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The Proteins We Work With: A Guide to Supported Antigen Materials
A technical overview of how in vitro discovery platforms support VHH antibody and peptide discovery across challenging protein classes, from soluble enzymes to membrane proteins, toxic antigens and complex multimeric targets, using tailored antigen presentation strategies. Read more
Building Smarter Therapeutics with VHH Bolt-Ons
VHH antibodies provide modular, high-performance components that can enhance biologics across multiple modalities. From albumin-binding half-life extension to bi-/multi-specific engineering and intracellular TPD, VHH bolt-ons enable more flexible, efficient and targeted therapeutic design. This article examines the key applications, design considerations e case studies that illustrate how VHH domains support next-generation engineered biologics. Read more
CIS Display™ vs. Phage Display: Choosing the Right Fit for VHH or Peptide Discovery
Choosing the right display technology is a critical decision in therapeutic and diagnostic discovery procedures. This article compares CIS Display™ with Phage Display, focusing on their underlying techniques, important benefits, and suitable applications. Read more
NGS in Antibody Discovery: How Deep is Your Sequence?
Next-generation sequencing is redefining antibody discovery. From validating library diversity to uncovering rare binders and powering AI-driven design, NGS offers additional insights that enhance VHH antibody discovery and selection. Read more
Unlocking Hard-to-Drug Targets: How VHH Antibodies Overcome Drug Discovery Barriers
Today, the term ‘undruggable’ is being redefined. Advances in membrane protein solubilization, allosteric modulation, and therapeutic viral vectors have led to proof that these targets can be tackled. Read more
A Competitive and Ethical Future in Discovery
Traditionally, antibody generation relied on immunizing animals (e.g. mice, rabbits, or even llamas) to raise binders against a target antigen. However, emerging synthetic antibody library technologies now allow scientists to bypass animal immunization by using in silico designed vast libraries of human or humanized antibody fragments.
Explore the science behind our antibody discovery platforms
White Paper “Data-Driven Validation of Synthetic VHHs”
This white paper provides a data-driven validation of Isogenica’s synthetic VHH libraries, powered by Colibra® technology. Designed for biotech and pharmaceutical scientists, it demonstrates how these libraries enhance and accelerate drug discovery, particularly in oncology and immunotherapy. DownloadExtending half-lives of VHH antibodies
Because VHHs are small, they can be cleared quickly from the bloodstream. This can be a useful feature for some applications, but often a longer plasma half-life is desirable. DOWNLOADAdvantages of VHH in bi-specifics
To learn more about the application of VHHs in bi-specifics, we have condensed our expertise into a downloadable Application Note. DOWNLOADOptimizing CAR-T and T-cell antibody engagers: a role for VHH single domain antibodies
This whitepaper summarises the clinical and research landscape for CAR-T and T-cell engaging antibody therapies and show how single domain VHH antibodies can be applied to optimise the next generation of these important new therapeutic modalities. DOWNLOADIsogenica’s PD-L1 VHH as Functional Antagonists
PD-1 is an immune checkpoint protein expressed on the surface of multiple types of immune cells, including antigen-stimulated T-cells and tumour specific T-cells1. Interaction between PD-1 and its ligands (PD-L1 or PD-L2), is responsible for the regulation of T-cell activation, apoptosis, proliferation and cytokine production. DOWNLOADAnti-LRP5/6 VHH inhibits WNT pathway and prevents tumour growth
VHH are the variable domain of heavy chain only antibodies. They are small in size (~15 kD) and biophysically robust. With tunable half-lives, these antibodies are ideal for targeting inaccessible epitopes, achieving enhanced tissue penetration, multi-target binding and formatting for payload delivery… DOWNLOAD





