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QMCF Technology

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QMCF Technology

Our QMCF Technology is a proprietary, fast, and reliable transient mammalian expression system for recombinant protein production with high yields of up to 1g/L. QMCF utilizes genetic modifications which increase the expression vector copy-number while ensuring their even distribution during cell division, guaranteeing near-stable expression levels.

QMCF-made recombinant proteins are suitable for pre-clinical in vivo & in vitro studies, structural biology, drug discovery and as well as for commercial diagnostic assays. 

QMCF Technology Highlights



We use QMCF and ProBioGen GlymaxX® technologies fused together to produce afucosylated antibodies.



Patented QMCF technology in CHO and HEK293 cells provide high affinity antigens as well as antibodies.



Scale-up from 96 well plate to tens of liters.




By using QMCF technology more than 15 years, we have improved and heavily used this platform for protein production. On average 1500 proteins are produced and 1250 different proteins purified annually.



Over 100 different expression vectors to cover different promoters, antibody backbones for various antibody formats and mutations (Fc mutated).


Science behind QMCF Technology

QMCF plasmids carry hybrid replicons composed of mouse polyomavirus core replication origin in combination with Epstein-Barr virus EBNA-1 protein binding sites (FR — Family of Repeats) as nuclear retention elements. Stably expressed EBNA-1 and polyomavirus Large T proteins in CHOEBNALT85 cell line ensures the replication and maintenance of QMCF expression vectors in QMCF cells.
HEK293 and CHO based QMCF cell lines are stable cell lines expressing EBV EBNA-1 protein and PyV Large T antigen. pQMCF expression plasmids comprise of mouse polyomavirus (PyV) core replicon, the FR element of EBV, and an expression cassette with multicloning site (MCS) for expression of gene of interest (GOI).

Comparison between two CHO-based
expression systems


Compared to two CHO based expression systems, QMCF is robust and efficient enabling production of proteins that others fail. QMCF had higher productivity for 13 of 21 produced targets.
Read the paper here.

Fusion protein strategy

Fusion domain (FD) increases the production of proteins, that are challenging even with QMCF expression technology. Our data shows extremely high production without fusion cleavage, as it is not necessity and do not alter the immunization. Fusion domain increases the production of  ADAMTS13 ~20 fold. 


We have licensing options for QMCF Technology for protein production. For further information please contact:


Silla, et al, Episomal Maintenance of Plasmids with Hybrid Origins in Mouse Cells; Journal of Virology, Dec 2005: 15277-15288. Read the paper here.
Kasemaa K, Talts K, Täht E, Toots U, Ustav M. DNA Transfer into Animal Cells Using Stearylated CPP Based Transfection Reagent. Methods Mol Biol. Novebmer 2021: 569-578. Read the paper here.
Arukuusk P, Pärnaste L, Oskolkov N, Copolovici DM, Margus H, Padari K, Möll K, Maslovskaja J, Tegova R, Kivi G, Tover A, Pooga M, Ustav M, Langel U. New generation of efficient peptide-based vectors, NickFects, for the delivery of nucleic acids. Biochim Biophys Acta. 2013 May;1828(5):1365-73. Read the paper here.
Malm M, Kuo CC, Barzadd MM, Mebrahtu A, Wistbacka N, Razavi R, Volk AL, Lundqvist M, Kotol D, Tegel H, Hober S, Edfors F, Gräslund T, Chotteau V, Field R, Varley PG, Roth RG, Lewis NE, Hatton D, Rockberg J. Harnessing secretory pathway differences between HEK293 and CHO to rescue production of difficult to express proteins. Metab Eng. 2022 Jul;72:171-187. Read the paper here.
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