Journal: bioRxiv

Article Title: Inexpensive High-Throughput Multiplexed Cytokine Detection for Tuberculosis Diagnostics Using Amplified Enzymatic Metallization

doi: 10.64898/2026.01.27.700981

Figure Lengend Snippet: (a) Schematic of immunoassay for cytokine detection. (b) Initial LOD optimization for the IFN-γ assay. (c-e) IFN-γ (n=2), IL-2 (n=5), TNF-α (n=2) dilution curves using recombinant cytokines (f-h) Correlation plots of ELISA absorbance values at 450 nm versus silver darkness values for IFN-γ (f), TNF-α (g), and IL-2 (h). All fit lines are four-parameter logistic sigmoidal curves.

Article Snippet: Recombinant human IFN-γ protein (11725-HNAS), biotinylated anti-human IFN-γ antibody (11725-R209-B), anti-human IFN-γ antibody (11725-R238), HRP-conjugated anti-human IFN-γ antibody (11725-R209-H), recombinant human TNF-α protein (10602-HNAE), biotinylated anti-human TNF-α antibody (10602-MM08-B), and anti-human TNF-α antibody (10602-MM01) were obtained from SinoBiological.

Techniques: Recombinant, Enzyme-linked Immunosorbent Assay

Journal: bioRxiv

Article Title: Inexpensive High-Throughput Multiplexed Cytokine Detection for Tuberculosis Diagnostics Using Amplified Enzymatic Metallization

doi: 10.64898/2026.01.27.700981

Figure Lengend Snippet: (a) Schematic demonstrating the stimulation groups and controls. Dilution curves for IFN-γ (b-c), IL-2 (d-e), and TNF-α (f-g) in pooled LTB+ and LTB-clinical supernatant samples. Clinical samples consisted of NIL (negative control), Ag1, Ag2, and Mitogen (positive control) groups (n=2).

Article Snippet: Recombinant human IFN-γ protein (11725-HNAS), biotinylated anti-human IFN-γ antibody (11725-R209-B), anti-human IFN-γ antibody (11725-R238), HRP-conjugated anti-human IFN-γ antibody (11725-R209-H), recombinant human TNF-α protein (10602-HNAE), biotinylated anti-human TNF-α antibody (10602-MM08-B), and anti-human TNF-α antibody (10602-MM01) were obtained from SinoBiological.

Techniques: Negative Control, Positive Control

Journal: bioRxiv

Article Title: Inexpensive High-Throughput Multiplexed Cytokine Detection for Tuberculosis Diagnostics Using Amplified Enzymatic Metallization

doi: 10.64898/2026.01.27.700981

Figure Lengend Snippet: Individual participant silver darkness values for IFN-γ (a), IL-2 (b), and TNF-α (c) detection from NIL, Ag1, Ag2, and Mitogen samples of IGRA+ and IGRA-patients using a sample dilution of 1:10. Average of n=2 repeats was plotted for each sample.

Article Snippet: Recombinant human IFN-γ protein (11725-HNAS), biotinylated anti-human IFN-γ antibody (11725-R209-B), anti-human IFN-γ antibody (11725-R238), HRP-conjugated anti-human IFN-γ antibody (11725-R209-H), recombinant human TNF-α protein (10602-HNAE), biotinylated anti-human TNF-α antibody (10602-MM08-B), and anti-human TNF-α antibody (10602-MM01) were obtained from SinoBiological.

Techniques:

Journal: bioRxiv

Article Title: Inexpensive High-Throughput Multiplexed Cytokine Detection for Tuberculosis Diagnostics Using Amplified Enzymatic Metallization

doi: 10.64898/2026.01.27.700981

Figure Lengend Snippet: (a) Schematic of laser-cut PDMS microwell array reversibly assembled on a polystyrene petri dish and workflow of enzymatically amplified silver metallization using Biotin-BSA and poly-HRP-SA. (b) Cell-phone image of silver metallized wells after assay. (c) Biotin-BSA dilution curve obtained from cell-phone image silver darkness quantification in ImageJ. (d) Assay stack for initial biotinyl tyramide signal amplification testing using biotinylated anti-IFN-γ as capture. (e) Dilution curve of silver darkness of increasing biotinylated anti-IFN-γ as target and 10 µg/mL, 1 µg/mL, and 0 µg/mL biotinyl tyramide. All assays were repeated three (n=3) times and fit lines are four-parameter logistic sigmoidal curves.

Article Snippet: Recombinant human IFN-γ protein (11725-HNAS), biotinylated anti-human IFN-γ antibody (11725-R209-B), anti-human IFN-γ antibody (11725-R238), HRP-conjugated anti-human IFN-γ antibody (11725-R209-H), recombinant human TNF-α protein (10602-HNAE), biotinylated anti-human TNF-α antibody (10602-MM08-B), and anti-human TNF-α antibody (10602-MM01) were obtained from SinoBiological.

Techniques: Amplification

Journal: bioRxiv

Article Title: Inexpensive High-Throughput Multiplexed Cytokine Detection for Tuberculosis Diagnostics Using Amplified Enzymatic Metallization

doi: 10.64898/2026.01.27.700981

Figure Lengend Snippet: (a) Schematic of immunoassay for cytokine detection. (b) Initial LOD optimization for the IFN-γ assay. (c-e) IFN-γ (n=2), IL-2 (n=5), TNF-α (n=2) dilution curves using recombinant cytokines (f-h) Correlation plots of ELISA absorbance values at 450 nm versus silver darkness values for IFN-γ (f), TNF-α (g), and IL-2 (h). All fit lines are four-parameter logistic sigmoidal curves.

Article Snippet: Recombinant human IFN-γ protein (11725-HNAS), biotinylated anti-human IFN-γ antibody (11725-R209-B), anti-human IFN-γ antibody (11725-R238), HRP-conjugated anti-human IFN-γ antibody (11725-R209-H), recombinant human TNF-α protein (10602-HNAE), biotinylated anti-human TNF-α antibody (10602-MM08-B), and anti-human TNF-α antibody (10602-MM01) were obtained from SinoBiological.

Techniques: Recombinant, Enzyme-linked Immunosorbent Assay

Journal: bioRxiv

Article Title: Inexpensive High-Throughput Multiplexed Cytokine Detection for Tuberculosis Diagnostics Using Amplified Enzymatic Metallization

doi: 10.64898/2026.01.27.700981

Figure Lengend Snippet: (a) Schematic demonstrating the stimulation groups and controls. Dilution curves for IFN-γ (b-c), IL-2 (d-e), and TNF-α (f-g) in pooled LTB+ and LTB-clinical supernatant samples. Clinical samples consisted of NIL (negative control), Ag1, Ag2, and Mitogen (positive control) groups (n=2).

Article Snippet: Recombinant human IFN-γ protein (11725-HNAS), biotinylated anti-human IFN-γ antibody (11725-R209-B), anti-human IFN-γ antibody (11725-R238), HRP-conjugated anti-human IFN-γ antibody (11725-R209-H), recombinant human TNF-α protein (10602-HNAE), biotinylated anti-human TNF-α antibody (10602-MM08-B), and anti-human TNF-α antibody (10602-MM01) were obtained from SinoBiological.

Techniques: Negative Control, Positive Control

Journal: bioRxiv

Article Title: Inexpensive High-Throughput Multiplexed Cytokine Detection for Tuberculosis Diagnostics Using Amplified Enzymatic Metallization

doi: 10.64898/2026.01.27.700981

Figure Lengend Snippet: Individual participant silver darkness values for IFN-γ (a), IL-2 (b), and TNF-α (c) detection from NIL, Ag1, Ag2, and Mitogen samples of IGRA+ and IGRA-patients using a sample dilution of 1:10. Average of n=2 repeats was plotted for each sample.

Article Snippet: Recombinant human IFN-γ protein (11725-HNAS), biotinylated anti-human IFN-γ antibody (11725-R209-B), anti-human IFN-γ antibody (11725-R238), HRP-conjugated anti-human IFN-γ antibody (11725-R209-H), recombinant human TNF-α protein (10602-HNAE), biotinylated anti-human TNF-α antibody (10602-MM08-B), and anti-human TNF-α antibody (10602-MM01) were obtained from SinoBiological.

Techniques:

Journal: iScience

Article Title: Prognostic value of BTG1 for predicting decitabine sensitivity in de novo acute myeloid leukemia

doi: 10.1016/j.isci.2025.114327

Figure Lengend Snippet: Downstream signaling pathway of BTG1 in AML cell lines (A) Top three signaling pathways in terms of Gene Ratio were EBV infection (0.037), Wnt signaling pathway (0.035), and hematopoietic lineage (0.023) of KEGG pathway enrichment. (B) Effect of BTG1 on the mRNA expression of β-catenin, Cyclin D1, and C-Myc. (C) Effect of BTG1 on the protein expression of β-catenin and Cyclin D1. (D) The relative viability of AML cells after interference of BTG1 and treatment with FH535. (E) Apoptosis of AML cells after interference of BTG1 and treatment with FH535. Data are presented as mean ± standard deviation (SD). (ns, p > 0.05; ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001; ∗∗∗∗ p < 0.0001).

Article Snippet: Mouse monoclonal anti-human Cyclin D1 , Proteintech , Cat# 60186-1-Ig RRID: AB_10793718.

Techniques: Protein-Protein interactions, Infection, Expressing, Standard Deviation

Journal: iScience

Article Title: Prognostic value of BTG1 for predicting decitabine sensitivity in de novo acute myeloid leukemia

doi: 10.1016/j.isci.2025.114327

Figure Lengend Snippet: Biological functions of BTG1 and decitabine in AML cell lines (A) Viability of three AML cell lines following treatment with different concentrations of decitabine for 72h was determined. (B) Viability of three cell lines following treatment with 500 nM decitabine for different times was determined. (C) Cell proliferation after a 24-h treatment with different concentrations of decitabine in the control group, interfered cells, and overexpressed cells. (D) Kasumi1 were transfected with lentivirus to knockdown (shBTG1) or overexpress (BTG1-UP) BTG1 or empty control (NC); cell viability was determined. (E) Kasumi1 were transfected with lentivirus to knockdown (shBTG1) or overexpress (BTG1-UP) BTG1; apoptosis was determined after 500 nM decitabine treatment. (F) Relative expression of BTG1 mRNA in two cell lines treated with 500 nM decitabine. (G) Relative expression of BTG1 protein in two cell lines treated with different concentrations of decitabine. (H) The effect of decitabine on the protein expression levels of DNMT1, FOXO3a, and BTG1 in MV4-11. Data are presented as mean ± standard deviation (SD). (ns, p > 0.05, #/∗ p < 0.05, ##/∗∗ p < 0.01, ###/∗∗∗ p < 0.001, ####/∗∗∗∗ p < 0.0001).

Article Snippet: Mouse monoclonal anti-human BTG1 , Proteintech , Cat# 14879-1-AP RRID: AB_2067644.

Techniques: Control, Transfection, Knockdown, Expressing, Standard Deviation

Journal: iScience

Article Title: Prognostic value of BTG1 for predicting decitabine sensitivity in de novo acute myeloid leukemia

doi: 10.1016/j.isci.2025.114327

Figure Lengend Snippet: Downstream signaling pathway of BTG1 in AML cell lines (A) Top three signaling pathways in terms of Gene Ratio were EBV infection (0.037), Wnt signaling pathway (0.035), and hematopoietic lineage (0.023) of KEGG pathway enrichment. (B) Effect of BTG1 on the mRNA expression of β-catenin, Cyclin D1, and C-Myc. (C) Effect of BTG1 on the protein expression of β-catenin and Cyclin D1. (D) The relative viability of AML cells after interference of BTG1 and treatment with FH535. (E) Apoptosis of AML cells after interference of BTG1 and treatment with FH535. Data are presented as mean ± standard deviation (SD). (ns, p > 0.05; ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001; ∗∗∗∗ p < 0.0001).

Article Snippet: Mouse monoclonal anti-human BTG1 , Proteintech , Cat# 14879-1-AP RRID: AB_2067644.

Techniques: Protein-Protein interactions, Infection, Expressing, Standard Deviation

Journal: iScience

Article Title: Prognostic value of BTG1 for predicting decitabine sensitivity in de novo acute myeloid leukemia

doi: 10.1016/j.isci.2025.114327

Figure Lengend Snippet: Association of BTG1 expression before treatment and efficacy of decitabine-containing regimen (A) Comparison of BTG1 expression between CR and non-CR and between MRD negativity and MRD positivity in 37 patients who received decitabine with “7 + 3” regimen. (B) Comparison of BTG1 expression between CR and non-CR and between MRD negativity and MRD positivity in 23 patients who received a decitabine-containing regimen. (C) Comparison of BTG1 expression between CR and non-CR and between MRD negativity and MRD positivity in 60 patients. (D) ROC curve of BTG1 mRNA for predicting CR in 60 de novo patients. (E) ROC curve of BTG1 mRNA for predicting MRD negativity in 60 patients. Data are presented as mean ± standard deviation (SD). (∗ p < 0.05; ∗∗∗ p < 0.001).

Article Snippet: Mouse monoclonal anti-human BTG1 , Proteintech , Cat# 14879-1-AP RRID: AB_2067644.

Techniques: Expressing, Comparison, Standard Deviation