production platform

Leveraging the speed and agility of eukaryotic
cell-free expression protein expression.
expressing proteins in a single tube using microsome cell free expression technology.
Cell-free protein expression (CFPE) systems derived from crude cell extracts have been used for decades as a research tool and have introduced many attractive advantages to protein expression technology. However, a critical barrier to the adoption of CFPE systems as alternatives to cell-based approaches has been the problem of relatively low protein yields.
To address this problem, Bombi has taken advantage of plant cell biology and developed a novel eukaryotic cell-free expression system: MICE.
Our MICE-T utilizes tobacco cell lysates, depleted of vacuoles. Compared to other cell-free expression systems, the key differentiator of MICE-T is that its intact protein production machinery reflects that of a living cell.  It has built-in active energy storage and regeneration and includes everything necessary for in-vitro transcription (RNA polymerases, NTPs), translation reactions (ribosomes, translation initiation/elongation factors, tRNA, etc.), protein folding, disulfide bonding, and glycosylation.
Using a simple protocol, both the RNA transcription and translation take place in a single tube (combined transcription/translation). Reactions are started by simply mixing plasmid DNA with a proprietary reaction mix. The outstanding protein yields are based on highly efficient protein expression over the duration of the reaction which takes approximately 48 hours.
continuous growing of tobacco by-2 cells
Nicotiana tabacum BY-2 cells are growing continuously in a specially designed rocking wave bioreactor at a constant packed cell volume and a doubling time of around 35 hours to ensure a reproducible supply of homogeneous cell material.
protoplast generation
The cells are harvested during the exponential growth phase and treated with a proprietary enzyme mixture to digest the cell wall to generate protoplasts.
Low-density vacuoles contain a great part of undesirable enzymes, including proteases and ribonucleases that can reduce protein expression.  They are removed by density-gradient centrifugation which yields high-density evacuolated protoplasts.
protoplast lysis
The recovered evacuolated protoplasts are washed, treated with a protease inhibitor mixture and lysed by nitrogen cavitation to  protect labile components from oxidation. The nuclei and non-disrupted cells are removed by centrifugation. The resulting reproducible cell-free homogenates are generated after nuclease treatment and nuclease deactivation. 
Protein expression
The system contains all factors required for in vitro transcription (RNA polymerases, NTPs) and translation reactions (ribosomes, translation initiation/elongation factors, tRNA, etc.). Both the RNA transcription and translation take place in a single tube (coupled transcription/translation). Protein expression takes place during the reaction which approximately takes 48 hours.
The isolated and extracted recombinant protein from the coupled cell-free lysate undergoes industry standard protein purification before finishing the biologic in its final form.
From gene sequence to protein production in as little as 7 days
Designed to accurately match the gene of interest
Ability to produce different proteins at the same time
The platform is linear scalable just by growing more BY-2 cells
glycan engineering

With increasing commercial opportunities for biotherapeutics across global markets, demands are as high as ever for technologies that can support production of complex glycoproteins. N-linked glycosylation is a common post-translational modification to many proteins that may influence biological activity, protein conformation, stability, solubility, secretion, pharmacokinetics, and antigenicity.

Consequently, the ability to control and tailor N-glycosylation is critical for today’s antibody engineering. Bombi’s MICE platform provides in-situ glycan engineering, supported by multi-attribute analytical methods such as mass spectrometry to elucidate and quantify precise glycoforms on recombinant proteins.

why glycan engineering?

Bombi's MICE platform delivers products with inherently greater N-linked glycosylation homogeneity versus competing platforms:

  • Bacteria do not glycosylate. Yeast hyperglycosylate. Chinese hamster ovary [CHO] cell lines do not precisely mimic human glycosylation patterns and intellectual property barriers limit access to glycosylation controls in CHO.

  • N. tabacum BY-2 cells  do not attach α1,6-fucose, terminal β1,4-galactose residues or any sialic acid residues, leading to simpler, more homogeneous N-linked glycosylation patterns than other eukaryotic expression platforms.  It adds α1,3-fucose.



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several targets to tackle antimicrobial resistance.