rabbit anti relb  (Proteintech)

Journal: bioRxiv

Article Title: A Suite of Eight Toxoplasma gondii Effectors Cooperates to Activate the Non-canonical NF-κB Pathway

doi: 10.64898/2026.03.12.711255

Figure Lengend Snippet: A) Top-scoring transcription factors predicted to regulate the MYR1-dependent upregulated genes in HFF cells relative to uninfected controls were identified by analysis of previously published data using Enrichr. B-C) Representative images (top) and quantitative analysis (bottom) for RelB (B) and p52 (C) nuclear accumulation in HFFs infected with RH (WT), Δ myr1 or Δ myr1 ::MYR1 complement parasites. Twenty-four hours post-infection, cells were fixed and labeled with DAPI (blue), anti-GAP45 (red), and either anti-RelB or anti-p52 (green). Scale bars = 10 µm. Plots display the nuclear-to-cytoplasmic signal ratios for at least 300 infected cells (red arrows) per condition; uninfected cells are indicated by white arrows. Data from three independent experiments were combined for analysis. The horizontal dashed lines indicate the mean. Statistical significance was determined using a one-way ANOVA with Tukey’s multiple comparison test; ****P < 0.0001, ns = not significant.

Article Snippet: The following primary antibodies were used: rabbit anti-RelB (1:300; Proteintech, 25027-1-AP), mouse anti-NFκB p52 (1:100; Santa Cruz Biotechnology, sc-7386), and mouse anti-GAP45 or rabbit anti-GAP45 (kindly provided by Dr D. Etheridge, University of Georgia, USA).

Techniques: Infection, Labeling, Comparison

Journal: bioRxiv

Article Title: A Suite of Eight Toxoplasma gondii Effectors Cooperates to Activate the Non-canonical NF-κB Pathway

doi: 10.64898/2026.03.12.711255

Figure Lengend Snippet: A-B) Representative images (top) and quantitative analysis (bottom) for RelB (A) and p52 (B) nuclear accumulation in MEFs infected with RH (WT), Δ myr1 or Δ myr1 ::MYR1 complement parasites. Twenty-four hours post-infection, cells were fixed and labeled with DAPI (blue), anti-GAP45 (red), and either anti-RelB or anti-p52 (green). Scale bars = 10 µm. Plots display the nuclear-to-cytoplasmic signal ratios for at least 300 infected cells (red arrows) per condition; uninfected cells are indicated by white arrows. Data from three independent experiments were combined for analysis. The horizontal dashed lines indicate the mean. Statistical significance was determined using a one-way ANOVA with Tukey’s multiple comparison test; ****P < 0.0001, ns = not significant.

Article Snippet: The following primary antibodies were used: rabbit anti-RelB (1:300; Proteintech, 25027-1-AP), mouse anti-NFκB p52 (1:100; Santa Cruz Biotechnology, sc-7386), and mouse anti-GAP45 or rabbit anti-GAP45 (kindly provided by Dr D. Etheridge, University of Georgia, USA).

Techniques: Infection, Labeling, Comparison

Journal: bioRxiv

Article Title: A Suite of Eight Toxoplasma gondii Effectors Cooperates to Activate the Non-canonical NF-κB Pathway

doi: 10.64898/2026.03.12.711255

Figure Lengend Snippet: T. gondii activates the non-canonical NF-κB pathway through MYR1-dependent TRAF3 depletion and NIK stabilization. (A) Representative images (top) and quantitative analysis (bottom) for RelB nuclear accumulation in HFFs infected with RH (WT) parasites over a 24-h time course. At 6, 12, 18, and 24 h post-infection, cells were fixed and labeled with DAPI (blue), anti-GAP45 (red), and anti-RelB (green). Scale bars = 10 µm. Plots display the nuclear-to-cytoplasmic intensity ratios for at least 300 infected cells (red arrows) per condition; uninfected cells are indicated by white arrows. Data from three independent experiments were combined for analysis. The horizontal dashed lines indicate the mean. Statistical significance was determined using a one-way ANOVA with Tukey’s multiple comparison test; ***P < 0.001, ****P < 0.0001, ns = not significant. (B) Immunoblot analysis (top) and corresponding quantification (bottom) of TRAF3, NIK, p100 phosphorylation, and p100-to-p52 processing in HFFs that were uninfected (UI) or infected with RH (WT), Δmyr1 or Δmyr1 ::MYR1 complement parasites. Lysates collected 24 h post-infection were resolved by SDS-PAGE and probed with specific primary antibodies; β-tubulin served as a loading control. Band intensities were measured using ImageJ and normalized to β-tubulin. Data are presented as mean ±SD from three biological replicates. Statistical significance for all panels was determined using a one-way ANOVA with Tukey’s multiple comparison test; **P < 0.01, ***P < 0.001, ****P < 0.0001, ns = not significant

Article Snippet: The following primary antibodies were used: rabbit anti-RelB (1:300; Proteintech, 25027-1-AP), mouse anti-NFκB p52 (1:100; Santa Cruz Biotechnology, sc-7386), and mouse anti-GAP45 or rabbit anti-GAP45 (kindly provided by Dr D. Etheridge, University of Georgia, USA).

Techniques: Infection, Labeling, Comparison, Western Blot, Phospho-proteomics, SDS Page, Control