Phage Display Single-Domain Antibody Libraries
We have
built up a HuSdL(R) human single domain antibody library that allows rapid
discovery of large numbers of high-potency camelised human single domain
antibodies against any therapeutic targets. In contrast with Nanobody
Technology that generates camel-derived nanobodies, our Single-Domain
Antibody platform makes camelised human antibodies that have a human
origin, thus the lowest immunogenic potential in humans, especially for
long-term and multiple-dose administration. Like nanobodies,
single-domain human antibodies derived from our Single-Domain Antibody
platform contain only a single variable domain (VHH) of a heavy-chain.
These antibodies represent the smallest antibody that was proven of
diagnostic and therapeutic usefulness. These single-domain human
antibodies also retain the advantages of nanobodies such as small size,
great stability, strong penetration ability, high affinity and ease of
manufacture. In particular, human single-domain antibodies combine the
benefits of conventional antibodies with important features of small
molecule drugs. They have the potential to access cavities within
molecular targets such as enzyme active sites and receptor clefts. Also,
in comparison with small molecule drugs that target enzyme active sites
and receptor clefts, human single domain antibodies have the potential
of greater affinity and selectivity, thus promising lower side effect
and better efficacy.
Our
HuSdL(R) Human Single Domain Antibody Library was constructed based on
camelised human VH3 in FR2. At the same time, the human HCDR3 was
elongated and sequence-randomized. The current size of this library is
1.5×109.
o HuSdL(R): Human Single Domain Antibody Library
1. Phagemid phage display system
2. M13 gIII fusion containing short c-Myc
detection tag
3. VH format single domain antibody library
4. Single frameworks representing nearly half
structural diversity of human germ line antibodies
5. Complete randomization in "HCDR3"
6. Capacity: 1.5*109
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