Recombinant AMH Protein Expression and Purification

Recombinant AMH protein was expressed and purified, as previously reported (6 (link), 20 (link)). Briefly, AMH with an enhanced cleavage site albumin leader, Q425R MIS (LR-MIS) was produced using a stable Chinese hamster ovary cell line (6 (link), 23 (link)). Conditioned media was purified using an affinity chromatography column, with 6E11 antibody primary amino coupled to an N-hydroxysuccinimide (NHS) column (Cytiva) (6 (link), 23 (link), 35 ). AMH mature was then purified away from the prodomain by reverse phase chromatography and stored for future use, as previously reported (20 (link)).

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Hart K.N., Stocker W.A., Nagykery N.G., Walton K.L., Harrison C.A., Donahoe P.K., Pépin D, & Thompson T.B. (2021). Structure of AMH bound to AMHR2 provides insight into a unique signaling pair in the TGF-β family. Proceedings of the National Academy of Sciences of the United States of America, 118(26), e2104809118.

Publication 2021

NHS) column

Affinity chromatography Albumin Antibody Cell line Chinese hamster Cleavage Conditioned media Ovary Recombinant protein Reverse phase chromatography

Corresponding Organization : University of Cincinnati

Other organizations : Monash University, Swinburne University of Technology, Massachusetts General Hospital, Harvard University

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Variable analysis

independent variables

Expression and purification of recombinant AMH protein

dependent variables

Purification of AMH mature from the prodomain

control variables

Use of stable Chinese hamster ovary cell line for AMH production
Affinity chromatography column with 6E11 antibody for purification
Reverse phase chromatography for further purification of AMH mature

controls

Positive control: Not explicitly mentioned
Negative control: Not explicitly mentioned

Annotations

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