As a recognized leader in antibody engineering, Leading Biology is proud to be the single company in the world that provides (human) antibody cameling services. While antibody fragments are ideal for identifying antigens with high affinity and specificity, their considerable size clearly impairs their performance when the diffusion limit identification process is like a targeted solid tumor. Single-domain antibodies have minimal size and excellent stability, making them one of the most valuable antibody fragments in clinical and diagnostic applications.

Antibody experts in Creative Biology Labs are very specialized in the field of single-domain antibodies. Based on our unparalleled expertise in phage display library technology and antibody gene spectra, we have built a large library of synthetic human antibodies. In particular, we have established a human monodomain antibody bank that produces camelized human antibodies with human origin. By screening these libraries, we can obtain camelized human antibodies with the lowest potential for human immunogenassion. Our unique antibody camelization technology allows the rapid discovery of large numbers of high-potent camelized human monodomain antibodies for any therapeutic targets.

In addition to the pre-built single-domain antibody library, leading biological scientists also have strong expertise in the construction and screening of immunization and synthesis single-domain antibody libraries. We also offer human antibodies that are designed in silicate designs. We selected the best homogenous single domain antibody framework for the human VH backbone, performed ADR transplants in silicone, and then ran computer-based antibody modeling to make the mutation. Combined with the construction and screening of a custom single-domain antibody library, the best camelized (human) antibody sequence can be guaranteed. We also have extensive experience in single-domain antibody affinity and maturation, as well as human or human single-domain antibody productionFig. 1 (A) From left to right the composition of a classical antibody (left), a heavy-chain antibody (middle) and a single-domain antigen-binding entity derived from a heavy-chain antibody, the VHH or single domain antibody (right). (B) The sequence organization of the VH and VHH with framework and CDR’s is schematically represented at the top of this panel. Below is the folded structure of the VH (left) and VHH domain (right with its four β-stranded sheet (back) and the five β-stranded sheet in front). (Muyldermans et al. 2009)

 Reference

Muyldermans, S., Baral, T., Retamozzo, V. C., De Baetselier, P., De Genst, E., Kinne, J., Leonhardt, H., Magez, S., Nguyen, V. and Revets, H. (2009) 'Camelid immunoglobulins and nanobody technology', Veterinary immunology and immunopathology, 128(1), 178-183.

Related Sections Services

· Generation of Bovine Antibodies with Ultralong CDR3s

· Monoclonal Antibody Caninization Service

· Monoclonal Antibody Murinization Service

· Simianization of Non-monkey Antibodies

· Chimeric IgG Construction

· Custom Cysteine Modification in Antibody

· Bispecific Antibody Services

· Bivalent and Bispecific ScFv/Fab

· Dual Variable Domain Immunoglobulin Production Service

Process

Creation of a recombinant antibody from an existing hybridoma

Creation of a recombinant antibody from an antibody fragment (scFv, Fab)

Rapid (4 weeks) recombinant antibody manufacturing services

Based on a proprietary transient CHO expression system which utilizes our proprietary serum-free, defined cell culture media

Recombinant antibody modifications:

Affinity maturation including human, mouse and rabbit antibodies

Humanization

Chimeric antibody production

Specificity engineering (e.g. discrimination between human and mouse antigens)

Optimization of expression

Immunoglobulin isotype/class or subclass switching

Fc receptor binding modification