The lead product, Hupresin®, makes it possible to purify efficiently butyrylcholinesterase, which should facilitate its large scale production. The innovative Hupresin® technology results from the combination of two elements: a custom synthesized compound called huprine having an appropriate affinity for cholinesterases and a selected solid support on which the huprine ligand is grafted. The resulting affinity resin has perfect characteristics to specifically bind cholinesterases, providing the best performances on the market.



The Hupresin® technology and the synthesis of huprine derivatives are internationally patented (WO2011124712 & WO2015077317). In addition, our R&D team continues to develop new ligands for manufacturing of new more efficient resins for the purification of BChE.




Because of the fitted affinity of Hupresin® for butyrylcholinesterase, the purification of the enzyme is possible in a single step. The Hupresin® has proven to have a higher capacity and a higher specificity for butyrylcholinesterase leading to a better enzyme quality, a better enzyme yield and a shorter production time. The performances of Hupresin® will help producing butyrylcholinesterase at lower cost and in optimized manufacturing time. Hupresin® is available in 10 mL, 100 mL and 500 mL batches.

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New !!! Hupresin® AC

Hupresin® AC ligand has been grafted on a Fast Flow Sepharose matrix. This new affinity resin has proven to be efficient for the purification of plasmatic butyrylcholinesterase. Hupresin® AC is available in 10 mL, 100 mL and 500 mL batches.

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Hupresin® Magnet

Hupresin® magnet is the magnetic version of Hupresin® resulting rom the grafting of a hupresin derivative on a magnetic solid support. The research and development platform of CHEMFORASE is now working on the optimization of Hupresin® Magnet to provide the best performances. This technology might facilitate the development of diagnosis tool useful for proving exposure to nerve agents and for identifying the type of poison involved. Hupresin® Magnet is available in 500 µL batch.

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The cholinergic system is based on the neurotransmitter acetylcholine (Ach) and found widely distributed in both central and peripheral nervous systems. Cholinesterases are a family of enzymes that catalyze the hydrolysis of Ach into choline and acetic acid, an essential process allowing for the restoration of the cholinergic neuron. Cholinesterases are divided into two: acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). AChE participates in cholinergic transmission by hydrolyzing acetylcholine and is expressed in nerve and blood cells. Compared to AChE, the physiological role of BChE is not well understood.



Butyrylcholinesterase from human plasma is a potential drug candidate that can be employed in several therapeutic fields. Enhancement of endogenous levels of hBChE can:


  • protect against the toxicity of
  • organophosphate pesticides and nerve agents
  • reduce risks of complications due to cocaine abuse
  • reverse muscle relaxant-induced apnea following surgery anesthesia
  • alleviate symptoms caused by local anesthetics

It can be used either prophylactically or as a treatment drug. While production of hBChE by genetic engineering methods provide reasonable quantities of the enzyme, the purification step still remains limited in terms of efficacy and time. Our new affinity gel, Hupresin® , has been proven to be superior to the classical methods for purification of both recombinant human BChE and plasma BChE because of its higher binding capacity and its higher specificity for hBuChE. A single purification step can yield larger quantities of highly pure BChE. This new chromatographic support will help to reduce the costs associated for the production of BChE-based drugs such as nerve agents bioscavengers.