Our Science

Our platform combines cutting edge science with a rational, reproducible process

Applying our proprietary antibody discovery and engineering technology, we generate highly potent and stable antibody Fv fragments, which serve as building blocks to create mono- or multispecific antibody fragment-based therapeutics with tailored pharmacokinetic (PK) properties. Our multi-specific approaches are designed to enable novel modes of action, combine synergistic functions into a single product candidate and restrict activity to specific tissues in the body to limit off-target toxicities.

Our technology platforms allow to overcome limitations of conventional antibodies, alternative scaffold, and single-domain antibody technologies and to improve the probability of success in discovery and development. Numab’s plug-and-play platform allows for a highly rational and reproducible process to rapidly yield clinical candidates with unmatched CMC characteristics supporting high-yield manufacturing and high-concentration formulation.

At the heart of our plug-and-play platform are a modular scaffolding technology – the λ-Cap™ – with unprecedented stability, and the ability to generate highly stable multispecific antibody formats. Together these two cornerstones fuel our ability to generate a broad variety of first in class Multispecific Antibody-based Therapeutics by Cognate Heterodimerization, or MATCH™ for short.


Engineering next generation biologics

  • Human antibody variable region (Fv) fragments with unprecedented potency, stability and solubility present ideal building blocks for multispecific therapeutics with modern drug properties.
  • Modular assembly of multispecific molecules from stable Fv building blocks enables realization of novel mechanisms of action.
  • Ultra-high throughput discovery engine yielding panels of best-in-class potency antibodies on repeatable basis.

Our Technology

Ultra-high throughput antibody discovery

Rabbit antibodies – high yield of high affinity

While our human acceptor scaffold and MATCHTM-formats are in principle applicable to antibodies from any source (human, rodent, etc.), our proprietary pipeline is fuelled by a powerful combination of rabbit immunization and an ultra-high throughput flow cytometry procedure to exhaustively characterize the full rabbit antibody repertoire of hundreds of millions of antibodies, in a few days. Our discovery process typical yields panels of hundreds of high-affinity monoclonal antibodies.

Stabilized and Humanized Antibody FV fragment

Highly Stable Building Blocks

Our proprietary λ-CapTM technology is the basis of our highly stable, fully human variable region fragment, or Fv, acceptor scaffold onto which complementary-determining regions, or CDRs, from conventional antibodies can be engrafted.

Numab stabilizes its antibody Fv fragments by exchanging a notoriously unstable part of the scaffold (FW4 of Vϰ) by a stability conferring sequence referred to as λ-CapTM (FW4 of Vλ).

A scaffold with unmatched stability

Traditionally, antibody Fv fragments have proven intractable to therapeutic use due to their inherent instability. With an elegant engineering step, Numab has overcome this hurdle by replacing a short stretch of a human variable light kappa-chain with the equivalent λ-chain stretch at the C-terminus of the light chain. This results in a fully human Fv acceptor scaffold with unmatched stability on which CDRs (complementarity determining regions) from any monoclonal antibody can be engrafted, irrespective of their origin, be it human, rodent, or rabbit. The so-called λ-CapTM constitutes a true breakthrough and endows our human acceptor scaffold with hitherto elusive stability. The resulting favorable properties have effectively turned the humanization/stabilization procedure into a routine procedure for most antibodies while maintaining their affinity and on the whole, adopting the favourable human acceptor scaffold’s biophysical properties.

Numab Numab Numab Numab

Differentiated Multi-specific Therapeutics

Multispecific Antibody-based Therapeutics by Cognate Heterodimerization (MATCHTM) is a modular scaffolding technology with unprecedented stability, and the ability to generate highly stable multispecific antibody formats.

The proprietary, highly flexible, multi-specific format has the potential to incorporate up to six λ-CappedTM Fv fragment building blocks and, consequently, to allow for up to six binding specificities.

The MATCHTM format is a heterodimer that can contain up to six different antigen-binding sites. The variable heavy (VH) and light (VL) chains of the two core domains are placed in two separate protein chains, and their highly stable VH-VL interfaces drive the MATCHTM format’s heterodimerization.

MATCHTM formats can incorporate up to six λ-cappedTM Fv building blocks and binding specificities in a true plug-and-play fashion. Most importantly, the stability of the λ-capped Fv fragments and the fact that they do not aggregate confer excellent CMC properties on MATCHTM molecules.

Differentiating Properties


Potency Ultra-high potency rabbit antibodies


Multi-specificity Up to 6 different MoAs in one molecule


Manufacturability High yield manufacturing in platform antibody process


Formulability Concentration enables convenient self administration


Pharmacokinetics Prolonged serum half-life engineering & convenient dosing


Safety Proprietary technology to reduce immunogenicity

Posters and Publications

ND021 – Poster presentation at AACR Annual Meeting 2020 Download PDF

ND021 – Poster presentation at AACR Annual Meeting 2022 Download PDF

ND021 – Poster presentation at SITC Annual Meeting 2022 Download PDF

ND026 – Poster presentation at EADV Congress 2022 Download PDF

ND028 – Poster presentation at SITC Annual Meeting 2020 Download PDF

ND028 – Poster presentation at AACR Annual Meeting 2022 Download PDF

ND032 – Poster presentation at SITC Annual Meeting 2021 Download PDF

ND032 – Poster presentation at SITC Annual Meeting 2023 Download PDF

Egan TJ et al. Novel multispecific heterodimeric antibody format allowing modular assembly of variable domain fragments Download PDF

Johansson MU et al. Design of antibody variable fragments with reduced reactivity to preexisting anti-drug antibodies Download PDF

Snell D et al. An engineered T-cell engager with selectivity for high mesothelin-expressing cells and activity in the presence of soluble mesothelin Download PDF

Warmuth S et al. Engineering of a trispecific tumor-targeted immunotherapy incorporating 4-1BB costimulation and PD-L1 blockade Download PDF

Stay informed.

Cookies: OK! Privacy Statement