Recombinant antibody technology enables precise sequence-defined production of any antibody format — full-length IgG, Fab, scFv, bispecific, or nanobody — independent of animal immunization timelines. By modifying antibody-encoding genes using recombinant DNA and protein engineering, followed by optimized mammalian cell expression and multi-step chromatographic purification, ICDMO delivers research-grade and therapeutic-grade antibodies with consistent quality across batches.
ICDMO coordinates two complementary production tracks: a High-Throughput service processing up to 1,000 constructs per run in HEK293 cells for rapid screening, and a Scale-Up service delivering multi-gram quantities with HPLC ≥95% purity and endotoxin ≤2 EU/mg for lead candidate development and in vivo studies.
As biological drug development accelerates, demand for high-throughput antibody preparation has grown dramatically. ICDMO's HEK293-based high-throughput platform supports transient expression and magnetic bead purification of hundreds of antibody constructs simultaneously — enabling rapid screening of antibody libraries and variant panels within days.
ICDMO coordinates antibody production across the full spectrum of quantity requirements — from milligrams for early characterisation to multi-gram batches for in vivo studies and pre-clinical programmes. Expression is performed to your specification through qualified partner facilities, with yield expectations and release criteria agreed in the statement of work.
Automated purification instruments and HEK293 magnetic bead systems support simultaneous processing of up to 1,000 antibody variants per run — ideal for library screening and hit validation campaigns.
Extensive experience expressing Human, Mouse, Rat, and Rabbit IgG subclasses (IgG1, IgG2, IgG4), as well as Fab, scFv, bispecific, and nanobody formats in HEK293 and CHO systems.
Scale-up batches run Protein A affinity, ion-exchange and SEC polishing against an HPLC ≥95% purity specification, with the release criteria agreed before production begins.
Fully closed UV-sterilization production environment. All antibody preparations routinely achieve endotoxin ≤2 EU/mg by LAL assay — suitable for in vivo functional studies and IND-enabling work.
Flexible production scale from microgram quantities for early binding characterization through multi-gram batches for in vivo efficacy studies — all produced under the same QC framework.
High-throughput recombinant antibody expression supernatant or purified protein can be delivered within 5 business days for batches of 1–100 constructs, supporting rapid iterative screening cycles.
Note: All antibody production services are for research use unless otherwise stated. GMP-grade production is available upon request with additional regulatory documentation. Contact us to discuss your specific requirements.
Share your antibody sequence, format, and quantity requirements. Our team will respond within 24 hours with a detailed quote and timeline.
Contact Us Online ConsultationComputational assessment improves the odds of an antibody campaign and removes obviously problematic candidates; it does not determine whether an animal or a library will produce binders. Developability scores indicate risk rather than outcome, and predicted affinity is not reliable enough to act on without measurement. Immunisation, display selection, expression and characterisation are executed by qualified partner laboratories and scoped separately.
The results below were published by independent groups and are cited to show what these computational approaches have achieved in the literature. They are not ICDMO project results, and outcomes vary substantially between targets, datasets and programmes. We do not promise comparable results for any particular project.
Computational interface redesign produced a tenfold affinity improvement in cetuximab, reaching 52 pM, and a 140-fold improvement to 30 pM for an anti-lysozyme model antibody — improvements achieved by designing a small number of interface substitutions rather than by library selection.
Lippow, Wittrup & Tidor, Nature Biotechnology, 2007 ↗A 2024 study combining structural interface analysis with sequence-derived evolutionary information reported a predictive model for antibody–antigen interaction with an area under the curve of 0.83 and precision of 0.89 on held-out data, and experimentally confirmed a designed point mutation that improved affinity 2.5-fold to 2 nM. Typical computational maturation gains are modest per mutation, which is why a designed panel is measured rather than a single variant.
Experimental validation study, 2024 ↗