Fig. 1.
Fig. 1. Expression and purification of Epo (R103A). / (A) A 10% sodium dodecyl sulfate gel of a typical purification is shown. Load indicates the yeast-conditioned media loaded on the Ni2+ column. BT indicates the breakthrough fraction, wash indicates the 3 wash fractions, elution indicates the three 1-mL fractions eluted with 0.25 M imidazole, and pool indicates the final pooled product. (B) An immunoblot of the Epo (R103A) preparation using polyclonal rabbit anti-Epo antibody. (C) N-terminal protein sequence of yeast-expressed Epo (R103A).

Expression and purification of Epo (R103A).

(A) A 10% sodium dodecyl sulfate gel of a typical purification is shown. Load indicates the yeast-conditioned media loaded on the Ni2+ column. BT indicates the breakthrough fraction, wash indicates the 3 wash fractions, elution indicates the three 1-mL fractions eluted with 0.25 M imidazole, and pool indicates the final pooled product. (B) An immunoblot of the Epo (R103A) preparation using polyclonal rabbit anti-Epo antibody. (C) N-terminal protein sequence of yeast-expressed Epo (R103A).

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