antibodies against hif1 α  (Proteintech)

Journal: PeerJ

Article Title: UBE2S and HIF1α expression patterns and stratified analysis reveal prognostic value in esophageal squamous cell carcinoma

doi: 10.7717/peerj.20694

Figure Lengend Snippet: (A–D) UBE2S staining intensities: negative, weak, moderate, strong. (E) UBE2S IHC scores ( p < 0.001). (F–I) HIF1 α staining intensities: negative, weak, moderate, strong. (J) HIF1 α IHC scores ( p = 0.004). (K–N) p110 α staining intensities: negative, weak, moderate, strong. (O) p110 α IHC scores ( p = 0.039). All micrographs shown at ×200 magnification.

Article Snippet: The primary antibodies used were: UBE2S (rabbit polyclonal, 14115-1-AP, 1:360; Proteintech), HIF1 α (rabbit monoclonal, bs-0737R, 1:400; BIOSS), and p110 α (rabbit polyclonal, C73F8, 1:250; ZSGB-Bio).

Techniques: Staining

Journal: PeerJ

Article Title: UBE2S and HIF1α expression patterns and stratified analysis reveal prognostic value in esophageal squamous cell carcinoma

doi: 10.7717/peerj.20694

Figure Lengend Snippet: (A, B) Pan-cancer mRNA expression analysis of UBE2S (A) and HIF1 α (B) across TCGA malignancies, indicating significant overexpression in ESCA. (C, D) Validation of UBE2S (C) and HIF1 α (D) mRNA overexpression in the TCGA-ESCA tumor cohort compared to a pooled normal tissue reference (integrating GTEx data; p < 0.001, Wilcoxon rank-sum test). (E, F) Independent validation in the GEO dataset ( GSE161533 ) confirms significant overexpression of UBE2S (E) and HIF1 α (F) in ESCC tissues compared to paired adjacent non-tumorous tissues ( p < 0.001). (G) Correlation analysis within the TCGA-ESCA cohort reveals a significant positive correlation between UBE2S and HIF1 α mRNA expression levels (Pearson’s correlation; R = 0.42, p = 0.0013).

Article Snippet: The primary antibodies used were: UBE2S (rabbit polyclonal, 14115-1-AP, 1:360; Proteintech), HIF1 α (rabbit monoclonal, bs-0737R, 1:400; BIOSS), and p110 α (rabbit polyclonal, C73F8, 1:250; ZSGB-Bio).

Techniques: Expressing, Over Expression, Biomarker Discovery

Journal: PeerJ

Article Title: UBE2S and HIF1α expression patterns and stratified analysis reveal prognostic value in esophageal squamous cell carcinoma

doi: 10.7717/peerj.20694

Figure Lengend Snippet: (A, B) Kaplan–Meier survival curves showing that high expression of UBE2S is significantly associated with poorer overall survival (OS; p = 0.006) and progression-free survival (PFS; p = 0.034). (C, D) Similarly, high expression of HIF1 α is associated with reduced OS ( p < 0.001) and PFS ( p = 0.002). (E, F) Patients were stratified into four groups based on UBE2S and HIF1 α co-expression status: Group 1 (dual-negative), Group 2 (UBE2S-negative/HIF1 α -positive), Group 3 (UBE2S-positive/HIF1 α -negative), and Group 4 (dual-positive). Kaplan–Meier analysis revealed significant stratification of both OS ( p < 0.001) and PFS ( p = 0.005) among these groups, with patients exhibiting dual-positive expression (Group 4) demonstrating the poorest outcomes.

Article Snippet: The primary antibodies used were: UBE2S (rabbit polyclonal, 14115-1-AP, 1:360; Proteintech), HIF1 α (rabbit monoclonal, bs-0737R, 1:400; BIOSS), and p110 α (rabbit polyclonal, C73F8, 1:250; ZSGB-Bio).

Techniques: Expressing

Journal: Advanced Science

Article Title: Tumoroid Model Reveals Synergistic Impairment of Metabolism by Iron Chelators and Temozolomide in Chemo‐Resistant Patient‐derived Glioblastoma Cells

doi: 10.1002/advs.202412505

Figure Lengend Snippet: DFO and DFP upregulate Hif1‐α expression and ROS generation in non‐resistant and TMZ‐resistant cells. A) Hif1‐α expression, imaged by IF microscopy (A‐left panels) and flow cytometry (A‐right panels) as well as western blotting (the protein, for the same experimental conditions across the lanes, came from the same lysate master mix, used in this figure and in Figures and ), revealed upregulation in response to 24 h of hypoxia and 50 µM DFO and DFP treatments. Flow cytometry quantification of Hif‐1α accumulation, indicating higher levels in DFO‐treated non‐resistant cells compared to DFP and hypoxia, with a similar trend observed in TMZ‐resistant cells. Glucose uptake analyses (B‐top panels) highlighted a pronounced difference between non‐resistant and TMZ‐resistant cells, with varying glucose concentrations affecting proliferation rates (B‐bottom panels), suggesting a critical threshold and different responses under hypoxic and normoxic conditions. This denotes the high sensitivity of normoxic TMZ‐resistant cell to DFO. In contrast, hypoxic TMZ‐resistant cells were less sensitive to all tested concentrations of DFO and DFP. C) Non‐monotonic dose‐dependent increase of ROS in DFO‐treated non‐resistant and TMZ‐resistant cells. DFP induced increases in ROS across all conditions. Hypoxia reduced the effect of both DFO and DFP in TMZ‐resistant cells. N = 3 biological independent experiments and statistically significant at * p ‐value < 0.05 and ** p ‐value < 0.01. Scale bar is 100 µm.

Article Snippet: Rabbit anti BAX (Cat# 92 772), rabbit anti caspase3 (9662), mouse anti HIF1‐α (Cat# 79 233), rabbit anti β‐actin (Cat# 4967), anti‐rabbit IgG (H+L)‐DyLight 800 (Cat# 5151) and anti‐mouse IgG (H+L)‐DyLight 800 (Cat# 5257) were purchased from CellSignaling.

Techniques: Expressing, Microscopy, Flow Cytometry, Western Blot

Journal: Journal of Dental Sciences

Article Title: Hypoxia amplifies arecoline-induced invasion and metastasis in oral squamous cell carcinoma – Insights into TGF-β1 signaling and collagen production

doi: 10.1016/j.jds.2024.12.026

Figure Lengend Snippet: Protein expression in SCC-25 cells treated with arecoline under hypoxia . (A) Western blot analysis of protein expression levels for HIF1-α, type I collagen, TGF-β1, and phosphorylated Smad2/3 in SCC-25 cells treated with 2.5 μg/mL arecoline under normoxic and hypoxic conditions. β-actin was used as the loading control. (B) Arecoline at 2.5 μg/mL upregulates the protein levels of type I collagen, TGF-β1, and phosphorylated Smad3 in SCC-25 cells under normoxia. (C) Hypoxia alone significantly increases the expression of HIF1-α, type I collagen, and TGF-β1 in both control and arecoline-treated SCC-25 cells, with a further enhancement seen in the arecoline-treated group. Data are presented as mean ± SE (n = 4). Statistical significance was determined using a t-test, with significant differences indicated as follows: ∗ P < 0.05; ∗∗ P < 0.01; ∗∗∗ P < 0.001; ∗∗∗∗ P < 0.0001.

Article Snippet: Membranes were blocked with 2% BSA (Sigma–Aldrich, Merck, Darmstadt, Germany) and incubated overnight with primary antibodies for TGF-β1 (Abcam, Cambridge, UK), collagen I (Proteintech, Rosemont, IL, USA), HIF1-α (Proteintech), Phospho-Smad2 (Cell Signaling Technology, Danvers, MA, USA), Smad2/3 (Cell Signaling Technology) and β-actin (Abcam).

Techniques: Expressing, Western Blot, Control