Fig. 1
From: Co-relation with novel phosphorylation sites of IκBα and necroptosis in breast cancer cells
Identification of phosphorylation of serine 63 and 262 on IκBα using MALDI-TOF MS. a Newly found phospho-serine 63 of IκBα. Comparison of Mass range expansion of 1700–1750 m/z regions from the MALDI mass spectra of (a) inactivated IκBα; (b) IκBα activated by AurkC; (c) IκBα activated by IKKβ. Mass spectrum of IκBα activated by AurkC indicated exclusive peaks. Peaks were 54–67 peptide including phospho-serine 63 amino acid from IκBα. b Novel phospho-site serine 262 amino acid from IκBα. Comparison of MALDI MS spectra of (a) non-activated IκBα; (b) IκBα activated by AurkC; (c) IκBα activated by IKKβ tryptic digestion peptide between m/z 2250 and 2350 was shown. Unique peaks found m/z 2340.154 in (b). Peaks were 246–264 peptide including unknown phosphorylated amino acid from IκBα. A peptide present five serine and threonine