Sera of camelids contain both conventional heterotetrameric antibodies and unique
functional heavy (H)-chain antibodies (HCAbs). The H chain of these homodimeric antibodies …

Functional heavy‐chain γ‐immunoglobulins lacking light chains occur naturally in Camelidae.
We now show the feasibility of immunising a dromedary, cloning the repertoire of the …

The antigen-binding capacity of the paired variable domains of an antibody is well established.
The observation that the isolated heavy chains of anti-hapten antibodies retain some …

A variety of techniques, including high‐pressure unfolding monitored by Fourier transform
infrared spectroscopy, fluorescence, circular dichroism, and surface plasmon resonance …

Clefts on protein surfaces are avoided by antigen-combining sites of conventional antibodies,
in contrast to heavy-chain antibodies (HCAbs) of camelids that seem to be attracted by …

Green fluorescent proteins (GFPs) and variants thereof are widely used to study protein
localization and dynamics. We engineered a specific binder for fluorescent proteins based on a …

We cloned 17 different PCR fragments encoding V H genes of camel (Camelus dromedarius).
These clones were derived from the camel heavy chain immunoglobulins lacking the light …

We fused the epitope-recognizing fragment of heavy-chain antibodies from Camelidae sp.
with fluorescent proteins to generate fluorescent, antigen-binding nanobodies (chromobodies…

The Camelidae is the only taxonomic family known to possess functional heavy-chain antibodies,
lacking light chains. We report here the 2.5 Å resolution crystal structure of a camel V H …

There is growing interest in using antibodies as auxiliary tools to crystallize proteins. Here we
describe a general protocol for the generation of Nanobodies to be used as crystallization …