

Nuclera, the biotechnology company accelerating drug discovery by providing rapid, easy access to functional proteins through its benchtop eProtein Discovery System, today announced a £9 million financing extension, bringing the company’s total Series C funding to £65 million. The raise was led by Elevage Medical Technologies and Jonathan Milner, joined by existing investors British Business Bank and GK Goh. The investment will accelerate the integration of antibody expression and binding validation capabilities into the firm's eProtein Discovery benchtop system, which enables multiplex protein screening, characterisation, and expression in-house.
Expanding eProtein Discovery with antibody-specific capabilities represents a strategic step as Nuclera moves into AI-enabled protein engineering, addressing a critical industry need for scalable, standardised, and high-quality datasets that can be used to power AI models in biologics discovery. The advancement will enable researchers to perform end-to-end expression, purification, and binding validation of full-format antibodies on an integrated, high-throughput system.
Since the closure of its previous Series C financing in 2024, the company has advanced its eProtein Discovery capabilities with the addition of a membrane protein workflow, extended its global footprint to broaden customer access across APAC and the Middle East, and initiated a collaboration with Cytiva to accelerate the path from DNA to fully purified and characterized proteins to better understand drug-target interactions. In parallel, the eProtein Discovery system was installed at Domainex, the first CRO implementation of the system, streamlining protein production services and further validating the system’s commercial and scientific impact.
Combining unique cell-free expression systems, novel digital microfluidics, and robust screening data, eProtein Discovery provides clear guidance on which protein has the best chance of success early on, thereby reducing the time, cost, and uncertainty traditionally associated with protein expression and purification.