cyclin a ir115 antibody Search Results


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iReal Biotechnology Inc cyclin a ir115 antibody
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p21  (Bio-Rad)
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Bio-Rad p21
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Santa Cruz Biotechnology gapdh
Figure <t>7.</t> <t>MSN</t> upregulated RUNX2 expression in CRC cells. Expression levels of MSN and RUNX2 were determined through RT-qPCR. (A) Silencing of MSN reduced the expression of RUNX2 in HCT 116 cells. (B) The nuclear translocation of β-catenin was determined through Western blotting of cytoplasmic and nuclear extracts. PARP and <t>GAPDH</t> were used as loading controls for nuclear and cytoplasmic fractions, respectively. (C) Levels of Phospho-GSK3β-S9 and total GSK3β were determined in vector and MSN over DLD-1 cells through Western blotting. GAPDH is shown as a loading control. RUNX2 and MMP9 were evaluated through RT-qPCR in the presence of β-catenin inhibitors, ICG-001 and PKF118-310, in HCT 116 cells (D) and vector and MSN-overexpressing DLD-1 cells (E). RUNX2 expression was determined through RT-qPCR in scrambled control and MSN-KD HCT 116 cells after treatment with a GSK3β inhibitor, TWS 119 treatment (F). * p < 0.05, ** p < 0.01.
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Cell Signaling Technology Inc e cadherin
Figure <t>7.</t> <t>MSN</t> upregulated RUNX2 expression in CRC cells. Expression levels of MSN and RUNX2 were determined through RT-qPCR. (A) Silencing of MSN reduced the expression of RUNX2 in HCT 116 cells. (B) The nuclear translocation of β-catenin was determined through Western blotting of cytoplasmic and nuclear extracts. PARP and <t>GAPDH</t> were used as loading controls for nuclear and cytoplasmic fractions, respectively. (C) Levels of Phospho-GSK3β-S9 and total GSK3β were determined in vector and MSN over DLD-1 cells through Western blotting. GAPDH is shown as a loading control. RUNX2 and MMP9 were evaluated through RT-qPCR in the presence of β-catenin inhibitors, ICG-001 and PKF118-310, in HCT 116 cells (D) and vector and MSN-overexpressing DLD-1 cells (E). RUNX2 expression was determined through RT-qPCR in scrambled control and MSN-KD HCT 116 cells after treatment with a GSK3β inhibitor, TWS 119 treatment (F). * p < 0.05, ** p < 0.01.
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Santa Cruz Biotechnology β catenin
Figure <t>7.</t> <t>MSN</t> upregulated RUNX2 expression in CRC cells. Expression levels of MSN and RUNX2 were determined through RT-qPCR. (A) Silencing of MSN reduced the expression of RUNX2 in HCT 116 cells. (B) The nuclear translocation of β-catenin was determined through Western blotting of cytoplasmic and nuclear extracts. PARP and <t>GAPDH</t> were used as loading controls for nuclear and cytoplasmic fractions, respectively. (C) Levels of Phospho-GSK3β-S9 and total GSK3β were determined in vector and MSN over DLD-1 cells through Western blotting. GAPDH is shown as a loading control. RUNX2 and MMP9 were evaluated through RT-qPCR in the presence of β-catenin inhibitors, ICG-001 and PKF118-310, in HCT 116 cells (D) and vector and MSN-overexpressing DLD-1 cells (E). RUNX2 expression was determined through RT-qPCR in scrambled control and MSN-KD HCT 116 cells after treatment with a GSK3β inhibitor, TWS 119 treatment (F). * p < 0.05, ** p < 0.01.
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Cell Signaling Technology Inc n cadherin
Figure <t>7.</t> <t>MSN</t> upregulated RUNX2 expression in CRC cells. Expression levels of MSN and RUNX2 were determined through RT-qPCR. (A) Silencing of MSN reduced the expression of RUNX2 in HCT 116 cells. (B) The nuclear translocation of β-catenin was determined through Western blotting of cytoplasmic and nuclear extracts. PARP and <t>GAPDH</t> were used as loading controls for nuclear and cytoplasmic fractions, respectively. (C) Levels of Phospho-GSK3β-S9 and total GSK3β were determined in vector and MSN over DLD-1 cells through Western blotting. GAPDH is shown as a loading control. RUNX2 and MMP9 were evaluated through RT-qPCR in the presence of β-catenin inhibitors, ICG-001 and PKF118-310, in HCT 116 cells (D) and vector and MSN-overexpressing DLD-1 cells (E). RUNX2 expression was determined through RT-qPCR in scrambled control and MSN-KD HCT 116 cells after treatment with a GSK3β inhibitor, TWS 119 treatment (F). * p < 0.05, ** p < 0.01.
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Image Search Results


Figure 7. MSN upregulated RUNX2 expression in CRC cells. Expression levels of MSN and RUNX2 were determined through RT-qPCR. (A) Silencing of MSN reduced the expression of RUNX2 in HCT 116 cells. (B) The nuclear translocation of β-catenin was determined through Western blotting of cytoplasmic and nuclear extracts. PARP and GAPDH were used as loading controls for nuclear and cytoplasmic fractions, respectively. (C) Levels of Phospho-GSK3β-S9 and total GSK3β were determined in vector and MSN over DLD-1 cells through Western blotting. GAPDH is shown as a loading control. RUNX2 and MMP9 were evaluated through RT-qPCR in the presence of β-catenin inhibitors, ICG-001 and PKF118-310, in HCT 116 cells (D) and vector and MSN-overexpressing DLD-1 cells (E). RUNX2 expression was determined through RT-qPCR in scrambled control and MSN-KD HCT 116 cells after treatment with a GSK3β inhibitor, TWS 119 treatment (F). * p < 0.05, ** p < 0.01.

Journal: International journal of molecular sciences

Article Title: Identification of Moesin (MSN) as a Potential Therapeutic Target for Colorectal Cancer via the β-Catenin-RUNX2 Axis.

doi: 10.3390/ijms241310951

Figure Lengend Snippet: Figure 7. MSN upregulated RUNX2 expression in CRC cells. Expression levels of MSN and RUNX2 were determined through RT-qPCR. (A) Silencing of MSN reduced the expression of RUNX2 in HCT 116 cells. (B) The nuclear translocation of β-catenin was determined through Western blotting of cytoplasmic and nuclear extracts. PARP and GAPDH were used as loading controls for nuclear and cytoplasmic fractions, respectively. (C) Levels of Phospho-GSK3β-S9 and total GSK3β were determined in vector and MSN over DLD-1 cells through Western blotting. GAPDH is shown as a loading control. RUNX2 and MMP9 were evaluated through RT-qPCR in the presence of β-catenin inhibitors, ICG-001 and PKF118-310, in HCT 116 cells (D) and vector and MSN-overexpressing DLD-1 cells (E). RUNX2 expression was determined through RT-qPCR in scrambled control and MSN-KD HCT 116 cells after treatment with a GSK3β inhibitor, TWS 119 treatment (F). * p < 0.05, ** p < 0.01.

Article Snippet: The membranes were probed using the following primary antibodies at 4 ◦C overnight: GAPDH (sc-32233, Santa Cruz Biotechnology, Dallas, TX, USA), MSN (ab52490, Abcam PLC, Cambridge, UK), cyclin A (iR115, iReal Biotechnology Co., Hsinchu City, Taiwan), cyclin B (GTX10091), cyclin D (iR117-294, iReal Biotechnology Co., Hsinchu City, Taiwan), p21 (MCA2325, Bio-Rad Laboratories, Hercules, CA, USA), fibronectin (sc9068, Santa Cruz Biotechnology, Santa Cruz, CA, USA), N-cadherin (13116, Cell Signaling Technology, Danvers, MA, USA), vimentin (iR45-137, iReal Biotechnology Co., Hsinchu City, Taiwan), E-cadherin (3195, Cell Signaling Technology, Danvers, MA, USA), β-catenin (sc-7963, Santa Cruz Biotechnology, Santa Cruz, CA, USA), and PARP (sc-25780, Santa Cruz Biotechnology, Santa Cruz, CA, USA).

Techniques: Expressing, Quantitative RT-PCR, Translocation Assay, Western Blot, Plasmid Preparation, Control