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Santa Cruz Biotechnology small interfering rna sirna transfection
Inverse correlation of E-cadherin expression with ERK phosphorylation. (A) Expression of E-cadherin in 4 cervical cancer cell lines determined via western blot analysis. α-actinin was used as the loading control for quantitative western blotting. (B) SiHa, ME180, and SNU-17 cells were transfected with <t>siRNA</t> against E-cadherin for 48 h. Protein expression of E-cadherin, P-ERK, ERK, and α-actinin was analyzed by western blot. (C) 50 nM EGF was added to SiHa and SNU-17 cells for 15 min, and lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody. (D) SiHa and SNU-17 cells were transfected with siRNA against E-cadherin for 48 h. Lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody.
Small Interfering Rna Sirna Transfection, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Inverse correlation of E-cadherin expression with ERK phosphorylation. (A) Expression of E-cadherin in 4 cervical cancer cell lines determined via western blot analysis. α-actinin was used as the loading control for quantitative western blotting. (B) SiHa, ME180, and SNU-17 cells were transfected with <t>siRNA</t> against E-cadherin for 48 h. Protein expression of E-cadherin, P-ERK, ERK, and α-actinin was analyzed by western blot. (C) 50 nM EGF was added to SiHa and SNU-17 cells for 15 min, and lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody. (D) SiHa and SNU-17 cells were transfected with siRNA against E-cadherin for 48 h. Lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody.
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Inverse correlation of E-cadherin expression with ERK phosphorylation. (A) Expression of E-cadherin in 4 cervical cancer cell lines determined via western blot analysis. α-actinin was used as the loading control for quantitative western blotting. (B) SiHa, ME180, and SNU-17 cells were transfected with <t>siRNA</t> against E-cadherin for 48 h. Protein expression of E-cadherin, P-ERK, ERK, and α-actinin was analyzed by western blot. (C) 50 nM EGF was added to SiHa and SNU-17 cells for 15 min, and lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody. (D) SiHa and SNU-17 cells were transfected with siRNA against E-cadherin for 48 h. Lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody.
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Inverse correlation of E-cadherin expression with ERK phosphorylation. (A) Expression of E-cadherin in 4 cervical cancer cell lines determined via western blot analysis. α-actinin was used as the loading control for quantitative western blotting. (B) SiHa, ME180, and SNU-17 cells were transfected with <t>siRNA</t> against E-cadherin for 48 h. Protein expression of E-cadherin, P-ERK, ERK, and α-actinin was analyzed by western blot. (C) 50 nM EGF was added to SiHa and SNU-17 cells for 15 min, and lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody. (D) SiHa and SNU-17 cells were transfected with siRNA against E-cadherin for 48 h. Lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody.
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Santa Cruz Biotechnology e cadherin sirna
Inverse correlation of E-cadherin expression with ERK phosphorylation. (A) Expression of E-cadherin in 4 cervical cancer cell lines determined via western blot analysis. α-actinin was used as the loading control for quantitative western blotting. (B) SiHa, ME180, and SNU-17 cells were transfected with <t>siRNA</t> against E-cadherin for 48 h. Protein expression of E-cadherin, P-ERK, ERK, and α-actinin was analyzed by western blot. (C) 50 nM EGF was added to SiHa and SNU-17 cells for 15 min, and lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody. (D) SiHa and SNU-17 cells were transfected with siRNA against E-cadherin for 48 h. Lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody.
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Santa Cruz Biotechnology c transfection
Inverse correlation of E-cadherin expression with ERK phosphorylation. (A) Expression of E-cadherin in 4 cervical cancer cell lines determined via western blot analysis. α-actinin was used as the loading control for quantitative western blotting. (B) SiHa, ME180, and SNU-17 cells were transfected with <t>siRNA</t> against E-cadherin for 48 h. Protein expression of E-cadherin, P-ERK, ERK, and α-actinin was analyzed by western blot. (C) 50 nM EGF was added to SiHa and SNU-17 cells for 15 min, and lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody. (D) SiHa and SNU-17 cells were transfected with siRNA against E-cadherin for 48 h. Lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody.
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Santa Cruz Biotechnology sirna targeting e cadherin sc 35242
Inverse correlation of E-cadherin expression with ERK phosphorylation. (A) Expression of E-cadherin in 4 cervical cancer cell lines determined via western blot analysis. α-actinin was used as the loading control for quantitative western blotting. (B) SiHa, ME180, and SNU-17 cells were transfected with <t>siRNA</t> against E-cadherin for 48 h. Protein expression of E-cadherin, P-ERK, ERK, and α-actinin was analyzed by western blot. (C) 50 nM EGF was added to SiHa and SNU-17 cells for 15 min, and lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody. (D) SiHa and SNU-17 cells were transfected with siRNA against E-cadherin for 48 h. Lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody.
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Inverse correlation of E-cadherin expression with ERK phosphorylation. (A) Expression of E-cadherin in 4 cervical cancer cell lines determined via western blot analysis. α-actinin was used as the loading control for quantitative western blotting. (B) SiHa, ME180, and SNU-17 cells were transfected with siRNA against E-cadherin for 48 h. Protein expression of E-cadherin, P-ERK, ERK, and α-actinin was analyzed by western blot. (C) 50 nM EGF was added to SiHa and SNU-17 cells for 15 min, and lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody. (D) SiHa and SNU-17 cells were transfected with siRNA against E-cadherin for 48 h. Lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody.

Journal: Cancer Genomics & Proteomics

Article Title: Loss of E‐cadherin Activates EGFR‐MEK/ERK Signaling, Promoting Cervical Cancer Progression

doi: 10.21873/cgp.20501

Figure Lengend Snippet: Inverse correlation of E-cadherin expression with ERK phosphorylation. (A) Expression of E-cadherin in 4 cervical cancer cell lines determined via western blot analysis. α-actinin was used as the loading control for quantitative western blotting. (B) SiHa, ME180, and SNU-17 cells were transfected with siRNA against E-cadherin for 48 h. Protein expression of E-cadherin, P-ERK, ERK, and α-actinin was analyzed by western blot. (C) 50 nM EGF was added to SiHa and SNU-17 cells for 15 min, and lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody. (D) SiHa and SNU-17 cells were transfected with siRNA against E-cadherin for 48 h. Lysates were immunoprecipitated with an EGFR antibody followed by immunoblotting with E-cadherin antibody. The blot was re-probed with anti-EGFR antibody.

Article Snippet: Small interfering RNA (siRNA) transfection. siRNAs specific for E-cadherin were procured from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

Techniques: Expressing, Phospho-proteomics, Western Blot, Control, Transfection, Immunoprecipitation

Knockdown of E-cadherin expression promotes cervical cancer cell proliferation through ERK signaling. (A) SiHa and SNU-17 cells (2×105) were plated on six-well plates and then cells were transfected with siRNA against E-cadherin. At 24 h intervals, cells were harvested and counted. (B) SiHa and SNU-17 cells transfected with siE-cadherin were treated with DMSO or 20 μM PD98059 for 24 h. Protein expression of E-cadherin, P-ERK, ERK, and α-actinin was analyzed by western blot. (C) SiHa and SNU-17 cells were transfected with siRNA against E-cadherin for 24 h and then treated with DMSO or 20 μM PD98059 for an additional 24 h. 72 h after seeding the cells, cells were dissociated and counted.

Journal: Cancer Genomics & Proteomics

Article Title: Loss of E‐cadherin Activates EGFR‐MEK/ERK Signaling, Promoting Cervical Cancer Progression

doi: 10.21873/cgp.20501

Figure Lengend Snippet: Knockdown of E-cadherin expression promotes cervical cancer cell proliferation through ERK signaling. (A) SiHa and SNU-17 cells (2×105) were plated on six-well plates and then cells were transfected with siRNA against E-cadherin. At 24 h intervals, cells were harvested and counted. (B) SiHa and SNU-17 cells transfected with siE-cadherin were treated with DMSO or 20 μM PD98059 for 24 h. Protein expression of E-cadherin, P-ERK, ERK, and α-actinin was analyzed by western blot. (C) SiHa and SNU-17 cells were transfected with siRNA against E-cadherin for 24 h and then treated with DMSO or 20 μM PD98059 for an additional 24 h. 72 h after seeding the cells, cells were dissociated and counted.

Article Snippet: Small interfering RNA (siRNA) transfection. siRNAs specific for E-cadherin were procured from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

Techniques: Knockdown, Expressing, Transfection, Western Blot