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Fig. 3 | BMC Biotechnology

Fig. 3

From: Roles of N-linked and O-linked glycosylation sites in the activity of equine chorionic gonadotropin in cells expressing rat luteinizing hormone/chorionic gonadotropin receptor and follicle-stimulating hormone receptor

Fig. 3

Western blotting analysis of recombinant equine chorionic gonadotropin (rec-eCG). The proteins in the conditioned media were collected and concentrated 5–10-fold. The rec-eCG samples were resolved using sodium dodecyl sulfate–polyacrylamide gel electrophoresis and blotted onto a membrane. The proteins were detected using anti-myc-tag and horseradish peroxidase-conjugated goat anti-mouse IgG antibodies. The proteins were treated with peptide-N-glycanase F to remove N-linked oligosaccharides and subjected to western blotting. Lane 1, Marker; Lane 2, rec-eCGβ/α-wt; Lane 3, rec-eCGβ/αΔ56, Lane 4, rec-eCGβ-D/α; Lane 5, rec-eCGβ-D/αΔ56, − , not treated with peptide-N-glycanase F; +, treated with peptide-N-glycanase F

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BMC Biotechnology

ISSN: 1472-6750

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