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Image Search Results
Journal: Journal of Cellular and Molecular Medicine
Article Title: MicroRNA‐30e‐5p promotes cell growth by targeting PTPN13 and indicates poor survival and recurrence in lung adenocarcinoma
doi: 10.1111/jcmm.13198
Figure Lengend Snippet: PTPN13 rescued tumour proliferation‐promoting effects by miR‐30e. ( A and B ) The effects of PTPN13 overexpression on cell proliferation in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by MTT assay. ( C and D ) The effects of PTPN13 overexpression on the protein expression of EGFR/AKT pathway in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by western blotting. ( E and F ) The effects of PTPN13 knockdown on the protein expression of EGFR/AKT pathway in sh‐miR‐30e‐transfected A549 and NCI‐H23 cells indicated by Western blotting.
Article Snippet: Lentivirus‐mediated miR‐30e overexpression, miR‐30e shRNA and PTPN13 overexpression vectors, negative control vector (NC) and virion‐packaging elements were from Genechem (Shanghai, China); The primary antibodies of PTPN13 (rabbit monoclonal antibody, ab198882), β‐actin (mouse monoclonal antibody, ab8226),
Techniques: Over Expression, Transfection, MTT Assay, Expressing, Western Blot
Journal: Scientific Reports
Article Title: Altered PTPN13–β-catenin interaction by pathogenic mutations and involvement of this axis in B-cell receptor signalling
doi: 10.1038/s41598-025-33151-y
Figure Lengend Snippet: Analysis of the interaction between β-catenin and PTPN13. β-catenin levels were analysed in T cells from a healthy control and patients from two different families harbouring PTPN13 mutations: Family A, carrying a homozygous p.R1838Q mutation (A-1), and Family B, carrying heterozygous p.W1274C and p.S1004del mutations (B-1, B-2). A representative Western blot is shown in ( A ), while the quantification of five independent experiments is presented in ( B ). ( C ) Schematic representation of the modular structure of β-catenin and the constructs used in the in vitro protein interaction experiments: full-length β-catenin (blue line), a construct lacking the C-terminal region (β-catenin ΔC, green line), and a construct containing only the C-terminal region (β-catenin C-terminal, boxed in purple). ( D ) Schematic representation of the modular structure of PTPN13 and the constructs used: full-length PTPN13, the N-terminal region including the KIND and FERM domains (boxed in orange), the central region containing the five PDZ domains (boxed in pink), and the C-terminal region containing the PTP domain (boxed in grey). The interaction between β-catenin and PTPN13 was assessed by pull-down assays as described in the Methods section. ( E ) Representative experiment showing the interaction between full-length PTPN13 and the three β-catenin constructs. The input extract is shown in the first lane, followed by the pull-down interaction in the subsequent lanes. ( F ) Quantification of these experiments. ( G ) Representative experiment demonstrating the interaction between full-length β-catenin and the four PTPN13 constructs. The upper panel shows the pull-down interaction, and the lower panel displays the corresponding input. ( H ) Quantification of these experiments. Anti-HA was used to detect (E–G) and quantify PTPN13 signals (F–H), as all constructs carry this tag. The arrowhead indicates the expected size of the PTPN13 construct. Statistically significant differences relative to the corresponding control (black column) are indicated as follows: *** p < 0.001 and ** p < 0.01. Cropped blots are shown for clarity. Original blots are presented in the Supplementary File.
Article Snippet: Commercial primary antibodies were obtained from the following sources: Becton Dickinson – anti-β-catenin (#610154), anti-BTK (#611116), anti-phospho-ERK (pT202/pY204) (#612358); Cell Signaling Technology – anti-phospho-BTK (pY223) (#5082S), anti-phospho-PLCγ2 (pY1217) (#3871S);
Techniques: Control, Mutagenesis, Western Blot, Construct, In Vitro