anti foxj1 antibodies  (Boster Bio)

Journal: Frontiers in Oncology

Article Title: Construction of a novel cuproptosis-related gene signature for predicting microenvironment, prognosis and therapeutic response in cervical cancer

doi: 10.3389/fonc.2025.1532772

Figure Lengend Snippet: Overexpression of FOXJ1 decreased the proliferation, invasion, migration and the level of EMT process through the regulation of cuproptosis. (A) Western blotting showed the overexpression efficiency of FOXJ1 plasmid in HeLa and SiHa cells. (B, C) CCK-8 and EdU assays showing FOXJ1 attenuation of the proliferation of cervical cancer cells. (D) Colony formation assay showing reduced ability of forming colonies after overexpression of FOXJ1. (E) The migration and invasion abilities of cervical cancer cells determined by Transwell assay. (F) Overexpression of FOXJ1 reduced the protein levels of N-cadherin, Vimentin and Snail in cervical cancer cells. (G) Western blot analysis revealed that overexpression of FOXJ1 downregulated the expression of key cuproptosis-related proteins, LIAS and LIP-DLAT. This suppression was reversed upon treatment with the copper chelator TTM (40μM). (H) EdU assays demonstrated that FOXJ1 inhibits the proliferation of HeLa cells via cuproptosis. (I) Transwell assay experiments indicated that FOXJ1 suppresses the migration and invasion abilities of HeLa cells through the cuproptosis. Data are presented as the mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001.

Article Snippet: FOXJ1 , sc-53139 , 1:200 , 1:100 , Mouse polyclonal , Santa Cruz, USA.

Techniques: Over Expression, Migration, Western Blot, Plasmid Preparation, CCK-8 Assay, Colony Assay, Transwell Assay, Expressing

Journal: bioRxiv

Article Title: H3N2 influenza virus tropism shifts to glycan receptors on tracheal ciliated cells

doi: 10.1101/2025.09.12.675939

Figure Lengend Snippet: ( A ) Schematic of the airway epithelial layer and cell type-specific markers for ciliated cells, acetyl-α-tubulin ( red ) and FOXJ1 (yellow), and for secretory/goblet cells, MUC5AC ( magenta ). ( B ) Human trachea sections were stained with cell type markers and either SNA lectin ( left) , BK/79 recombinant HA (rHA) ( middle ), and WI/18 HA ( right) ( green ). See Figure S18 for additional images. ( C ) Diagram of the analyses employed to determine whether the HA staining is closer to ciliated or goblet cells, based on a 3D model constructed from confocal images. ( D ) Proximity of BK/79 and WI/18 HA staining to markers of secretory/goblet cells and epithelial cells. ( E ) Glycan biosynthetic pathways for LacNAc extension ( top ) or terminating a LacNAc-terminated glycan substrate ( bottom ). ( F ) Uniform manifold approximation and projection (UMAP) representation of cell types from human nasal (N) and tracheobronchial (TB) samples ( upper panel ) and expression of ST6GAL1 ( lower left ) and B3GNT2 ( lower right ). ( G ) Expression of glycosyltransferase genes in ciliated, secretory/goblet, and basal cell populations in trachea. Data was reanalyzed from the publicly available scRNAseq data of Deprez et al (2020).

Article Snippet: The primary antibodies used in this study were as follows: anti-acetyl-α-tubulin antibody (Sigma, 1:2000), anti-mucin-5AC antibody (Abcam, 1:150), anti-FoxJ1 antibody (RnD systems, 1:400), anti-His-tag antibody (Novus Biologicals, 25 μg/mL), biotinylated SNA lectin (Vector laboratories, 1:100).

Techniques: Staining, Recombinant, Construct, Glycoproteomics, Expressing