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. Author manuscript; available in PMC: 2013 May 21.

Published in final edited form as: Biotechnol Prog. 2012 May 21;28(3):846–855. doi: 10.1002/btpr.1542

Analysis of purified mAb 277 Ala and Gly stable lysates and supernatants

(A) The eluted fractions (lanes 1–6, in the order they were eluted from the column from first (1) to last (6)) from protein A purified Ala-138 (top panel) and Gly-26 (bottom panel) lysates were probed using the same α-human Fcγ antibody under reducing conditions. The top band for the Ala-138 and Gly-26 panels is ~50 kDa. Lane 7 is the crude lysate. (B) SDS-PAGE of the reduced (left) and non-reduced (right) purified supernatant shows that none of the low molecular weight HC band was secreted.

Analysis of purified mAb 277 Ala and Gly stable lysates and supernatants

(A) The eluted fractions (lanes 1–6, in the order they were eluted from the column from first (1) to last (6)) from protein A purified Ala-138 (top panel) and Gly-26 (bottom panel) lysates were probed using the same α-human Fcγ antibody under reducing conditions. The top band for the Ala-138 and Gly-26 panels is ~50 kDa. Lane 7 is the crude lysate. (B) SDS-PAGE of the reduced (left) and non-reduced (right) purified supernatant shows that none of the low molecular weight HC band was secreted.