Journal: Experimental and Therapeutic Medicine

Article Title: Expression of N-cadherin proteins in myocardial hypertrophy in rats

doi: 10.3892/etm.2013.1431

Figure Lengend Snippet: Oligonucleotide primers of N-cadherin and β-actin.

Article Snippet: Primary antibodies of N-cadherin (1:100; Wuhan Boster Biological Technology Ltd., Wuhan, China) were incubated overnight at 4°C and subsequently incubated at 37°C for 30 min in biotin-labeled IgG and streptavidin-biotin complex liquid.

Techniques:

Journal: Experimental and Therapeutic Medicine

Article Title: Expression of N-cadherin proteins in myocardial hypertrophy in rats

doi: 10.3892/etm.2013.1431

Figure Lengend Snippet: N-cadherin expression in the myocardial tissue by immunohistochemical method. (A) Control group. (B) Experimental group. Magnification, ×400.

Article Snippet: Primary antibodies of N-cadherin (1:100; Wuhan Boster Biological Technology Ltd., Wuhan, China) were incubated overnight at 4°C and subsequently incubated at 37°C for 30 min in biotin-labeled IgG and streptavidin-biotin complex liquid.

Techniques: Expressing, Immunohistochemical staining, Control

Journal: Experimental and Therapeutic Medicine

Article Title: Expression of N-cadherin proteins in myocardial hypertrophy in rats

doi: 10.3892/etm.2013.1431

Figure Lengend Snippet: Comparison of the average area and brightness of N-cadherin expression in the myocardium (mean ± standard deviation).

Article Snippet: Primary antibodies of N-cadherin (1:100; Wuhan Boster Biological Technology Ltd., Wuhan, China) were incubated overnight at 4°C and subsequently incubated at 37°C for 30 min in biotin-labeled IgG and streptavidin-biotin complex liquid.

Techniques: Comparison, Expressing, Control

Journal: Experimental and Therapeutic Medicine

Article Title: Expression of N-cadherin proteins in myocardial hypertrophy in rats

doi: 10.3892/etm.2013.1431

Figure Lengend Snippet: N-cadherin expression in the myocardial tissue by immunofluorescence method. (A) Control group. (B) Experimental group. Magnification, ×400.

Article Snippet: Primary antibodies of N-cadherin (1:100; Wuhan Boster Biological Technology Ltd., Wuhan, China) were incubated overnight at 4°C and subsequently incubated at 37°C for 30 min in biotin-labeled IgG and streptavidin-biotin complex liquid.

Techniques: Expressing, Immunofluorescence, Control

Journal: Experimental and Therapeutic Medicine

Article Title: Expression of N-cadherin proteins in myocardial hypertrophy in rats

doi: 10.3892/etm.2013.1431

Figure Lengend Snippet: Reverse transcription polymerase chain reaction; products of N-cadherin. M, Marker; 1–2, experimental group; 3–4, control group.

Article Snippet: Primary antibodies of N-cadherin (1:100; Wuhan Boster Biological Technology Ltd., Wuhan, China) were incubated overnight at 4°C and subsequently incubated at 37°C for 30 min in biotin-labeled IgG and streptavidin-biotin complex liquid.

Techniques: Reverse Transcription, Polymerase Chain Reaction, Marker, Control

Journal: PLoS ONE

Article Title: Identification of Tyrosine-9 of MAVS as Critical Target for Inducible Phosphorylation That Determines Activation

doi: 10.1371/journal.pone.0041687

Figure Lengend Snippet: (A) HEK293T cells were transfected with increasing amount of Flag-vector, Flag-WT or Flag-Y9F mutant. Cells were harvested for Trypan Blue counting 48 h post-transfection. Data are mean of three independent experiments ± SEM done in triplicate. (B) HEK293T cells were transfected with 1.0 µg expression vector encoding Flag-vector, Flag-WT or Flag-Y9F mutant. Annexin V assays were performed 48 hours post-transfection.

Article Snippet: Annexin V staining was performed as indicated with the Annexin V-Biotin Apoptosis Detection Kit (BD Bioscience).

Techniques: Transfection, Plasmid Preparation, Mutagenesis, Expressing

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Derivation of Endothelial Cells From Human Embryonic Stem Cells by Directed Differentiation

doi: 10.1161/atvbaha.110.204800

Figure Lengend Snippet: Figure 1. Taqman low-density array (TLDA) analysis of mRNA levels in pluri- potent hESCs and cells subjected to directed differentiation to vascular endo- thelial cells. hESCs were either main- tained under pluripotency conditions or under feeder- and serum-free monolayer-directed differentiation to vas- cular endothelial cells over 21 days. TLDA analysis was performed on extracted mRNA at different time points. A, Markers shown: pluripotency- associated mRNAs: Nanog, Oct 4, and Sox 2, with significant reduction in expression observed with progression of differentiation. B, early mesoderm mark- ers (brachyury, NKX2.5, Mesp1, and Mixl1) vascular endothelial cells (FLT-1, KDR, CD31, VE-cadherin, and CD34). Data are given as the meanSEM. * P0.05, **P0.01, and ***P0.001 vs the time-matched pluripotent sample. Supplemental Table I provides the data for complete TLDA analysis.

Article Snippet: Cells were incubated at 4°C overnight with the following antibodies: mouse IgG monoclonal anti–human OCT4 (1:200; Santa Cruz Biotechnology, Inc, Heidelberg, Germany); mouse IgG monoclonal anti–human Nanog (1:200; Abcam plc, Cambridge, England); mouse IgG monoclonal anti–human CD31 (1:100; Dako UK Ltd, Ely, England); and goat IgG polyclonal VE-cadherin (1:100; R&D Systems).

Techniques: TLDA Assay, Expressing

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Derivation of Endothelial Cells From Human Embryonic Stem Cells by Directed Differentiation

doi: 10.1161/atvbaha.110.204800

Figure Lengend Snippet: Figure 2. Expression of endothelial and angiogenesis-related proteins. A, FACS analysis and immunocytofluorescent staining of endothelial marker proteins. Increasing positive expression of CD31 (FL1 and far panel) and VE-cadherin (FL2 and middle panel) observed in a time-dependent manner to 21-day differen- tiation, using 4,6-diamidino-2-phenylindole (DAPI) (nuclear counterstain [blue]) (scale bar indicates 20 m). Representative scans and images from 3 independent experiments. B, Mem- brane scans of angiogenic markers in differentiated hESC-ECs (days 0, 10, 14, and 21 of differentiation). Array images are from 10-minute exposure to x-ray film. Supplemental Figure III pro- vides the corresponding densometric analysis.

Article Snippet: Cells were incubated at 4°C overnight with the following antibodies: mouse IgG monoclonal anti–human OCT4 (1:200; Santa Cruz Biotechnology, Inc, Heidelberg, Germany); mouse IgG monoclonal anti–human Nanog (1:200; Abcam plc, Cambridge, England); mouse IgG monoclonal anti–human CD31 (1:100; Dako UK Ltd, Ely, England); and goat IgG polyclonal VE-cadherin (1:100; R&D Systems).

Techniques: Expressing, Staining, Marker

Journal: Oncotarget

Article Title: JNK inhibitor alleviates apoptosis of fetal neural stem cells induced by emulsified isoflurane

doi: 10.18632/oncotarget.21505

Figure Lengend Snippet: (A) Cells were treated with different concentrations of EI and cultured for 12hr, then analyzed by flow cytometry. (B) Annexin V-FITC and PI staining after EI treatment. Cells were treated with EI for 12hr. Annexin positive cell ratio of FNSCs after EI treatment and JNK blocker SP600125. (C) Inhibitory ratio of cell proliferation in all groups. (D) The level of p-JNK, JNK and Caspase3 was determined by immunoblot analysis. GAPDH was used as a loading control. (E, F) JNK inhibition by the specific inhibitor SP600125 rescued FNSCs from a decrease in survival and upregulated cell viability. JNK-dependent apoptosis was inhibited by JNK blocker SP600125. The expression of p-JNK and JNK protein in FNSCs was increased by EI in comparison with N group. (G) Caspase3 was activated by EI with immunoblot analysis. JNK blocker SP600125 can decrease the expression of Caspase3 in group EI2SP. All data were derived form results of three independent experiments. Values are expressed as the mean ± standard deviation (SD). * P <0.05, ** P <0.01, *** P <0.001. Normal group (group N), Intralipid group (group F), EI of 7.56mM (group EI1), EI of 9.52mM (group EI2), EI of 11.48mM (group EI3) and EI of 9.52mM plus SP600125 of 20μM (group EI2SP).

Article Snippet: Cells undergoing apoptosis at the indicated time were identified using FITC Annexin V Apoptosis Detection Kit (BD), following the manufacturer's instructions.

Techniques: Cell Culture, Flow Cytometry, Staining, Western Blot, Inhibition, Expressing, Derivative Assay, Standard Deviation

Journal: Cell Death & Disease

Article Title: Cell-cell contact-driven EphB1 cis- and trans- signalings regulate cancer stem cells enrichment after chemotherapy

doi: 10.1038/s41419-022-05385-5

Figure Lengend Snippet: A The heatmap of the expression of receptor tyrosine kinases (RTKs) genes between 3 cell phases induced by cisplatin; The final heatmap was plotted after being balanced by the Z -score. Z sores were calculated for each row (each gene) by subtracting the mean and dividing by the standard deviation. B RT-qPCR Validation of EphB1 expression. C Western blot analysis of EphB1 and p-EphB1 in cisplatin-treated A549 cells at different time points; D , E Assessment of p-EphB1 in lung cancer patients. Tumor biopsies were fixed and stained for p-EphB1. Scale bar = 20 μm; The immunohistochemical scores were shown on the right; Student’s t test, P values were shown. Primary tumor: biopsies from lung primary tumors; Chemo: biopsies from lung tumors after neoadjuvant chemotherapy; Metastasis: biopsies from metastatic brain of lung cancer patients; F Immunofluorescence images of lung cancer cells with different cell density. Cells were planted in 6-well plates at different cell density. Cells at different density were incubated with RFP-conjugated p-EphB1 antibody and GFP-conjugated EphB1 antibody. Cells were counterstained with DAPI. Scale bar = 20 μm; G Western blot analysis of proteins obtained from si-E-cadherin-treated A549 cells.

Article Snippet: Antibodies to proteins were obtained from the following sources: EphB1 (#ab129103) and phos-EphB1 (#ab61791) for Western blot were purchased from Abcam; EphB1 (#AF542) for immunohistochemistry was purchased from Novus Biologicals; Ki67, p53, CyclinA2 and E-cadherin (#3195) were from Cell Signaling Technology; β-actin (#60008-1-Ig) and GAPDH (#60004-1-Ig) were from Proteintech.

Techniques: Expressing, Standard Deviation, Quantitative RT-PCR, Biomarker Discovery, Western Blot, Staining, Immunohistochemical staining, Immunofluorescence, Incubation

Journal: Cell Death & Disease

Article Title: Cell-cell contact-driven EphB1 cis- and trans- signalings regulate cancer stem cells enrichment after chemotherapy

doi: 10.1038/s41419-022-05385-5

Figure Lengend Snippet: A Schematic diagram of mutants. Four construct mutants were constructed including mutants that lack the fibronectin type III domain (FNΔ), that lack cysteine-rich region (CRDΔ), that lack ligand-binding domain (LBDΔ) or Y594 phosphorylation site mutation (Y594Δ); B Western blot analysis. The expression of EphB1, p-EphB1, p38, p-p38 and E-cadherin was evaluated after transfected with EphB1 wt and mutants or co-transfection of EphB1 and Efnb2; C The phosphorylation levels were evaluated by the ratio of phosphorylated EphB1 and total EphB1. D Transwell migration and invasion assays after co-transfection of EphB1 and Efnb2; E Cell cycle analysis after co-transfection of EphB1 and Efnb2. F Protein–protein interactions between EphB1, EfnB2 and p38. GFP/EphB1 was transfected into A549 cells and co-immunoprecipitation was performed using an anti-GFP antibody to characterize protein–protein interactions. G Colocalization of EphB1 and E-cadherin. Immunofluorescent images of E-cadherin and EphB1. The transfection of EphB1 constructs expresses fusion GFP. Red fluorescence indicates E-cadherin staining and green fluorescence indicates EphB1. Images were taken at ×100 magnification and scale bar indicates 100 μm.

Article Snippet: Antibodies to proteins were obtained from the following sources: EphB1 (#ab129103) and phos-EphB1 (#ab61791) for Western blot were purchased from Abcam; EphB1 (#AF542) for immunohistochemistry was purchased from Novus Biologicals; Ki67, p53, CyclinA2 and E-cadherin (#3195) were from Cell Signaling Technology; β-actin (#60008-1-Ig) and GAPDH (#60004-1-Ig) were from Proteintech.

Techniques: Construct, Ligand Binding Assay, Phospho-proteomics, Mutagenesis, Western Blot, Expressing, Transfection, Cotransfection, Migration, Cell Cycle Assay, Protein-Protein interactions, Immunoprecipitation, Fluorescence, Staining

Journal: Cell Death & Disease

Article Title: Cell-cell contact-driven EphB1 cis- and trans- signalings regulate cancer stem cells enrichment after chemotherapy

doi: 10.1038/s41419-022-05385-5

Figure Lengend Snippet: A549 cells were seeded at low density in sphere medium in ultra-low attachment cell plates. Formed spheres were observed after 14 days. A Representative images of sphere-forming cells. Western blot assay was used to evaluate the expression EphB1, p-EphB1 and E-cadherin in sphere-forming cells. B Western blot analysis of cells after treatment of EphrinB2-Fc. C Flow cytometry analysis for stem cell surface marker CD133. The histogram graph was shown in ( D ). E Western blot analysis. The expression of Nanog and Sox2 was evaluated after transfected with EphB1 wt and mutants or Co-transfection of EphB1 and EfnB2.

Article Snippet: Antibodies to proteins were obtained from the following sources: EphB1 (#ab129103) and phos-EphB1 (#ab61791) for Western blot were purchased from Abcam; EphB1 (#AF542) for immunohistochemistry was purchased from Novus Biologicals; Ki67, p53, CyclinA2 and E-cadherin (#3195) were from Cell Signaling Technology; β-actin (#60008-1-Ig) and GAPDH (#60004-1-Ig) were from Proteintech.

Techniques: Western Blot, Expressing, Flow Cytometry, Marker, Transfection, Cotransfection

Journal: Cell Death & Disease

Article Title: Cell-cell contact-driven EphB1 cis- and trans- signalings regulate cancer stem cells enrichment after chemotherapy

doi: 10.1038/s41419-022-05385-5

Figure Lengend Snippet: A In the dormant EMT cells which showed disrupted cell-cell contacts, ligand-independent EphB1 promoted entry of lung cancer cells into G0-G1 phase of cell cycle through activating p-p38 and downregulating E-cadherin; B Interaction of cell-contact-mediated cis- and trans-signalings. Disruption of cis-signaling activates trans-signaling; C Disruption of trans-signaling inhibits EphB1 forward signaling; D In the state of MET, in which cell-cell adhesion was recovered, interactions of EphB1 and ligand EphrinB2 in trans promoted the stemness of cancer cells through upregulating Nanog and Sox2.

Article Snippet: Antibodies to proteins were obtained from the following sources: EphB1 (#ab129103) and phos-EphB1 (#ab61791) for Western blot were purchased from Abcam; EphB1 (#AF542) for immunohistochemistry was purchased from Novus Biologicals; Ki67, p53, CyclinA2 and E-cadherin (#3195) were from Cell Signaling Technology; β-actin (#60008-1-Ig) and GAPDH (#60004-1-Ig) were from Proteintech.

Techniques: Disruption

Journal: Molecular Medicine Reports

Article Title: NLRP3 inflammasome inactivation driven by miR-223-3p reduces tumor growth and increases anticancer immunity in breast cancer

doi: 10.3892/mmr.2019.9889

Figure Lengend Snippet: sh-NLRP3 inhibits the growth and migration of human breast cancer cells MCF-7 in vitro . (A) Percentage of apoptotic cells in three groups was detected by performing Hoechst staining. White arrows, nucleus (magnification, ×400). (B) Cell migration measured by Transwell analysis (magnification, ×400). (C) Protein expression levels of Ki67 and VEGF were detected by western blotting. (D) Proliferation of breast cancer cells following treatment with sh-NLRP3 and with sh-Ctrl was measured by Cell Counting kit-8. *P<0.05 vs. respective MCF-7. NLRP3, NACHT, LRR and PYD domains-containing protein 3; sh, short hairpin; VEGF, vascular endothelial growth factor; Ctrl, control; Ki67, proliferation marker protein Ki67.

Article Snippet: Subsequently, the membranes were incubated overnight at 4°C with anti-NLRP3 (15101; 1:500), anti-proliferation marker protein Ki67 (9129; 1:1,000; Ki67; both CST Biological Reagents Co., Ltd., Shanghai, China), anti-vascular endothelial growth factor (VEGF; ab32152; 1:500 Abcam, Cambridge, UK), anti-PYD and CARD domain-containing protein (ASC; sc-271054; 1:500; Santa Cruz Biotechnology, Inc., Dallas, TX, USA), anti-IL-1β (ab200478; 1:500), anti-IL-18 (ab71495; 1:500; both Abcam) and anti-GAPDH (35174.; 1:1,000) primary antibodies, followed by incubation with secondary antibody conjugated to horseradish peroxidase (7074; 1:1,000; both CST Biological Reagents Co., Ltd.) at room tempreture for 2 h. Following washing with TBS, proteins were visualized using enhanced chemiluminescence reagents Rabbit IgG (Pierce; Thermo Fisher Scientific, Inc.), according to the manufacturer's protocol.

Techniques: Migration, In Vitro, Staining, Expressing, Western Blot, Cell Counting, Control, Marker

Journal: Molecular Medicine Reports

Article Title: NLRP3 inflammasome inactivation driven by miR-223-3p reduces tumor growth and increases anticancer immunity in breast cancer

doi: 10.3892/mmr.2019.9889

Figure Lengend Snippet: miR-233 suppresses the growth and migration of human breast cancer cells by inactivating the NLRP3 pathway. (A) Cell migration was measured by Transwell assays (magnification, ×400). (B) Ki67 and VEGF protein expression levels were detected by western blotting. (C) Cell proliferation of breast cancer cells following transfection with miR-223 mimics and pc-NLRP3 was measured by Cell Counting kit-8. (D) Protein expression levels of ASC, IL-1β and IL-18 were detected by western blotting. *P<0.05. miR, microRNA; NLRP3, NACHT, LRR and PYD domains-containing protein 3; IL-, interleukin; ASC, PYD and CARD domain-containing protein; VEGF, vascular endothelial growth factor; Ki67, proliferation marker protein Ki67; scram, scramble.

Article Snippet: Subsequently, the membranes were incubated overnight at 4°C with anti-NLRP3 (15101; 1:500), anti-proliferation marker protein Ki67 (9129; 1:1,000; Ki67; both CST Biological Reagents Co., Ltd., Shanghai, China), anti-vascular endothelial growth factor (VEGF; ab32152; 1:500 Abcam, Cambridge, UK), anti-PYD and CARD domain-containing protein (ASC; sc-271054; 1:500; Santa Cruz Biotechnology, Inc., Dallas, TX, USA), anti-IL-1β (ab200478; 1:500), anti-IL-18 (ab71495; 1:500; both Abcam) and anti-GAPDH (35174.; 1:1,000) primary antibodies, followed by incubation with secondary antibody conjugated to horseradish peroxidase (7074; 1:1,000; both CST Biological Reagents Co., Ltd.) at room tempreture for 2 h. Following washing with TBS, proteins were visualized using enhanced chemiluminescence reagents Rabbit IgG (Pierce; Thermo Fisher Scientific, Inc.), according to the manufacturer's protocol.

Techniques: Migration, Expressing, Western Blot, Transfection, Cell Counting, Marker

Journal: Molecular Medicine Reports

Article Title: NLRP3 inflammasome inactivation driven by miR-223-3p reduces tumor growth and increases anticancer immunity in breast cancer

doi: 10.3892/mmr.2019.9889

Figure Lengend Snippet: NLRP3 inflammasome inactivation driven by miR-233 reduces the development of tumors in vivo . (A) Tumor volume was measured by subcutaneously injecting MCF-7 cells transfected with miR-223 mimics into nude mice. (B) Survival curve of nude mice was measured for 25 days. (C) Expression level of TUNEL, Ki67 and VEGF were detected by immunohistochemistry (magnification, ×400). (D) Protein expression levels of NLRP3 and ASC were detected by western blotting. (E) Concentrations of IL-1β, IL-18 and IL-10 were detected by ELISA. *P<0.05 vs. respective MCF-7. NLRP3, NACHT, LRR and PYD domains-containing protein 3; IL-, interleukin; ASC, PYD and CARD domain containing protein; TUNEL, terminal deoxynucleotidyl transferase dUTP nick end labeling; miR, microRNA; Ki67, proliferation marker protein Ki67; scram, scramble.

Article Snippet: Subsequently, the membranes were incubated overnight at 4°C with anti-NLRP3 (15101; 1:500), anti-proliferation marker protein Ki67 (9129; 1:1,000; Ki67; both CST Biological Reagents Co., Ltd., Shanghai, China), anti-vascular endothelial growth factor (VEGF; ab32152; 1:500 Abcam, Cambridge, UK), anti-PYD and CARD domain-containing protein (ASC; sc-271054; 1:500; Santa Cruz Biotechnology, Inc., Dallas, TX, USA), anti-IL-1β (ab200478; 1:500), anti-IL-18 (ab71495; 1:500; both Abcam) and anti-GAPDH (35174.; 1:1,000) primary antibodies, followed by incubation with secondary antibody conjugated to horseradish peroxidase (7074; 1:1,000; both CST Biological Reagents Co., Ltd.) at room tempreture for 2 h. Following washing with TBS, proteins were visualized using enhanced chemiluminescence reagents Rabbit IgG (Pierce; Thermo Fisher Scientific, Inc.), according to the manufacturer's protocol.

Techniques: In Vivo, Transfection, Expressing, TUNEL Assay, Immunohistochemistry, Western Blot, Enzyme-linked Immunosorbent Assay, Marker

Journal: Frontiers in Immunology

Article Title: TOX Acts as a Tumor Suppressor by Inhibiting mTOR Signaling in Colorectal Cancer

doi: 10.3389/fimmu.2021.647540

Figure Lengend Snippet: TOX represses the EMT process. IHC shows assay E-cadherin (A) and vimentin (B) expression in CRC and para-CRC tissues ( n = 40). (C) Western blot shows EMT-related proteins ZEB1, E-cadherin, vimentin, and Snail expression in PLVX-Flag-TOX and PLVX-Flag SW1116 cells. (D) Western blot assay shows ZEB1, E-cadherin, vimentin, and Snail in shCK HCT116, shTOX-1 (sh1), and shTOX-2 (sh2) HCT116 cells. (E) qRT-PCR shows ZEB1, E-cadherin, vimentin, and Snail expression in PLVX-Flag-TOX, PLVX-Flag SW1116, shCK HCT116, shTOX-1 (sh1), and shTOX-2 (sh2) HCT116 cells. Each experiment was repeated three times. * p < 0.01, *** p < 0.001, **** p < 0.0001.

Article Snippet: Resolved proteins were transferred to polyvinylidene fluoride membranes and incubated with antibodies against TOX (#ab155768, 1:1,000; Abcam, USA), EMT markers (E-cadherin #3195, Snail #3879, and vimentin #5741, 1:1,000, CST, USA; ZEB1 #21544-1-AP, 1:1000 Proteintech, China), and PI3K/AKT/mTOR pathway molecules (p-PI3K #4228, PI3K #4249, p-AKT, AKT, mTOR #2983, p-mTOR #2974, 1:1,000; CST, USA).

Techniques: Expressing, Western Blot, Quantitative RT-PCR

Journal: Frontiers in Immunology

Article Title: TOX Acts as a Tumor Suppressor by Inhibiting mTOR Signaling in Colorectal Cancer

doi: 10.3389/fimmu.2021.647540

Figure Lengend Snippet: TOX acts as a tumor suppressor by inhibiting mTOR signaling in colorectal cancer. TOX acts as a CRC suppressor with decreasing expression and longer OS. TOX partly suppressed the mTOR signaling to inhibit cell proliferation, migration, invasion, and EMT process. Rapamycin alone or combined with PD1 inhibitor has therapeutic potential in CRC.

Article Snippet: Resolved proteins were transferred to polyvinylidene fluoride membranes and incubated with antibodies against TOX (#ab155768, 1:1,000; Abcam, USA), EMT markers (E-cadherin #3195, Snail #3879, and vimentin #5741, 1:1,000, CST, USA; ZEB1 #21544-1-AP, 1:1000 Proteintech, China), and PI3K/AKT/mTOR pathway molecules (p-PI3K #4228, PI3K #4249, p-AKT, AKT, mTOR #2983, p-mTOR #2974, 1:1,000; CST, USA).

Techniques: Expressing, Migration