REAL MEMBRANE PROTEINS
THE PROBLEM: Membrane proteins are difficult to express, fold, and stabilise. Their complex structure, containing both hydrophobic and hydrophilic domains, makes them particularly challenging to work with. Overexpression in cells can lead to toxicity, and maintaining structural integrity after purification is difficult.
COMMON PROBLEMS
Fragments
Cell-Based Expression
Detergents
Cell-Free With Nanodiscs
ALiCE® MAKES MEMBRANEPROTEINS ACCESSIBLE
ALiCE® recreates the natural process of membrane protein expression. It uses ribosome-studded microsomes with active SEC translocation pathways, enabling proteins to be inserted into membranes during translation. This results in native-like folding and functional integrity. Without living cells, ALiCE® allows high expression levels without toxicity limitations. Proteins can then be isolated within their native lipid environment using copolymers.

KEY BENEFITS
- Full-length proteins
- Native membrane environment
- High yields
- Functional integrity
PROOF
CASE 1:
Increased yield with maintained function
ALiCE® produced a multi-pass membrane protein with approximately 100 µg/mL yield, compared to less than 2 µg/mL in HEK systems. Binding activity remained comparable, with over 90% purity achieved in a single purification step.
CASE 2:
First full-length expression of FGFR3-TACC3
After decades of research challenges, ALiCE® enabled full-length expression of FGFR3-TACC3, achieving yields greater than 300 µg/mL with minimal optimisation.
APPLICATION
ALiCE® is available as a service for outsourced projects or can be implemented directly in your laboratory.