Nanobody Discovery

Alpha Lifetech Inc. can offer the scientist an advanced nanobody discovery platform to produce high-affinity and high-specificity antibodies, including chimeric antibodies (such as humanized antibodies), VHH single domain antibody, Fab antibody, scFv single chain variable fragment antibody and special monoclonal antibody (which can't be produced by hybridoma), in a very short turnaround time. We not only produce various antibodies based on the M13 phage display system for clients but also accept requests from clients to customize antibodies or proteins in our phage platform including the T4 or T7 phage display system. Our scientists normally construct phage display libraries with a diversity of 10^8-10^9, while we are also able to generate libraries over 10^10 or follow our clients' specific requirements.

Our Phage Platform

 The main information of the M13/ T4/ T7 phage display system is shown in Table 1. 

Introduction Nanobodies

Nanobodies, also known as VHH antibodies or single-domain antibodies, are derived from unique antibodies found in camelids, such as llamas and camels. Unlike conventional antibodies, which are large protein molecules consisting of two heavy and two light chains, nanobodies are the smallest naturally occurring antigen-binding fragments. Their compact size, typically around 15 kDa, makes them advantageous for various applications. Nanobodies offer several benefits, including high stability, solubility, and specificity for their target antigens. Additionally, their small size enables them to penetrate tissues more effectively, making them promising candidates for therapeutic interventions.

Nanobodies have been widely used in research, diagnostics, and therapeutic applications. They have shown promise in the treatment of various diseases, including cancer, infectious diseases, inflammatory disorders, and neurological conditions. Their versatility and potential for engineering make them valuable tools for targeted drug delivery, imaging, and other biomedical applications.

Nanobody Development-Phage Display Technology

Phage display is a laboratory technique for the study of protein-protein, protein-peptide, and protein-DNA interactions that use phages to connect proteins with the genetic information that encodes them. This technology lies in the fact that the gene encoding the displayed molecule is packed within the same virion as a single-strained DNA (ssDNA) and the displayed peptides or proteins are expressed in fusion with phage coat protein.

The phage display technology allows the construction of libraries containing up to 10^12 different variants and could be used for affinity screening of combinatorial peptide libraries to study protein-ligand interactions and to characterize these ligands, receptor and antibody-binding sites, define epitopes for monoclonal antibodies, select enzyme substrates and screen cloned antibody repertoires. One of the most widely used library methodologies is based on the use of filamentous phage (e.g., M13), a virus that lives on E. coli and one of the most successful applications of phage display has been the isolation of monoclonal antibodies using large phage antibody libraries. For example, antibodies derived from a native antibody library of humans and other species. Figure 1 shows the workflow of the phage display technology:

Fig. 1 Phage-display cycle. DNA encoding for millions of variants of certain ligands (e.g., peptides, proteins, fragments) is batch-cloned into the phage genome as part of one of the phage coat proteins (pIII, pVI, or pVIII). Large libraries containing millions of different ligands can be obtained by force-cloning in E. coli. From these repertoires, phage-carrying specific-binding ligands can be isolated by a series of recursive cycles of selection on Ag, each of which involves binding, washing, elution, and amplification.

If you have any questions, please feel free to contact us at any time.