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Anti e cadherin antibody

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The Anti-E-cadherin antibody is a laboratory reagent used in various research applications. It is a specific antibody that binds to the E-cadherin protein, which is involved in cell-cell adhesion. The antibody can be used to detect and study the expression and distribution of E-cadherin in biological samples.

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Lab products found in correlation

Facsaria 2 sorter, by BD (2 mentions) Interleukin 4 (il 4), by Thermo Fisher Scientific (1 mentions) Ifn γ, by Thermo Fisher Scientific (1 mentions) Mitotracker red cmxros, by Thermo Fisher Scientific (1 mentions) Lipopolysaccharides (lps), by Merck Group (1 mentions) Lsm 510 confocal laser scanning microscope, by Zeiss (1 mentions) Vectastain elite abc, by Vector Laboratories (1 mentions) Biotinylated anti rat igg secondary antibody, by Vector Laboratories (1 mentions) Observer z1 inverted microscope, by Zeiss (1 mentions) Irdye 800cw goat anti rabbit secondary antibody, by LI COR (1 mentions) Irdye 680 goat anti mouse secondary antibody, by LI COR (1 mentions) Odyssey infrared imaging system, by LI COR (1 mentions) Forskolin, by Merck Group (1 mentions) Lsm image examiner software, by Zeiss (1 mentions) Anti vimentin antibody, by Thermo Fisher Scientific (1 mentions) Immunol fluorence staining kit, by Beyotime (1 mentions) Anti fade fluorescence mounting medium, by Beyotime (1 mentions) Hrp conjugated goat anti rabbit igg, by Santa Cruz Biotechnology (1 mentions) Sc 47778, by Santa Cruz Biotechnology (1 mentions) Goat anti mouse igg, by Santa Cruz Biotechnology (1 mentions)

Close spelling variants of this product

Rat anti-E-cadherin (131900) antibody Anti-E-cadherin rat antibody E-cadherin antibody Anti-E-cadherin E-cadherin

9 protocols using anti e cadherin antibody

1

E-cadherin Immunostaining Protocol for Embryos

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For E-cadherin immunostaining, embryos were dissected at E9.0 to E9.5 and were stained in whole mount with anti-E-Cadherin antibody (Life Technologies, 1:1000 dilution). A biotinylated anti-rat IgG secondary antibody (Vector Laboratories), followed by Vectastain Elite ABC (Vector Laboratories) and TSA fluorescein tyramide reagent (PerkinElmer) amplification, were used to detect anti-E-cadherin as described [36 ]. Embryos were photographed using a Zeiss Observer Z1 inverted microscope.
To compare E-cadherin staining intensity, mutant and control embryos were fixed in 4 % paraformaldehyde at 4 °C overnight, cut by vibratome, then stained with anti-E-Cadherin antibody (Life Technologies, 1:1000 dilution), using an Alexa-488-conjugated anti-rat IgG secondary antibody (Life Technologies, 1:1000 dilution) as described [37 ]. Images were collected using a Zeiss LSM510 laser scanning confocal microscope (data not shown).
Wright K.D., Mahoney Rogers A.A., Zhang J, & Shim K. (2015). Cooperative and independent functions of FGF and Wnt signaling during early inner ear development. BMC Developmental Biology, 15, 33.
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2

Macrophage Polarization and Mitochondrial Function

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Bone marrow derived macrophages (BMDM) were differentiated for 5 days in RPMI 1640 media with 15% fetal calf serum (FCS) and antibiotic-antimycotic solution supplemented with M-CSF (20 ng/ml). Polarization of BMDM was performed for additional 3 days RPMI 1640 media with 15% fetal calf serum (FCS) with 100 ng/ml LPS (Sigma–Aldrich, St. Louis, MO, USA) and 10 ng/ml IFNγ (PeproTech, Rocky Hill, NJ) for M1 macrophages and with IL-4 (10 ng/ml, PeproTech, Rocky Hill, NJ) for M2 macrophages. CO treatment was applied at 250 ppm in CO chamber (5% CO2, 21% O2 and 95% humidity) as previously described [18 (link)].
PC3 cells were co-cultured with BMDM from Hmox1fl/fl or LyzM-Cre:Hmox1fl/fl mice in a 1:2 or 1:5 ratio for 24 h. PC3/BMDM cells alone or in co-culture were used for immunostaining using anti-E-cadherin antibody (CatNo: ab15148) and Mitotracker Red CMXRos (Life Technologies), for detecting mitochondria as well as for direct testing of mitochondrial activity Mitochondria Stress Kit (Seahorse) was used as previously described [49 (link)].
Overexpression of HO-1: Constructs were kindly provided by Dr. Chau (Taiwan) and forced overexpressions of Flag, HO-1-Flag or truncated HO-1-Flag (t-HO-1) were established in PC3 cells upon transfection with Amaxa. Forty eight hours after transfection, cells were stained or cell lysates were immunoblotted.
Nemeth Z., Li M., Csizmadia E., Döme B., Johansson M., Persson J.L., Seth P., Otterbein L, & Wegiel B. (2015). Heme oxygenase-1 in macrophages controls prostate cancer progression. Oncotarget, 6(32), 33675-33688.
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3

Immunoblotting Analysis of Cell Signaling

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Immunoblotting analysis was performed according to the procedures as previously described [27 (link)]. Briefly, HT-29 cells or Caco-2 cells were seeded onto 12-well plates at 2×105 cells per well, treated with 4 mM NaB for 4 d, then cells were lysed and collected for protein extraction. The extracts were separated by 10% SDS-PAGE and transferred to nitrocellulose membranes, then incubated with antibodies and visualized using an Odyssey Infrared Imaging System (Li-Cor Biosciences, Lincoln, NE). Band density was normalized to β-actin. Antibodies against villin, IDH1, PDH, PARP, caspase-3, MSH2, MLH1 were purchased from Cell Signaling Technology (Danvers, MA). Anti-E-cadherin antibody was purchased from Life Technologies. Anti-TET3 antibody was purchased from Thermo Scientific (Waltham, MA). Anti-Ac-H3 and anti-Ac-H4 antibodies were purchased from Santa Cruz (Dallas, Texas). Anti-β-actin antibody was purchased from DSHB (Iowa City, IA). IRDye 680 goat anti-mouse secondary antibody and IRDye 800 CW goat anti-rabbit secondary antibody were purchased from Li-Cor Biosciences (Lincoln, NE).
Sun X, & Zhu M.J. (2018). Butyrate inhibits indices of colorectal carcinogenesis via enhancing α-ketoglutarate-dependent DNA demethylation of mismatch repair genes. Molecular nutrition & food research, 62(10), e1700932.
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4

Forskolin-Induced Trophoblast Barrier Characterization

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Following formation of a confluent epithelial monolayer on the membrane surface in the upper microchannel, we treated the apical side of the epithelium with forskolin to activate the protein kinase A pathway in the cultured trophoblasts. A stock solution of forskolin (Sigma; 5 mg/mL in DMSO) was diluted with F-12K medium to a final concentration of 50 uM and perfused through the upper microchannel. After 72 hours of forskolin treatment, the trophoblast cells were fixed in 4% PFA, permeabilized in Triton-X 100, and then incubated with 2% BSA in PBS for immunofluorescence staining. To analyze changes in junctional protein expression, the samples were incubated with anti-E-cadherin antibody (Life Technologies) in 2% BSA, followed by secondary antibody and DAPI. Additionally, media perfusate was collected at 48, 72, and 96 hours from both untreated and forskolin-treated devices. The collected samples were analyzed using a human chorionic gonadotropin beta (β-hCG) ELISA kit (Abcam) to quantify the levels of β-hCG produced by the trophoblast population at each time point.
Blundell C., Tess E.R., Schanzer A.S., Coutifaris C., Su E.J., Parry S, & Huh D. (2016). A microphysiological model of the human placental barrier. Lab on a chip, 16(16), 3065-3073.
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5

Derivation of Primary PDAC Cell Lines

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Derivation of primary PDAC cell lines were performed as previously described36 (link). Fresh tumors were minced with sterile razor blades, digested with dispase II (17105041, Gibco, 4 mg/ml)/collagenase IV (17104019, Gibco, 4 mg/ml)/RPMI for 1 h at 37°C, filtered by a 70 μm cell strainer, resuspended in RPMI/20%FBS and then seeded on collagen I coated plates (087747, Fisher Scientific). Cells were maintained in RPMI medium with 20% FBS and 1% penicillin, streptomycin and amphotericin B (PSA) antibiotic mixture. Cancer cells were further purified by FACS based on YFP or E-Cadherin expression (anti-E-cadherin antibody, 50-3249-82, eBioscience, 1:100). The sorted cells, using BD FACSAria™ II sorter (South Campus Flow Cytometry Core Lab of MD Anderson Cancer Center) were subsequently expanded in vitro. All studies were performed on cells cultivated less than 30 passages. As these are primary cell lines no further authentication methods were applicable and no mycoplasma tests were performed.
Zheng X., Carstens J.L., Kim J., Scheible M., Kaye J., Sugimoto H., Wu C.C., LeBleu V.S, & Kalluri R. (2015). EMT Program is Dispensable for Metastasis but Induces Chemoresistance in Pancreatic Cancer. Nature, 527(7579), 525-530.
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6

Derivation of Primary PDAC Cell Lines

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Derivation of primary PDAC cell lines were performed as previously described36 (link). Fresh tumors were minced with sterile razor blades, digested with dispase II (17105041, Gibco, 4 mg/ml)/collagenase IV (17104019, Gibco, 4 mg/ml)/RPMI for 1 h at 37°C, filtered by a 70 μm cell strainer, resuspended in RPMI/20%FBS and then seeded on collagen I coated plates (087747, Fisher Scientific). Cells were maintained in RPMI medium with 20% FBS and 1% penicillin, streptomycin and amphotericin B (PSA) antibiotic mixture. Cancer cells were further purified by FACS based on YFP or E-Cadherin expression (anti-E-cadherin antibody, 50-3249-82, eBioscience, 1:100). The sorted cells, using BD FACSAria™ II sorter (South Campus Flow Cytometry Core Lab of MD Anderson Cancer Center) were subsequently expanded in vitro. All studies were performed on cells cultivated less than 30 passages. As these are primary cell lines no further authentication methods were applicable and no mycoplasma tests were performed.
Zheng X., Carstens J.L., Kim J., Scheible M., Kaye J., Sugimoto H., Wu C.C., LeBleu V.S, & Kalluri R. (2015). EMT Program is Dispensable for Metastasis but Induces Chemoresistance in Pancreatic Cancer. Nature, 527(7579), 525-530.
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7

Immunofluorescence Staining of Epithelial-Mesenchymal Markers

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The cells were seeded on square coverslips in six-well plates for 24 h to allow them to attach. Subsequently, the cells were fixed, permeated and blocked using the Immunol Fluorence Staining kit (Beyotime Institute of Biotechnology). The cells were then incubated with anti-E-cadherin antibody (diluted at 1:100; 701134; Thermo Fisher Scientific, Inc.), anti-N-cadherin antibody (diluted at 1:200; PA5-19486; Thermo Fisher Scientific, Inc.) and anti-vimentin antibody (diluted at 1:200; PA5-27231; Thermo Fisher Scientific, Inc.) overnight at 4°C. Secondary antibody (diluted at 1:200; ab150077; Abcam, Cambridge, MA, USA) was applied for 1 h at room temperature. The cells were counterstained with DAPI and washed with PBS following each step of the staining procedure. Coverslips were mounted using Anti-fade Fluorescence Mounting Medium (Beyotime Institute of Biotechnology). The long and short axes of cells were measured using the Zeiss LSM Image Examiner software (version 4.2.0.121; Carl Zeiss AG, Oberkochen, Germany), and the long/short axis ratio was determined by counting 100 cells per experiment.
Fang S., Yu L., Mei H., Yang J., Gao T., Cheng A., Guo W., Xia K, & Liu G. (2016). Cisplatin promotes mesenchymal-like characteristics in osteosarcoma through Snail. Oncology Letters, 12(6), 5007-5014.
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8

Western Blot Analysis of Kidney Proteins

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Kidney proteins were extracted with 1× cell lysis buffer containing Protease Inhibitor Cocktail (Sigma‐Aldrich). After centrifugation at 12500 g at 4°C for 30 min, supernatant was collected and 20 μL of lysate from each sample was run on a 10% dodecyl sulfate (SDS)‐polyacrylamide gel and then electrophoretically transferred to a polyvinylidene difluoride (PVDF) membrane. PVDF membranes were rinsed in TBST (10 mmol/L Tris‐HCL, pH 7.4, 0.9% NaCl, 0.05% Tween 20, and 1 mmol/L EDTA) and blocked in blocking buffer (TBST containing 5% bovine serum albumin) for 1 hour at room temperature. PVDF membranes were then incubated with primary antibodies against β‐actin (sc‐47778, Santa Cruz Biotechnology, CA, USa), E‐cadherin (anti‐E‐cadherin antibody, Thermo Scientific), and α‐smooth muscle actin (α‐SMA; anti‐alpha SMA antibody ab5694, Abcam) overnight at 4°C. Subsequently, the membranes were washed, and then incubated with secondary antibodies (HRP‐conjugated goat anti‐rabbit IgG or goat anti‐mouse IgG (Santa Cruz) for 1 hour at room temperature. The membrane was developed with enhanced chemiluminescent (ECL) substrate (Li‐cor, Lincoln, NE, USA) and exposed to UVP chemiluminescence (Biolite LLC, Upland, CA, USA).
Han S.T., Kim J.S., Lee J.Y., Kim M.K., Yoo J.S., Han B.G., Choi S.O, & Yang J.W. (2017). The mechanism of attenuation of epithelial‐mesenchymal transition by a phosphodiesterase 5 inhibitor via renal klotho expression. Clinical and Experimental Pharmacology & Physiology, 45(3), 269-277.
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9

Intestinal Barrier Protein Assay Protocol

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Maltose dextrin was purchased from Bioserv (Flemington, NJ; Cat# 3585), and Lieber DeCarli liquid diet (Dyets no. 710260) was procured from Dyets Inc. (Bethlehem, PA). Hoechst 33342 dye was purchased from Thermo Fisher Scientific (Waltham, MA; #62249). 33-1500 (clone oc-3f10) and anti-occludin (#33-1500) antibodies were obtained from Invitrogen (Carlsbad, CA). Anti-E-cadherin antibody (#14-3249-82) was purchased from Thermo Fisher Scientific, and anti-β-catenin antibody (#PA5-77934) was obtained from Invitrogen. AlexaFlour-488-conjugated anti-mouse IgG (#AP127P) and Cy3-conjugated anti-rabbit IgG (#12-348) were purchased from Millipore Sigma (Burlington, MA). Guanidinium chloride was purchased from Millipore Sigma, and reduced (#70-18-8) and oxidized (#27025-41-8) glutathione was procured from Sigma Aldrich. All other chemicals were purchased from Sigma-Aldrich (St Louis, MO) or Thermo Fisher Scientific (Tustin, CA).
Shukla P.K., Rao R.G., Meena A.S., Giorgianni F., Lee S.C., Raju P., Shashikanth N., Shekhar C., Beranova S., Balazs L., Tigyi G., Gosain A, & Rao R. (2023). Paneth cell dysfunction in radiation injury and radio-mitigation by human α-defensin 5. Frontiers in Immunology, 14, 1174140.
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