Anti‐VE‐cadherin antibody was purchased from R&D Systems (Minneapolis, MN, USA). MLN4924 was purchased from Funakoshi Chemical Co. (Tokyo, Japan). Anti‐CUL3 (clone CUL3‐9, catalog# SAB4200180), anti‐Flag mAb, M2, and mouse monoclonal anti‐β‐actin antibody (clone AC‐15) were purchased from Sigma‐Aldrich (St. Louis, MO, USA). Anti‐β‐catenin antibody was purchased from Cell Signaling Technology (Danvers, MA, USA). Anti‐p120catenin (catalog# 610133) antibody was purchased from BD Transduction Laboratories (San Diego, CA, USA).
Anti p120 catenin
Manufactured by BD
Sourced in United States
Anti-p120-catenin is a lab equipment product used for the detection and analysis of the p120-catenin protein. It is a tool for researchers to study the expression and localization of this protein, which is involved in cell-cell adhesion and signaling pathways.
Automatically generated - may contain errors
Lab products found in correlation
Anti β catenin, by BD (5 mentions)
Anti vinculin, by Merck Group (2 mentions)
Anti n cadherin, by BD (2 mentions)
Lsm 780, by Zeiss (2 mentions)
Anti zo 1, by Thermo Fisher Scientific (2 mentions)
Cy3 conjugated secondary antibody, by Jackson ImmunoResearch (2 mentions)
Anti flag m2 mab, by Merck Group (1 mentions)
Mouse monoclonal anti β actin antibody clone ac 15, by Merck Group (1 mentions)
Anti β catenin antibody, by Cell Signaling Technology (1 mentions)
Anti β tubulin aa2, by Merck Group (1 mentions)
Anti zo 1, by BD (1 mentions)
Anti esrp1 2, by Rockland Immunochemicals (1 mentions)
Anti claudin 7, by Thermo Fisher Scientific (1 mentions)
Anti β catenin, by Santa Cruz Biotechnology (1 mentions)
Anti fibronectin, by Merck Group (1 mentions)
Anti α sma, by Merck Group (1 mentions)
Fitc conjugated phalloidin, by Merck Group (1 mentions)
Anti gapdh 14c10, by Cell Signaling Technology (1 mentions)
Horseradish peroxidase conjugated goat anti rabbit and anti mouse secondary antibodies, by Bio-Rad (1 mentions)
Claudin 4 mab, by Thermo Fisher Scientific (1 mentions)
8 protocols using anti p120 catenin
1
Antibodies for Protein Interaction Analysis
2
Antibody Expression Analysis of Epithelial Proteins
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The following antibodies were used: anti–E-cadherin (HECD1 #ab1416; Abcam; 24E10 #3195; Cell Signaling; #610182; BD Transduction Laboratories), anti–claudin-7 (#349100; Invitrogen), anti–p120-catenin (#610134; BD Transduction Laboratories), anti-ZO1 (#61096; BD Transduction Laboratories), anti–β-tubulin (AA2 #T8328; Sigma Aldrich), anti-APC (H290; Santa Cruz), anti–β-catenin (#610153; BD Transduction Laboratories), and anti-ESRP1/2 (Rockland). Antibodies were used at 1:1000 for immunoblot analysis and 1:200 for immunostaining, unless otherwise stated. Secondary antibodies for immunoblots were Alexa488 goat anti-mouse/rabbit (#A-11001 and #A-11035; Thermo Scientific) and Alexa546 goat anti-mouse/rabbit (#A-11030 and #A-11035; Thermo Scientific), used at 1:10,000.
3
Immunohistochemical Analysis of Cell-Cell Adhesion
4
Immunofluorescence Imaging of Cell-Cell Junctions
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Cells (1 × 105) were plated on fibronectin‐coated 4‐well chamber slides (5 μg/mL in PBS) and allowed to reach confluence (1–2 days). Cells were rinsed with PBS, fixed with cold acetone for 10 min on ice, permeabilized with PBS containing 0.1% Triton X‐100 for 12 min at room temperature, and then blocked with PBS containing 1% BSA at 37°C for 30 min. Following incubation, slides were washed once with PBS and incubated with specific primary antibodies for 2 h at room temperature. The primary antibodies were anti ‐ZO‐1 (Life Technologies), anti‐ β‐catenin, anti‐P120‐ catenin, anti‐N‐cadherin (BD Bioscience), anti‐vinculin and FITC‐conjugated phalloidin (Sigma) prepared in PBS (1:200) containing 1% BSA. Following incubation, slides were washed with PBS and incubated with specific Cy3‐conjugated secondary antibodies (Jackson ImmunoResearch, West Grove, PA; (1:800) in PBS containing 1% BSA for 1 h at room temperature. Following incubation, slides were washed four times with PBS and examined using a fluorescence microscope (Carl Zeiss Optical, Germany) and images were taken in digital format.
5
Immunodetection of Cell-Cell Junctions
6
GV1001 Peptide-Induced Angiogenesis Signaling
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GV1001, a human telomerase-derived 16-mer peptide, was provided by GemVax-KAEL (Seongnam, Republic of Korea). The following agents were obtained from commercial sources: vascular endothelial growth factor-A 165 (Merck Millipore, Billerica, MA, USA); anti-phospho-VEGFR-2 (Y1175), anti-phospho-MEK (S217/S221), anti-MEK, anti-phospho-Src (Y416), anti-Src, anti-phospho-p70S6K (T421/S424), anti-phospho-Akt (S473), anti-phospho-ERK (T202/Y204), anti-phospho-pRb (S780), and anti-phospho-pRb (S807/S811) (Cell Signaling Technology, Beverly, MA, USA); fibroblast growth factor-2 (FGF-2), anti-phosphotyrosine, anti-phospho-FAK(Y397), anti-FAK, anti-β-catenin, and anti-p120-catenin (BD Biosciences, Bedford, MA, USA); anti-vascular endothelial (VE)-cadherin, anti-VEGFR-2, anti-p70S6K, anti-Akt, anti-ERK, anti-Cdk2, anti-Cdk4, anti-cyclin D, anti-cyclin E, anti-p27kip1, anti-actin antibodies, and mouse and rabbit IgG-horseradish peroxidase conjugates (Santa Cruz Biotechnology, Santa Cruz, CA, USA); goat anti-mouse IgG-Alexa Fluor 488 conjugate (Thermo Fisher Scientific Co., Waltham, MA, USA).
7
Vinculin Knockdown in Breast Cell Lines
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The primary antibodies were used for immunofluorescence and immunoblotting: anti-E-cadherin (610181, BD); anti-a-catenin (610193, BD); anti-b-catenin (610154, BD); anti-g-catenin (610253, BD); anti-p120-catenin (610133, BD); anti-vinculin (BM1611, (Liang et al., 2018) . Virus-infected cells were selected with puromycin (1 mg/ml).
RNA interference MM436-10, MCF7 and MCF10A cells (2 3 10 5 ) were seeded per well in a 6-well plate, followed by lentiviral transduction with control vector (GV248) or two hairpins against vinculin. The hairpin target sequences were: shRNA1 (5 0 -CAGGCAAATCAGTTACTAA-3 0 ), shRNA2 (5 0 -CTGGAAATCAAGCTGCTTA-3 0 ). The shRNAs against vinculin were synthesized by Genechem, China. Stable cells expressing the shRNAs were selected using puromycin (1 mg/ml) 48 h after infection. For transient vinculin knockdown, cells were transfected with siRNA targeting the 3 0 -UTR of vinculin (5 0 -GGTGTTTGTTCATCTGTAA À3 0 ) and non-targeting control siRNA (5 0 -UUCUCCGAACGUGUCACGUTT-3 0 ) before further experimental assays. The knockdown efficiency was determined by qPCR and western blot.
RNA interference MM436-10, MCF7 and MCF10A cells (2 3 10 5 ) were seeded per well in a 6-well plate, followed by lentiviral transduction with control vector (GV248) or two hairpins against vinculin. The hairpin target sequences were: shRNA1 (5 0 -CAGGCAAATCAGTTACTAA-3 0 ), shRNA2 (5 0 -CTGGAAATCAAGCTGCTTA-3 0 ). The shRNAs against vinculin were synthesized by Genechem, China. Stable cells expressing the shRNAs were selected using puromycin (1 mg/ml) 48 h after infection. For transient vinculin knockdown, cells were transfected with siRNA targeting the 3 0 -UTR of vinculin (5 0 -GGTGTTTGTTCATCTGTAA À3 0 ) and non-targeting control siRNA (5 0 -UUCUCCGAACGUGUCACGUTT-3 0 ) before further experimental assays. The knockdown efficiency was determined by qPCR and western blot.
8
Immunofluorescence Staining of Cell-Cell Junctions
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Cells (5x104) were plated on fibronectin-coated glass chamber slides until confluent (1–2 days), washed in 1x MES (M5287; Sigma), fixed with 4% paraformaldehyde and permeabilized with 0.1% triton X100 for 10 min on ice, and blocked with 1% ovalbumin in TBS at 37°C for 20 min. Slides were washed with PBS and incubated with: anti-VE-cadherin (550548; BD Biosciences), anti-N-cadherin (610920; BD Biosciences), anti-β-catenin (610154; BD Biosciences), anti-P-120 catenin (610133; BD Biosciences), anti-ZO-1 (617300; Invitrogen), anti-vinculin (V4505; Sigma), and Alexa Fluor 488 Phalloidin (A12379; Thermo Fisher) in TBS containing 1% ovalbumin at 37°C for 30 min. After washing with PBS, cells were incubated with appropriate Cy3-conjugated secondary antibody (Jackson ImmunoResearch; 1:500 dilution in TBS containing 1% ovalbumin) at 37°C for 30 min. Cells were washed with PBS twice, analyzed using a fluorescent microscope (Carl Zeiss Optical Inc., Germany), and images were captured in digital format.
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