phospho acc antibody p acc  (Proteintech)

Journal: Nature Communications

Article Title: Ustilago maydis disrupts carbohydrate signaling networks to induce hypertrophy in host cells

doi: 10.1038/s41467-026-69532-8

Figure Lengend Snippet: a Schematic overview of the phosphoproteomics experiment: (1) seven-day-old maize seedlings were infected with mock, SG200, or CR- hap1 and collected at 3 dpi. Created in BioRender. Doehlemann, G. (2026) https://BioRender.com/1zmsye4 . (2) Total maize proteins were extracted and separated into total proteome and phosphoproteome fractions. (3) Protein peptides were phosphoenriched using titanium dioxide. (4) Peptides were fractionated and analyzed by mass spectrometry. (5) Identified spectra were mapped to the Z. mays genome to identify phosphorylation sites. b Venn diagram showing uniquely increased phosphorylated proteins in SG200 and CR- hap1 compared to mock. c Venn diagram showing uniquely decreased phosphorylated proteins in SG200 and CR- hap1 compared to mock. d GO enrichment analysis of proteins with increased phosphorylation in SG200 vs. CR- hap1 . Significance is indicated by -Log10( P -value), with color shading from red (high significance) to blue (low significance). e Overview of the SnRK1-dependent consensus motif at P-5 and P + 4 relative to phosphorylated Ser/Thr residues. The color scheme follows the MEME Suite’s coding for amino acids. Amino acid matching the known human AMPK consensus phosphorylation sequence is colored in pink and blue at P-2 and P + 3 positions, respectively. Thirteen proteins that perfectly match the SnRK1 consensus motif are indicated in bold. When the motif criteria were relaxed to require only one of the hydrophobic residues at either P–5 or P + 4, a total of 25 proteins matched the SnRK1 motif. Log₂FC values are color-coded: black for log₂FC > 1 or < – 1 with p < 0.05, and gray for all others. f Hap1 inhibits SnRK1-dependent phosphorylation of rACC1. A GFP-fused 57-amino acid peptide surrounding the Ser79 phosphorylation site of rat acetyl-CoA carboxylase 1 (rACC1) was co-expressed with the indicated proteins in N. benthamiana . SnRK1 activity was assessed by detecting rACC1 phosphorylation at Ser79 (pS79 ACC) using a phospho-specific Anti-P-S79 ACC antibody. Total rACC1 levels were detected with an anti-GFP antibody. Lane 1: expression of rACC1 alone; Lane 2: co-expression of rACC1 and SnRK1; Lane 3: co-expression of rACC1, SnRK1 and Hap1; Lane 4: co-expression of rACC1 and Hap1; Lane 5: co-expression of Hap1 and SnRK1. The positions of the molecular weight ladder are shown on the right. The experiment was repeated three times with similar results. g Quantification of SnRK1-dependent rACC1 phosphorylation in the presence or absence of Hap1. The bar graph shows the fold change of P-S79 rACC1 normalized to total rACC1 (P-ACC/ACC-total). P-ACC/ACC-total ratios were scaled to the Lane 3 condition (set to 1) to obtain fold-change values. Data represent three biological replicates, each from an independent blot. Bars show mean ± SEM. Statistical significance was determined by a paired t-test on log₂ transformed values.

Article Snippet: Phospho-Acetyl-CoA Carboxylase (Ser79) (anti-P-S79 ACC) antibody (CST, #3661, Dilution: 1:1000) was used to detect phosphorylation of ACC at serine 79.

Techniques: Phospho-proteomics, Infection, Titanium Dioxide, Mass Spectrometry, Sequencing, Activity Assay, Expressing, Molecular Weight, Transformation Assay

Journal: Scientific Reports

Article Title: Myoblast paracrine factors induce catabolic remodelling in electrically stimulated myotubes

doi: 10.1038/s41598-025-21126-y

Figure Lengend Snippet: EPS-induced structural and molecular alterations to myotubes are influenced by MBL exposure. ( A ) Transmission electron microscopy images of unstimulated (NS) C 2 C 12 myotubes and immediately post-electrical pulse stimulation (EPS). White arrows identify an intact Z line and yellow arrows denote Z line streaming. Scale bar = 1200 nm. ( B ) Cropped representative western blots from the same gel, delineated by a perforated line. ( C ) A graphical summary of β-dystroglycan, desmin, heat shock protein 70 (HSP70), calpain 3, phosphorylated acetyl CoA carboxylase at serine 79 (p-ACC ser79 ), total (t-)ACC, phosphorylated Unc-51-like kinase 1 at serine 555 (p-ULK1 ser555 ), t-ULK1, phosphorylated mammalian target of rapamycin at serine 2448 (p-mTOR ser2448 ), t-mTOR, phosphorylated eukaryotic translation initiation factor 4E-binding protein 1 at threonine 37&46 (p-4EBP1 Thr37/46 ), and t-4EBP1 protein content in resting and stimulated myotubes. ( D ) A visual schematic of the study design. Differentiated myotubes and media were collected following 1-hr of electrical pulse stimulation (EPS) or unstimulated incubation in fresh growth media. Transwells with (MBL+) or without (MBL–) myoblasts were inserted into the culture at 0-hrs post-EPS, and cell lysates were collected at various time points thereafter. ( E ) Creatine kinase (CK) activity in conditioned media of EPS damaged MBL + and MBL– myotubes. F - H ) Representative western blots of β-dystroglycan and desmin protein expression and accompanying graphical representations of EPS damaged MBL + and MBL– myotubes. N = 3. Data are expressed as means ± SEM. * p < 0.05 effect of MBL, # p < 0.05 effect of time. Two-tail independent Student’s t-test ( C ) and two-way ANOVA ( E , G , H ). Original western blots are presented in Supplementary Fig. 1.

Article Snippet: p-ACC Ser79 , CST , 3661 S , 1:1000.

Techniques: Transmission Assay, Electron Microscopy, Western Blot, Binding Assay, Incubation, Activity Assay, Expressing