N Cadherin Antibody - #AF5239

Fig. 5 Restoration of BIRC2 expression reverses the inhibitory effect of BRD7 on cell migration and invasion. A Scratch wound healing analysis of cell migration in 5-8 F and HNE1 cells stably with BRD7 overexpression, BRD7 and BIRC2 simultaneous overexpression or control. Quantification of the wound recovery rate of the three groups (right). B Matrigel invasion analysis of cell invasive capabilities in 5-8 F and HNE1 cells stably with BRD7 overexpression, BRD7 and BIRC2 simultaneous overexpression or control. C Significantly differently expressed proteins involved in EMT progression (E-cadherin, N-cadherin, Vimentin, ZO-1) in BRD7 overexpression, BIRC2 overexpression and BIRC2 restoration cells, respectively. GAPDH served as an internal control. Error bars represent the mean ± SD. *P 

FIGURE 4 MDK affects the ubiquitination modification of c-Myc and the Wnt/β-catenin signalling pathway. (A–C) Results from proteomic analysis indicated that MDK affected the Wnt/β-catenin signalling pathway and protein ubiquitination. The raw data are shown in Table S8. (A) Volcano plot analysis results showed differentially expressed proteins (Table S9). The red dots represent upregulated expression in the siMDK group compared with the control group, and the yellow dots represent downregulated expression in the siMDK group compared with the control group. (B) Cluster analysis results showed similarities and differences among the groups (control vs. siMDK) and the stability of the mass spectrometry results of the three repeated experiments (Table S10). (C) KEGG pathway enrichment analysis revealed the signalling pathway affected by MDK knockdown (Table S11). (D) After treatment with 10 mM MG132 for 4 h, siMDK-U118MG and siMDK-SF126 cell lysates were immunoprecipitated with c-Myc and immunoblotted with ubiquitination antibodies. (E) After treatment with 10 mM MG132 for 4 h, OE-MDK-SHG44 and OE-MDK-U87 cell lysates were immunoprecipitated with c-Myc and immunoblotted with ubiquitination antibodies. (F–G) 50 mg/mL cycloheximide was added (at different time points: 0, 2, 4, 6, and 8 h) to glioma cells transfected with siRNA to block protein synthesis. The expression of c-Myc was then detected by Western blot. (H) MDK knockdown was performed on SF126, U118MG, and U251, and then a Western blot was used to detect the Wnt/β-catenin signalling pathway and EMT pathway markers. (I) MDK was overexpressed in U87, BT325, and SHG44, and Western blot was used to detect the Wnt/β-catenin signalling pathway and EMT pathway markers.

FIGURE 4 MDK affects the ubiquitination modification of c-Myc and the Wnt/β-catenin signalling pathway. (A–C) Results from proteomic analysis indicated that MDK affected the Wnt/β-catenin signalling pathway and protein ubiquitination. The raw data are shown in Table S8. (A) Volcano plot analysis results showed differentially expressed proteins (Table S9). The red dots represent upregulated expression in the siMDK group compared with the control group, and the yellow dots represent downregulated expression in the siMDK group compared with the control group. (B) Cluster analysis results showed similarities and differences among the groups (control vs. siMDK) and the stability of the mass spectrometry results of the three repeated experiments (Table S10). (C) KEGG pathway enrichment analysis revealed the signalling pathway affected by MDK knockdown (Table S11). (D) After treatment with 10 mM MG132 for 4 h, siMDK-U118MG and siMDK-SF126 cell lysates were immunoprecipitated with c-Myc and immunoblotted with ubiquitination antibodies. (E) After treatment with 10 mM MG132 for 4 h, OE-MDK-SHG44 and OE-MDK-U87 cell lysates were immunoprecipitated with c-Myc and immunoblotted with ubiquitination antibodies. (F–G) 50 mg/mL cycloheximide was added (at different time points: 0, 2, 4, 6, and 8 h) to glioma cells transfected with siRNA to block protein synthesis. The expression of c-Myc was then detected by Western blot. (H) MDK knockdown was performed on SF126, U118MG, and U251, and then a Western blot was used to detect the Wnt/β-catenin signalling pathway and EMT pathway markers. (I) MDK was overexpressed in U87, BT325, and SHG44, and Western blot was used to detect the Wnt/β-catenin signalling pathway and EMT pathway markers.

Fig. 8 TRIML2 knockdown inhibits the proliferation, migration, and invasion of HNSC cells. (A, B) Western blot and RT-qPCR were used to validate the knockdown efficiency of TRIML2 in HNSC cell lines. (C-F) The proliferative ability was assessed by CCK-8 and EdU assays. (G-H) Migration and invasion ability were measured by wound-healing and transwell assays. (I) the canonical wnt and EMT-related proteins were detected by Western blot after TRIML2 knockdown. All in vitro experiments were performed in at least three independent replicates. The data are presented as the mean ± SD.

Fig. 9 From: CDH3 promotes the progression of lung adenocarcinoma through driving epithelial-mesenchymal transition progress CDH3 knockdown suppressed LUAD malignant phenotype and inhibited pathological EMT. (A) Cell proliferation analysis in CDH3 knockdown HCC827 and H1975 cell lines using CCK8 assay (n = 3). (B) The quantification and representative images of colony formation assays for CDH3 knockdown HCC827 and H1975 cell lines (t-test, n = 3). (C) The quantification and representative images of EdU assays for CDH3 knockdown HCC827 and H1975 cell lines (t-test, n = 3). (D) The quantification and representative images of wound healing assays for CDH3 knockdown HCC827 and H1975 cell lines. (t-test, n = 3). (E) Western blot was used to evaluate the expression levels of the EMT-related markers in for CDH3 knockdown HCC827 and H1975 cell lines. (F-H)Subcutaneous tumors developed from CDH3 knockdown HCC827 cells and control cells.

Fig. 1: The siRNA-KDM6B inhibited the migration of BMSCs in vitro. A The knockdown efficiency of KDM6B was verified by qRT-PCR. B, C The siRNA-KDM6B inhibited the protein expression of migration-related genes (N cadherin and CXCR4). D, E The IF showed the expression of CXCR4 was inhibited by siRNA-KDM6B. F, G The siRNA-KDM6B inhibited the actin cortical protrusions formation of BMSCs. H, I The scratch test showed that siRNA-KDM6B decreased the migration area of BMSCs. J, K Transwell test verified that siRNA-KDM6B inhibited the migrated MSCs number. (si-1: siKDM6B-1, si-2: siKDM6B-2, si-3: siKDM6B-3. *P