Recombinant VHH Antibodies

Partner with Rockland for immune-derived, antigen-matched VHH antibodies developed through our integrated camelid immunization and recombinant engineering platform. Our service delivers high-affinity, high-specificity antibodies engineered for demanding applications, from cryptic epitope detection and enzyme active site binding to virus neutralization and molecular imaging.

Our platform combines hyperimmunized camelid programs with single-cell selection from clonal display to generate reproducible antibodies tailored to your research or development goals. Recombinant VHH antibodies can be produced in bacterial, yeast, or mammalian expression systems and customized for your preferred format or application.

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Immunized VhH Antibody Platform

Accelerate your diagnostic or therapeutic programs with VHH antibodies that reflect true, in vivo immune responses. Rockland’s immunized VHH antibody platform produces purified, recombinant VHH antibodies in 14–24 weeks, engineered from antigen-specific immune responses.

By starting with immune-derived, antigen-matched VHH repertoires, our workflow preserves natural affinity maturation and developability traits. The result is high-performance VHH antibodies with the stability, specificity, and reproducibility required for demanding applications.

Antigen Preparation & Camelid Immunization

Our immunized VHH antibody platform starts with the preparation of the target antigen to increase its immunogenicity (capacity of a given antigen to induce an antibody response). Our experts can advise on the best methodology for antigen preparation and immunization.
VHH DNA Library Construction

The animal is then immunized with the target antigen, and the antibody response is monitored over time according to Rockland validated protocols.
Phage Display VHH Library Construction

Once the desired level of antibody is obtained, blood is harvested from the animal for the extraction of total RNA and used for construction of an immunized VHH antibody phage display library.
Phage Display VHH Library Panning/Screening

The library is then enriched for target antigen-specific binders by repetitive “panning”, a screening process that identifies individual positive antibody clones.
VHH Antibody Expression & Characterization

Each VHH antigen-specific clone obtained is expressed, purified, and characterized as desired (e.g., binding in ELISA or Western blots, bioassays, affinity assessment, flow cytometry, immunohistochemistry, etc.).

Why Partner with Rockland for VHH Antibody Development?

Rockland combines decades of antibody development expertise with specialized capabilities in camelid immunization, clonal display (phage or yeast), and recombinant VHH expression. Every project is supported by experienced scientists who help define an optimal strategy for your antigen, intended application, and downstream development needs.

What sets our VHH immunized library services apart:

Immune-derived VHH discovery for greater specificity and relevance
Camelid (llama or alpaca) immunization with your antigen, delivering VHHs with natural affinity maturation and higher biological relevance
Customizable schedules, adjuvants, and antigen formats to support even challenging targets
Affinity, specificity, cross-reactivity, and paired antibody selection to ensure assay-ready or development-ready performance
Recombinant production tailored to your application
Bacterial, yeast, or mammalian expression with optional Fc fusions, tags, signal peptides, and multi-specific formatting
Transparent data packages
Development and review by expert antibody engineers to support research, diagnostic development, or preclinical evaluation
Scientific partnership throughout the project
Collaborative guidance from concept to final deliverable

Frequently Asked Questions (FAQs) About VHH Antibodies

VHH antibodies, also called nanobodies or single-domain antibodies, are small (~11–15 kDa) antibody fragments derived from the variable heavy domain (VHH) of naturally occurring heavy-chain-only antibodies (HCAbs) found in camelid species such as llamas and alpacas. Unlike conventional IgG antibodies, VHHs comprise a single variable domain, yet retain full antigen-binding capability and can be recombinantly engineered into diverse formats for research, diagnostic, and therapeutic applications.

HCAbs are a unique class of antibodies that naturally lack light chains and do not contain the CH1 constant domain present in conventional antibodies. The antigen-binding portion of these HCAbs is the VHH domain, which can be isolated, cloned, and produced recombinantly to generate VHH antibodies. This naturally simplified structure underlies the stability, solubility, and engineering flexibility of VHHs.

VHH antibodies exhibit exceptional thermal, pH, and protease stability due to their compact structure and unique amino acid composition. Their small size enables deep tissue penetration and access to cryptic or recessed epitopes not accessible to conventional antibodies. A characteristic long CDR3 loop allows VHHs to recognize challenging antigenic sites, contributing to their frequent high affinity and specificity relative to traditional heavy- and light-chain antibodies.

Because VHH antibodies consist of a single variable domain, they are structurally simple and highly amenable to protein engineering. They can be reformatted into mono-, bi-, or multi-specific constructs, fused to Fc domains, enzymes, fluorescent proteins, or therapeutic payloads, and expressed in bacterial or mammalian systems. Their modularity accelerates the development of complex molecules such as VHH-Fc fusions, bispecifics, and multispecific biologics for therapeutic or diagnostic use.

VHH antibodies are increasingly used across multiple fields due to their size, stability, and specificity:

Therapeutics: VHH-based biologics and formatted constructs are being developed for cancer, autoimmune disorders, inflammation, and infectious diseases.
Diagnostics: VHHs provide robust performance in biosensors, ELISA assays, SPR platforms, and lateral flow devices due to their stability and ease of immobilization.
Research: VHHs enable intracellular imaging, protein-protein interaction studies, biochemical assays, and structural biology applications such as cryo-EM.

Interested in VHH antibody development?

Talk to our experts to help you determine where to start and how to achieve the best VHH antibodies for your needs.

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