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Fig. 3 | Journal of Inflammation

Fig. 3

From: Lipopolysaccharide-induced inflammation or unilateral ureteral obstruction yielded multiple types of glycosylated Lipocalin 2

Fig. 3

Endo- and exoglycosidase digestions of urinary LCN2 from LPS-treated mice. (a) Proteins were subjected to SDS-PAGE and CBB staining. Fetuin (48 kDa) served as a positive control substrate for PNGase F and NA, whereas RNase B (17 kDa) was the control substrate for Endo H. Each experiment was repeated three times. The numbers on the right sides of the figures indicate the molecular marker size (kDa). (b) The N-glycosylation sites of mouse urinary LCN2 were digested by PNGase F, Endo H, or NA. Each experiment was repeated six times. The numbers on the right sides of the figures indicate the molecular size of LCN2 (kDa). (c) Comparison of the PNGase F digestions between recombinant mouse LCN2 (left and center) and native mouse urinary LCN2 (right). Each experiment was repeated three times. Protein samples (5 μg) and samples of conditioned media (2 μL) were resolved by gel electrophoresis. The numbers on the right sides of the figures indicate the molecular size of LCN2 (kDa)

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Journal of Inflammation

ISSN: 1476-9255

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