rabbit anti relb (Proteintech)

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Proteintech rabbit anti relb

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 <t>either</t> <t>anti-RelB</t> 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.

Rabbit Anti Relb, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+relb/RELB+Antibody/bio_rxiv__64898__2026__03__12__711255-143-6-9
Average 93 stars, based on 23 article reviews

rabbit anti relb - by Bioz Stars, 2026-10

93/100 stars

Images

1) Product Images from "A Suite of Eight Toxoplasma gondii Effectors Cooperates to Activate the Non-canonical NF-κB Pathway"

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

Journal: bioRxiv

doi: 10.64898/2026.03.12.711255

Figure Legend 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.

Techniques Used: Infection, Labeling, Comparison

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.

Figure Legend 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.

Techniques Used: Infection, Labeling, Comparison

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

Figure Legend 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

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

Concentration Assay:

Article Title: Chlorogenic Acid Alleviated AFB1-Induced Hepatotoxicity by Regulating Mitochondrial Function, Activating Nrf2/HO-1, and Inhibiting Noncanonical NF-κB Signaling Pathway
Article Snippet: .. The membranes were blocked with TBST buffer containing 5% skim milk powder for 1 h, followed by incubating with the primary antibodies (included anti-TRAF2 (concentration, 1:1000), anti-RelB (concentration, 1:3000), anti-p52 (concentration, 1:1000), anti-Nrf2 (concentration, 1:6000), anti-Keap-1 (concentration,1:5000), anti-HO-1 (concentration,1:3000), and anti-GAPDH (concentration, 1:8000)) at 4 °C overnight (Proteintech, Wuhan, China), and then further incubated with the secondary antibodies (Proteintech, Wuhan, China; concentration, 1:8000) for 1 h at room temperature. ..

Incubation:

Article Title: Circulating Myeloid-derived Suppressor Cells Facilitate Invasion of Thyroid Cancer Cells by Repressing miR-486-3p.
Article Snippet: Equal amounts of protein sample were separated by 10% SDS-PAGE and transferred to PVDF membrane (Millipore, MA, USA). .. After blocking with 5% bovine serum albumin, membranes were incubated with rabbit anti-NF-κB2 (Cell Signaling Technology, MA, USA), anti-RelB (Proteintech, IL, USA) and anti-GAPDH (Proteintech) at a 1:1000 dilution overnight at 4°C. .. After washing with TBST, the bands were then incubated with the secondary antibody of conjugated anti-rabbit horseradish peroxidase (HRP) (Cell Signaling Technology) at room temperature for 2h.

Article Title: Dual-functional 3D-printed polyetheretherketone scaffolds with immunomodulatory nano‑calcium silicate/interleukin-4 coating synergistically enhance osteogenesis through macrophage M2 polarization and NF-κB pathway suppression
Article Snippet: The membranes were blocked with 5 % (w/v) skim milk (GC310001; Servicebio, China) in TRIS-buffered saline containing 0.1 % Tween-20 (TBST) for 1 h at room temperature and washed thrice with TBST. .. Subsequently, the membranes were incubated overnight at 4 ◦C with the following primary antibodies: anti-GAPDH (1:6000; GB15004–100, Servicebio, China), anti-RelB (1:1000; 25,027, Proteintech, USA), and anti-NFκB2 (1:1000; 10,409, Proteintech, USA). .. After three TBST washes, the membranes were incubated with a horseradish peroxidaseconjugated secondary antibody (1:2000; GB23303, Servicebio, China) at room temperature for 1 h. After three additional TBST washes, protein bands were visualized using an electrochemiluminescence substrate (PE0010; Solarbio, China) and imaged with a ChemiDoc MP Imaging System (Bio-Rad, USA).

Blocking Assay:

other:

Article Title: NF-κB fingerprinting reveals heterogeneous NF-κB composition in diffuse large B-cell lymphoma
Article Snippet: Anti-RelB , Polyclonal , Proteintech.

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