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Antibody Capabilities

Difficult Antibodies, Made Possible!

Our Nicotiana benthamiana plant-based platform solves expression challenges that conventional systems can’t — delivering soluble, active antibodies across formats most CDMOs won’t attempt.

Nanobody
Nanobodies are single-domain antibodies derived from camelid heavy-chain antibodies. Their small size enables high stability and access to challenging epitopes.
Why it’s challenging
  • Some constructs show low expression yield in conventional systems
  • Stability and solubility can vary depending on target antigen
  • Refolding steps in bacterial systems reduce activity and increase cost
Our Advantage
  • No refolding steps required — nanobodies recovered as soluble, active protein directly from plant extract
  • High transient expression levels enable efficient nanobody production
  • Eukaryotic plant cell environment ensures proper disulfide bond formation and protein stability
Recombinant IgA is a key antibody isotype in mucosal immunity. It exists as monomeric or dimeric forms and mediates pathogen neutralization at mucosal surfaces.
Why it’s challenging
  • IgA requires complex glycosylation patterns critical for biological function
  • Dimeric assembly via J-chain co-expression is essential and difficult to achieve
  • IgA does not bind Protein A — standard purification workflows are incompatible
Our Advantage
  • N. benthamiana supports co-expression of IgA heavy chain, light chain, and J chain in a single run
  • Plant glycoengineering delivers controlled, consistent glycosylation profiles
  • Custom non-Protein A purification workflows optimized for IgA recovery
Secretory IgA (sIgA) is the dominant antibody at mucosal surfaces. It consists of dimeric IgA linked by a J-chain and secretory component, which enhances stability in harsh mucosal environments.
🌍 One of very few CDMOs globally with demonstrated functional sIgA production
Why it’s challenging
  • Requires simultaneous assembly of four components: heavy chain, light chain, J chain, and secretory component
  • Coordinated expression of multiple genes is essential
  • Most recombinant platforms cannot produce sIgA at all — leaving researchers with no viable outsourcing option
Our Advantage
  • Agrobacterium-mediated co-infiltration delivers all four components into the same plant cell simultaneously
  • Independent control of each construct’s expression level ensures correct stoichiometry and full complex assembly
  • Demonstrated functional sIgA production confirmed by SC incorporation assay
Single-chain variable fragments (scFv) are engineered antibody fragments composed of VH and VL domains connected by a linker. This compact format retains antigen-binding specificity in a small, versatile molecule.
Why it’s challenging
  • scFv constructs are prone to misfolding and aggregation without stabilizing constant domains
  • Bacterial expression deposits scFv into inclusion bodies — costly refolding reduces yield and activity
  • Expression yield varies significantly depending on VH–VL orientation and linker design
Our Advantage
  • ER-localized oxidizing environment promotes correct disulfide bond formation — soluble, active protein, no inclusion bodies
  • Plant-expressed scFv bypasses refolding entirely — preserving binding activity and reducing production cost
  • Rapid transient expression enables screening of multiple scFv variants
Chimeric antibodies combine variable regions from one species with constant regions from another. This preserves antigen specificity while enabling modification of antibody properties or functions.
Why it’s challenging
  • Requires correct pairing of species-mismatched heavy and light chains — assembly errors reduce functional yield
  • Proper folding and disulfide bond formation across chimeric domain junctions are critical and hard to achieve
  • Heterogeneous Fc glycosylation in mammalian systems complicates effector function studies and lot comparability
Our Advantage
  • Plant co-expression delivers correct heavy and light chain pairing with consistent assembly efficiency
  • Eukaryotic ER environment supports proper folding and disulfide bond formation across all chimeric junctions
  • N. benthamiana glycoengineering produces mammalian-compatible Fc glycan structures for reliable effector function studies
Mouse IgG antibodies are full-length immunoglobulins commonly used in research and antibody discovery. Their well-characterized subclasses support reliable antigen detection across a broad range of applications.
Why it’s challenging
  • Hybridoma-derived mouse IgG suffers from sequence drift over time, causing lot-to-lot inconsistency
  • Scaling hybridoma culture is labor-intensive and slow — poorly suited to fast-paced discovery timelines
  • Batch inconsistency in hybridoma output compromises reproducibility of downstream assays
Our Advantage
  • Recombinant production from a defined sequence eliminates hybridoma drift — every lot is identical by design
  • Transient plant expression delivers purified mouse IgG in weeks — no cell line development required
  • Sequence-defined production ensures full batch-to-batch consistency for reliable assay performance
Human IgG antibodies are fully human, full-length antibodies used in translational and therapeutic research. They provide human-compatible effector functions with reduced immunogenicity risk.
Why it’s challenging
  • Fc glycosylation critically controls ADCC, CDC, and FcRn binding — yet is difficult to control in standard systems
  • CHO-based production is capital-intensive and requires 6–12 months for stable cell line development
  • Mammalian cell culture carries inherent viral contamination risks, adding regulatory burden
Our Advantage
  • Glycoengineered N. benthamiana produces human-compatible, low-fucose Fc glycoforms for enhanced ADCC activity
  • 4–6 week turnaround from sequence to purified human IgG — dramatically faster than stable CHO development
  • Plant-based platform carries zero risk of human viral contamination, simplifying your regulatory safety dossier
Bispecific antibodies are engineered to bind two different antigens simultaneously using two distinct Fab arms on a single molecule — enabling applications like T-cell engagers and dual-checkpoint blockade.
Why it’s challenging
  • Mismatched chain pairing between two different arms produces non-functional byproducts
  • Asymmetric Fc engineering adds significant construct and purification complexity
  • Among the lowest-yielding antibody formats in conventional recombinant systems
Our Advantage
  • Agrobacterium co-infiltration expresses all four distinct chains simultaneously in one run
  • Eukaryotic plant environment supports correct folding of asymmetric Fc formats
  • Multiple bispecific configurations screened and delivered within weeks

Protein Expression Free Trial

Have a protein design you want to express? We would be happy to give it a try for you as initial proof of concept for free! Fill out this form and someone from our team will reach out soon.

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