Representative histograms are shown to illustrate cell cycle distributions. Column charts on the right demonstrate quantification data of cells within each stage as indicated. d AU565 and AU565-USP2del cells were treated with 80 nM of 17-AAG for indicated times. Cell lysates were subjected to immunoblotting analysis using indicated antibodies. Degradation curves show the relative quantification of ErbB2 levels at corresponding time points. e Colony formation assays performed using AU565, AU565-USP2del, and AU565-USP2del-CCND1 cells. Column chart shows the relative amounts of colonies formed in each cell line. f AU565 and AU565-USP2del-CCND1 cells were treated with 100 μg/ml of cycloheximide for indicated times and lysed. Samples were analyzed by immunoblotting using indicated antibodies. Actin was probed to confirm equal loading. The turnover curve on the right shows the quantification of relative ErbB2 abundance from immunoblotting assays. Error bars represent standard error of the mean ( n = 3), with * p < 0.05 and ** p < 0.01.

Article Snippet: Goat anti-ErbB2 (AF1129) antibody was obtained from R&D systems.

Techniques: Cell Cycle Assay, Western Blot, Quantitative Proteomics

a HCC1954 cells were inoculated into female nude mice to generate xenograft mouse models. Mice were randomized into four groups to receive control vehicle, ML364, 17-AAG, or the combination of ML364 and 17-AAG. The sizes of xenografts were measured every 2 days and calculated tumor volumes were plotted. b Resected xenograft tumor samples from each treatment group. c Tumor weights were measured and plotted. d Tumor tissue sections were analyzed by immunohistochemistry using anti-ErbB2, anti-Ki-67, and anti-cyclin D1 antibodies. Images show representative xenograft sections. Scale bar = 50 μm. e Column charts show quantification data (integral optical density) of relative intensities for ErbB2, Ki-67, and cyclin D1. Error bars represent standard error of the mean ( n = 5), with * p < 0.05 and ** p < 0.01.

Journal: Cell Death and Differentiation

Article Title: The deubiquitylase USP2 maintains ErbB2 abundance via counteracting endocytic degradation and represents a therapeutic target in ErbB2-positive breast cancer

doi: 10.1038/s41418-020-0538-8

Figure Lengend Snippet: a HCC1954 cells were inoculated into female nude mice to generate xenograft mouse models. Mice were randomized into four groups to receive control vehicle, ML364, 17-AAG, or the combination of ML364 and 17-AAG. The sizes of xenografts were measured every 2 days and calculated tumor volumes were plotted. b Resected xenograft tumor samples from each treatment group. c Tumor weights were measured and plotted. d Tumor tissue sections were analyzed by immunohistochemistry using anti-ErbB2, anti-Ki-67, and anti-cyclin D1 antibodies. Images show representative xenograft sections. Scale bar = 50 μm. e Column charts show quantification data (integral optical density) of relative intensities for ErbB2, Ki-67, and cyclin D1. Error bars represent standard error of the mean ( n = 5), with * p < 0.05 and ** p < 0.01.

Article Snippet: Goat anti-ErbB2 (AF1129) antibody was obtained from R&D systems.

Techniques: Control, Immunohistochemistry

a 4T1 cells stably expressing ErbB2 (4T1-ErbB2) were implanted into female Balb/c mice for xenograft formation. Mice were randomly divided into four groups and administered with control vehicle, ML364, 17-AAG, or the indicated combination. The xenograft volumes were measured and plotted. b Xenografts resected from mice receiving different treatment as indicated. c Tumor weights of xenograft samples from each treatment group. d Immunoblotting analysis of tumor tissue samples using indicated antibodies to detect ErbB2 levels. Vinculin blots show equal loading. Column chart shows relative quantification of ErbB2 expression. Error bars represent standard error of the mean ( n = 5), with * p < 0.05.

Journal: Cell Death and Differentiation

Article Title: The deubiquitylase USP2 maintains ErbB2 abundance via counteracting endocytic degradation and represents a therapeutic target in ErbB2-positive breast cancer

doi: 10.1038/s41418-020-0538-8

Figure Lengend Snippet: a 4T1 cells stably expressing ErbB2 (4T1-ErbB2) were implanted into female Balb/c mice for xenograft formation. Mice were randomly divided into four groups and administered with control vehicle, ML364, 17-AAG, or the indicated combination. The xenograft volumes were measured and plotted. b Xenografts resected from mice receiving different treatment as indicated. c Tumor weights of xenograft samples from each treatment group. d Immunoblotting analysis of tumor tissue samples using indicated antibodies to detect ErbB2 levels. Vinculin blots show equal loading. Column chart shows relative quantification of ErbB2 expression. Error bars represent standard error of the mean ( n = 5), with * p < 0.05.

Article Snippet: Goat anti-ErbB2 (AF1129) antibody was obtained from R&D systems.

Techniques: Stable Transfection, Expressing, Control, Western Blot, Quantitative Proteomics

a The current working model shows the regulation of cell surface ErbB2 by USP2 and HSP90. Under steady state conditions, USP2 protects ErbB2 surface levels by restricting its ubiquitylation. Through inhibiting USP2, ML364 potentiates the pro-degradation effects of HSP90 inhibitors toward ErbB2, which collectively elicit potent anti-cancer effects.

Journal: Cell Death and Differentiation

Article Title: The deubiquitylase USP2 maintains ErbB2 abundance via counteracting endocytic degradation and represents a therapeutic target in ErbB2-positive breast cancer

doi: 10.1038/s41418-020-0538-8

Figure Lengend Snippet: a The current working model shows the regulation of cell surface ErbB2 by USP2 and HSP90. Under steady state conditions, USP2 protects ErbB2 surface levels by restricting its ubiquitylation. Through inhibiting USP2, ML364 potentiates the pro-degradation effects of HSP90 inhibitors toward ErbB2, which collectively elicit potent anti-cancer effects.

Article Snippet: Goat anti-ErbB2 (AF1129) antibody was obtained from R&D systems.

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goat anti human erbb2 her2 antibody af1129 (R&D Systems)

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