hela epithelial cervical cancer cell line  (ATCC)

Journal: bioRxiv

Article Title: Measure Sodium Transport in Cells with NMR

doi: 10.1101/2025.07.08.663659

Figure Lengend Snippet: The representative data sets of Na REXSY at t m = 2 ms (above) and the corresponding Q-Q plots (below) for ( a ) yeast cells, ( b ) HeLa cells, and ( c ) U-87 cells, respectively. In Q-Q plots, data points closer to a linear distribution indicate better normality. ( d ) The transport rate constant k ef , ( e ) The molar fraction of intracellular Na + ( f in ) and ( f ) The relaxation rate constants in in yeast group (n = 4), HeLa group (n = 5) and U-87 group (n = 5). The data were shown as mean ± s.e.m. * P <0.05, ** P <0.01, *** P <0.001. P values were calculated using one-way analysis of variance (ANOVA). N.S., not significant.

Article Snippet: HeLa epithelial cervical cancer cell line and human U87 glioma cell line were obtained from the American Type Culture Collection (ATCC, USA).

Techniques:

Journal: Methods in molecular biology (Clifton, N.J.)

Article Title: Phosphopeptide Enrichment Using Offline Titanium Dioxide Columns for Phosphoproteomics

doi: 10.1007/978-1-62703-360-2_8

Figure Lengend Snippet: Nanoflow reversed-phase liquid chromatography coupled online with a linear ion trap mass spectrometer for the analysis of TiO2-enriched phosphopeptides from a HeLa cell lysate using collision-induced dissociation (CID) for tandem MS and phosphate neutral loss-dependent MS/MS/MS (RPLC-MS2-MS3). The analysis is for 5 μL injection of phosphopeptides onto a 75 μm ID capillary column. The lower panel is the base peak chromatogram of the analysis. The upper panel shows the MS3 or MS2 spectra of the phosphopeptides ALVAT*PGKK, SGAQASSTPLS*PTR, and LLT*PTHSFLAR identified, respectively, from nucleolin, lamin-A/C, and microtubule-associated protein 7. The relatively high abundance levels of the LC chromatographic peaks, from which these phosphopeptides were eluted, demonstrate that phosphopeptides were effectively enriched from the HeLa cell lysate. The asterisk marks the phosphorylated Ser or Thr residues.

Article Snippet: Cell Culture of HeLa Cells Human cervical epithelial cancer cell line HeLa (ATCC).

Techniques: Reversed-phase Chromatography, Mass Spectrometry, Tandem Mass Spectroscopy, Injection

Journal: Methods in molecular biology (Clifton, N.J.)

Article Title: Phosphopeptide Enrichment Using Offline Titanium Dioxide Columns for Phosphoproteomics

doi: 10.1007/978-1-62703-360-2_8

Figure Lengend Snippet: Nanoflow reversed-phase liquid chromatography coupled online with a linear ion trap mass spectrometer for the analysis of TiO2-enriched phosphopeptides from a HeLa cell lysate using collision-induced dissociation (CID) for tandem MS and phosphate neutral loss-dependent MS/MS/MS (RPLC-MS2-MS3). The analysis is for 5 μL injection of phosphopeptides onto a 75 μm ID capillary column. The lower panel is the base peak chromatogram of the analysis. The upper panel shows the MS3 or MS2 spectra of the phosphopeptides ALVAT*PGKK, SGAQASSTPLS*PTR, and LLT*PTHSFLAR identified, respectively, from nucleolin, lamin-A/C, and microtubule-associated protein 7. The relatively high abundance levels of the LC chromatographic peaks, from which these phosphopeptides were eluted, demonstrate that phosphopeptides were effectively enriched from the HeLa cell lysate. The asterisk marks the phosphorylated Ser or Thr residues.

Article Snippet: Human cervical epithelial cancer cell line HeLa (ATCC).

Techniques: Reversed-phase Chromatography, Mass Spectrometry, Tandem Mass Spectroscopy, Injection