The primary antibodies were rabbit anti-human E-cadherin antibody (#3195; 1:1,000) and rabbit anti-human β-actin antibody (#4967; 1:1,000) (both from Cell Signaling Technology, Beverly, MA, USA). Horseradish peroxidase-conjugated (HRP) anti-rabbit antibodies (1:5,000; Santa Cruz Biotechnology, Santa Cruz, CA, USA) were used as the secondary antibodies. Cell lysates in 1X SDS loading buffer (60 mM Tris-HCl, pH 6.8; 2% SDS; 20% glycerol; 0.25% bromophenol blue; and 1.25% 2-mercaptoethanol) were incubated at 100°C for 10 min to facilitate sample loading for conventional western blot analysis. The relative protein levels were quantified using densitometry with a Gel-Pro Analyzer (Media Cybernetics, Rockville, MD, USA).
Rabbit anti human e cadherin antibody
Manufactured by Cell Signaling Technology
Sourced in United States, China, Japan
The Rabbit anti-human E-cadherin antibody is a primary antibody that specifically binds to the E-cadherin protein expressed in human cells. E-cadherin is a key cell-cell adhesion molecule involved in the maintenance of epithelial cell-cell junctions and tissue integrity. This antibody can be used to detect and study the expression and localization of E-cadherin in various human cell and tissue samples.
Automatically generated - may contain errors
Lab products found in correlation
Ne per nuclear and cytoplasmic extraction reagent, by Thermo Fisher Scientific (2 mentions)
Ripa buffer, by Thermo Fisher Scientific (2 mentions)
Horseradish peroxidase conjugated hrp anti rabbit antibodies, by Santa Cruz Biotechnology (1 mentions)
Rabbit anti human β actin antibody, by Cell Signaling Technology (1 mentions)
Gel pro analyzer, by Media Cybernetics (1 mentions)
Horseradish peroxidase, by Cell Signaling Technology (1 mentions)
Enhanced chemiluminescence detection system, by GE Healthcare (1 mentions)
Protease inhibitor mixture, by Merck Group (1 mentions)
Dc protein assay, by Bio-Rad (1 mentions)
3 protocols using rabbit anti human e cadherin antibody
1
Western Blot Analysis of E-cadherin and β-actin
2
Immunohistochemical Analysis of UHRF2 and E-cadherin
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The construction of TMAs and immunohistochemistry were performed as previously described.22 (link) Rabbit anti-human UHRF2 monoclonal antibody (1:1,000; Wuhan Boster Biological Technology, Ltd., Wuhan, People’s Republic of China) and rabbit anti-human E-cadherin antibody (1:100; Cell Signaling Technology, Danvers, MA, USA) were utilized to detect the levels of UHRF2 and E-cadherin. The density level of strong, moderate, and weak staining was defined as in previous studies.22 (link)–24 (link) The assessment was performed blindly by two pathologists.
3
Protein Expression Analysis Pipeline
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The whole cell lysates were prepared with RIPA buffer (Thermo Scientific) with a protease inhibitor mixture (Sigma), and the nuclear proteins were isolated with NE-PER Nuclear and Cytoplasmic Extraction Reagents (Thermo Scientific) as reported previously [19] . The protein concentration was determined by using a DC Protein Assay (Bio-Rad). The lysates (20 μg) were separated by electrophoresis on SDS-PAGE gels and transferred electrophoretically onto nitrocellulose membranes according to our previous reports [25] [26] [27] [28] . The following primary antibodies (Cell Signaling Japan, Tokyo, Japan) were used: rabbit anti-human E-cadherin antibody, rabbit anti-human N-cadherin antibody, rabbit anti-human vimentin antibody, rabbit anti-human ZEB1 antibody, rabbit anti-human ZEB2 antibody, rabbit anti-human β-actin antibody, rabbit anti-human histone H3 antibody, and rabbit anti-human α-tubulin antibody. After the reaction with a proper secondary antibody labeled with horseradish peroxidase (Cell Signaling Japan), the peroxidase activity was detected with an enhanced chemiluminescence detection system (GE Healthcare).
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