Phage display platform
Fully human VHH synthetic library
Efficient and Diversified
Extra-large storage capacity
High positive screening rate
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Introduction to the Fully Human Fab Synthetic Library Service
The fully human VHH synthetic library phage‑display platform is an antibody discovery system that seamlessly integrates phage‑display technology with a fully human VHH (single‑domain antibody) synthetic library, enabling efficient “fishing” and precise recognition between vast libraries of nanobodies and target proteins. Leveraging a pre‑designed, massively diversified VHH gene library, this platform displays compact, highly stable single‑domain antibody fragments on the phage surface, allowing rapid screening—from target to high‑affinity binders—within just a few weeks. Combining high throughput, flexibility, and speed, it stands as an indispensable, cutting‑edge innovation tool in next‑generation antibody drug development.
In addition to the development of fully human VHH synthetic library antibodies, our antibody discovery services also include:
Fully human Fab synthetic library
Alpaca immune library
Hybridoma Platform
Leveraging its proprietary phage‑display platform, Xichang Bio has assembled a team of scientists dedicated to the discovery and production of fully human VHH antibodies, thereby establishing a distinctive competitive edge in the field of fully human antibody discovery.
Key Highlights of the Fully Human VHH Synthetic Library Development Service
Fully humanized design
◉ Natural human germline gene framework
◉ Low immunogenicity risk and high drug-likeness
Huge storage capacity and diversity
◉ Storage capacity exceeds 4 × 10^10
◉ Employing a Trimer primer-based randomization strategy
High positive screening rate
◉ Molecules with nM–pM-level affinity
◉ Complete high-throughput screening within 2–3 weeks.
Affinity distribution of fully human VHHs developed by Xichang Bio
Process for Developing a Fully Human VHH Synthetic Library
Antigen expression or provided by the customer.
The curation and screening of the library’s collection
Upper-clearance off-rate screening
Cross-reactivity among species
VHH verification
VHH expression
Sequencing and sequence analysis of VHH-positive clones
Cell adhesion assay
Development and Application of a Fully Human VHH Synthetic Library
01
The fully human VHH synthetic library, owing to its single-domain architecture, high stability, and low immunogenicity conferred by its fully human sequence, has been widely employed in tumor immunotherapy, inflammatory diseases, and in vitro diagnostics.
02
In tumor immunotherapy, VHH‑based drug candidates targeting PD‑L1, HER2, and other antigens have been identified through phage‑display screening from fully human VHH libraries, and their therapeutic potential has been thoroughly validated in preclinical studies.
03
In the design of the antigen‑binding domain of CAR constructs, VHHs—owing to their small molecular size and the absence of light‑chain mismatch—can reduce the risk of tonic signaling and enhance tumor penetration, demonstrating superior safety and durability in CAR‑T therapies targeting a variety of antigens.
Details of the Fully Human VHH Synthetic Library Development Service
Case Study on the Development of a Fully Human VHH Synthetic Library
Frequently Asked Questions
How does the immunogenicity risk of fully human VHH compare with that of conventional camel‑derived or murine VHH?
The fully human VHH sequence is entirely designed based on the germline framework of human antibodies, with a humanization rate exceeding 98%, thereby fundamentally mitigating the risk of immunogenicity associated with heterologous proteins. In clinical applications, no additional humanization modifications are required, significantly reducing the likelihood of anti-drug antibody (ADA) formation and making it particularly well-suited for therapeutic regimens involving long-term, repeated dosing.
Do fully human VHHs still require affinity maturation or humanization?
Do fully human VHHs still require affinity maturation or humanization?
Why is VHH more advantageous than sCFv in CAR-T cell therapy?
Why is VHH superior to sCFv in CAR-T cell therapy?
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