antibodies against ampkα, phosphorylated (p)ampkα (thr172), acc, p-acc (ser79), and β-actin  (Cell Signaling Technology Inc)

Journal: Nutrients

Article Title: Arene Substitutions in Orchid Bibenzyls: Mechanistic Insights into Glucose Uptake and Lipid Metabolism for Targeting Metabolic Disorders

doi: 10.3390/nu17071104

Figure Lengend Snippet: Impacts of batatasin III and gigantol on adipogenesis-mediated signaling pathways. The activation (phosphorylation denoted with prefix p-) levels of some signaling pathways (AMPK-ACC and AKT/GSK-3 β) triggered during early differentiation of 3T3-L1 cells treated with non-cytotoxic concentrations (5–25 μM) of batatasin III ( A – F ) or gigantol ( G – L ) for 48 h were assessed using Western blot analysis. Undifferentiated (UC) and differentiated (DC) cells treated with vehicle (0.5% ( v / v ) dimethyl sulfoxide) served as controls. Protein levels were quantified using ImageJ software and normalized to β-actin. Numerical data are presented as means ± SDs from three independent experiments. Lowercase letters indicate statistically significant differences among means within the same experimental condition. Statistical analysis was conducted using one-way ANOVA followed by Tukey’s post hoc test at α = 0.05.

Article Snippet: The primary antibodies included GLUT1, GLUT4, PPARγ, C/EBPα, FAS, FABP4, PLIN1, adiponectin, AKT, phosphorylated AKT (p-AKT; Ser473), AMPKα, phosphorylated AMPKα (p-AMPKα; Thr172), AMPKβ1/2, phosphorylated AMPKβ1 (p-AMPKβ1; Ser182), ACC, phosphorylated ACC (p-ACC; Ser79), GSK3β, phosphorylated GSK3β (p-GSK3β; Ser9), and β-Actin, all purchased from Cell Signaling Technology (Danvers, MA, USA), while LPL and SREBP-1c antibodies were sourced from Invitrogen (Waltham, MA, USA).

Techniques: Protein-Protein interactions, Activation Assay, Phospho-proteomics, Western Blot, Software