Catalog No. : LEN-AL0103050

ALiCE™ Mini Kit

ALiCE™ Mini Kit



High yields in protein expression are key for high-throughput approaches with complex proteins and ultimately, translation into products. LenioBio will provide a range of tools to express proteins in any quantity required, including the notoriously difficult ones, based on the ALiCE® platform.

Just add DNA template and go!

With LenioBio’s simple, one-step, cell-free protein expression technology ALiCE™, it takes just hours to obtain various “difficult to express” proteins, including:

  • Antigenic vaccine components
  • Antibodies and antibody fragments
  • Peptide and protein hormones
  • Membrane proteins and glycoproteins
  • Cytotoxic proteins


  • 3 mg/mL protein in batch mode
  • Up to 30 times more protein at market competitive prices
  • Active mitochondria drive the reaction
  • Already validated for over 500 proteins
  • Post-translational modification (e.g. folding, disulfide bonds, glycosylation, etc)
  • Applicable across all industries and research fields

ALiCE®: 30 times more protein than other eukaryotic systems

ALiCE® produces up to 3 mg /mL in batch mode. This is 30 times more than any eukaryotic cell-free system currently being sold (including wheat germ, CHO, human, etc.). And, since pricing is similar, you get 30 times more proteins for each euro spent. 

AliCE® kit: Easy to use

ALiCE® is a radically different approach to cell-free expression and a platform unlike any others. Yet, your current cell-free expression processes can be easily translated to ALiCE® and you can expect yields you have never witnessed before.

Expression in the cytosolic fraction

  • Simply add the gene (e.g. within a plasmid) to the lysate
  • No need for multiple pipetting steps or other adjustments

Disulfide bonds

  • Simple addition of disulfide bonds
  • Addition of signal peptide triggers directing of proteins to microsomes
  • Mild detergent opens microsomes for collection

ALiCE®: Complexity made simple

ALiCE® produces notoriously difficult-to-express proteins. Both eukaryotic and prokaryotic cell-free systems fail to produce the most complex proteins at relevant quantities. ALiCE® has consistently proven its ability to successfully express both simple proteins like reporter proteins, as well as highly challenging ones, such as full-size antibodies.

ALiCE®: active mitochondria drive the reaction and microsomes enable complex protein structures 

The power of Alice lies in its intact organelles: active mitochondria provide a continuing energy supply and microsomes (endoplasmic reticulum reformed into vessels) enable folding of complex proteins and their glycosylation. This gives you a remarkably easy and scalable tool to express a broad spectrum of proteins. 

ALiCE®: across all industries and research fields

ALiCE® has been applied for years within Corteva Agriscience, the agrobioi division of DowDoPont, as well as Fraunhofer IME to express over 500 proteins of varying types. This shows that ALiCE® is applicable for any purpose, be it for biopharmaceuticals, technical enzymes, crop development, metabolic pathways, fundamental research, etc. 

Examples - Overview of proteins expressed in ALiCE®

Photos by courtesy of Simon Vogel and Matthias Buntru, Fraunhofer IME

Find more details in the Other Specifications section below.

Important Note: LenioBio GmbH offers this product under the provision that purchaser agrees to the Limited Use Label License 2018-09-09.1. For this document please refer to LenioBio webpage 
ItemSize Application Price
ALiCE™ Mini Kit

6 x 50µl

Extraction $750.20

How do we do it?

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, LenioBio has taken advantage of plant cell biology and is bringing to the market a novel eukaryotic cell-free expression system ALiCE® that yields significant quantities of protein. We start our proprietary production process with a robust and fast-growing tobacco cell line. We then remove the plant cell vacuoles, which contain harmful hydrolytic enzymes that can degrade lysate performance. What remains is an “almost living” extract containing the complete protein production machinery. 

ALiCE® cell-free eukaryotic protein expression kits provide outstanding value for money, lowering your cost to produce one mg of protein by as much as 100-fold, compared to competing kits.

A closer look on proteins expressed in ALiCE®

Full Size Antibody M12

  • 0.14 mg/mL protein in an earlier version of ALiCE®*
  • Hetero Tetramer which contains disulfide bonds
  • Directed to microsome for folding
  • Functionality verified with ELISA testing

*Buntru et al., Biotechnology and Bioengineering, 2015, Vol. 112, No. 5

Glucose oxidase

  • 1mg/mL protein
  • Homodimer which contains disulfide bonds
  • Directed to microsome for folding
  • Activity determined with colorimetric assay

Enhanced Yellow Fluorescent Protein (eYFP)

  • 3mg/mL protein
  • Has been expressed in 3 mL reactions
  • Monomer which contains no disulfide bonds
  • Activity determined with fluorescent assay

Membrane protein HB-EGF fused to eYFP

  • Heparin Binding - Epidermal Growth Factor - eYFP
  • Full size protein expressed with only minor signs of
  • Fragmentation
  • Protein incorporated into the microsomal membrane (arrow)


History: A decade of development

As a novel plant-based cell-free system, ALiCE® was developed within the Fraunhofer Institute (Germany) “Cell-free Bioproduction” Lighthouse Project from 2010–2014 and the federally funded R&D project “building blocks for industrial cell” (see publications). The strategic collaboration with Corteva Agriscience™, the Agriculture Division of DowDuPont™, brought ALiCE® the maturity, competences and funds needed to realize its breakthrough performance of 3000 µg per mL.

Since 2016, LenioBio has been optimizing the system for the expression of pharmaceutical proteins, technical enzymes, and other protein classes, and in March 2018, we obtained exclusive licenses from Dow and Fraunhofer to commercialize the technology under the brand name ALiCE®.

ALiCE®: A scalable platform

The key differentiator of ALiCE® compared with other cell-free expression systems is that its intact protein production machinery reflects that of the living cell. It has an active energy regeneration and includes everything necessary for protein folding, disulfide bonding, and glycosylation. Beyond its ease of use and unprecedented yields, ALiCE® also finally enables fully scalable cell-free eukaryotic expression.

The easy processes and scalability of ALiCE® will drastically reduce the development costs of protein-based products. To date, each scaling step requires adapting living cells in new conditions, which affects productivity and possibly even the protein candidates themselves. For example, the optimization of protein expression when scaling up recombinant CHO cells can take more than one year. Scaling up in ALiCE® sidesteps many of the complexities of cell-based systems and allows for much faster process development.

LenioBio will be realizing the potential of ALiCE® by merging the superior productivity, the unique ease of use (“just add the DNA”), the capability of expressing complex proteins, humanized glycosylation and its cost-effective structure into one platform.

ALiCE®: Publications by peers

Scientific reports where ALiCE® (>3 mg/mL) is applied will be published soon.

The Fraunhofer Institute IME have been working on the precursor of ALiCE® (up to 0.4 mg/mL) for an extended period and the experiences of our peers can be found in the following publications:

  • Buntru et al. Tobacco BY-2 cell-free lysate: an alternative and highly-productive plant-based in vitro translation system. BMC Biotechnology 2014;14:37.
  • Buntru et al. A versatile coupled cell-free transcription–translation system based on tobacco BY-2 cell lysates. Biotechnology and Bioengineering 2015;112(5):867–878.
  • Havenith et al. Combination of two epitope identification techniques enables the rational design of soy allergen Gly m 4 mutants. Biotechnology Journal 2017;12:1600441.
  • Huck et al. Combined 15N-labeling and TandemMOAC quantifies phosphorylation of MAP kinase substrates downstream of MKK7 in Arabidopsis. Frontiers in Plant Science 2017;8:2050.

Photos by courtesy of Simon Vogel and Matthias Buntru, Fraunhofer IME


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