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)).
Nhs column
Manufactured by Cytiva
The NHS) column is a chromatography column designed for the purification of proteins. It is commonly used in the field of biotechnology and pharmaceutical research. The column contains a matrix that is capable of binding to proteins with N-terminal histidine tags, allowing for the selective capture and purification of these tagged proteins from complex mixtures. The core function of the NHS) column is to facilitate the efficient separation and purification of target proteins of interest.
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Lab products found in correlation
2 protocols using nhs column
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Recombinant AMH Protein Expression and Purification
2
Purification of Recombinant AMH Protein
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Recombinant AMH protein was expressed and purified as previously reported10 (link),35 (link),36 (link),39 . Enhanced AMH protein containing an albumin leader sequence and Q450R mutation for enhanced cleavage (LR-MIS) was produced using a stably transfected Chinese hamster ovary cell line. Conditioned media was initially purified by affinity chromatography using an N-hydroxysuccinimide (NHS) column (Cytiva) primary amine coupled with full-length 6E11 antibody. A second size-exclusion chromatography step using a Superdex Increase 200 column (Cytiva) was used to separate dimeric AMH from oligomer species.
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