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Our phage display service offers a rich naïve library of 1.51 × 10¹⁰ variants, enabling the discovery of unique nanobodies in fewer panning rounds.
Leverage immune system priming with your own VHH library to increase the chances of isolating target-specific VHHs compared to a naïve library.
VHHs are easy to produce in all three systems, letting you select the expression system that best fits your application.
Receive at least 3 unique VHH candidates to compare affinities, design bispecific formats, and confidently advance development decisions.
Alpaca and llama VHHs offer higher VH homology, while camel VHHs provide longer CDR3s and greater diversity for challenging targets. Our experts will guide you on what is best for your project.
Case report
Case Report: Accelerating Early-Stage Discovery of PD-1-Targeting VHH Candidates for Non-Small Cell Lung Cancer Research
Thanks to their compact size (~15 kDa), VHHs penetrate tissues more easily than full-length antibodies, diffusing rapidly and clearing quickly. This makes them ideal when fast and efficient tissue access is critical.
Their small size allows VHHs to bind epitopes that traditional antibodies can’t reach, increasing the chances of discovering unique, high-affinity binders.
VHHs are highly stable, resisting heat, pH changes, and proteases while maintaining binding functionality. This allows their use in diverse applications such as capturing reagents or biosensing.
VHHs present a low immunogenicity thanks to their small size and to their high sequence homology with the human VH gene family III.
Develop targeted therapies using VHHs’ small, stable, and highly soluble properties to deliver payloads precisely without compromising binding.
Amplify your therapeutic effect by creating VHH-Fc or VHH-IgG fusions for enhanced targeting and functionality.
Tool
Briolay, T., Petithomme, T., Gravoueille, & al. (2025). Development of potent Affitin-based bispecific NK cell engagers for the therapy of MSLN-expressing cancers. Molecular Therapy: Oncology, 33(4), 201095.
Li, Z., Alshagawi, M. A., Oot, R. A., Alamoudi, & al. (2024). A nanobody against the V-ATPase c subunit inhibits metastasis of 4T1-12B breast tumor cells to lung in mice. Oncotarget, 15, 575–587.
We have been working with ProteoGenix since 2023 on the discovery of a VHH targeting a highly challenging surface protein. Using their proprietary LiAb-VHHMAX™ library, they successfully identified 4 specific binders which demonstrated specific target binding with no detectable off-targets. Working hand-in-hand, we continued our partnership on epitope mapping to identify the exact binding site, and ProteoGenix also determined the dissociation constant (KD), which perfectly matched our desired affinity range. Throughout the process, ProteoGenix’s extensive experience and scientific expertise have been invaluable. Their professional guidance and thoughtful advices helped us make the right strategic choices and advance our project efficiently and confidently.