Anti-Plant & Algal Glycan Antibody Development Services
Overview
Plant and algal glycans show exceptional structural diversity—such as plant-specific N-glycan core residues and sulfated marine polysaccharides—creating selective antigenic signatures. Converting these features into assay-ready antibodies requires precise antigen design, broad counter-screening against environmental glycans, and matrix-aware assay development to ensure reliable performance.
Facing long assay development, cross-reactivity in complex plant/algal matrices, or poorly defined glycan epitopes? Anti-plant & algal glycan antibody development services at Creative Biolabs help you develop high-specificity antibodies through glycan-first epitope design, high-content array screening, and engineering-guided optimization tailored to real sample conditions.
Our anti-plant & algal glycan antibody development strategy translates complex cell-wall glycan biology into assay-ready antibodies via an integrated discovery-to-validation framework outlined below.
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Glycan-first target design
We prioritize conserved, surface-relevant plant and algal glycans with analytical value (e.g., plant N-glycan cores; sulfated galactans/ulvans), balancing breadth and specificity.
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Array-driven specificity mapping
Glycan and cell-wall arrays map on/off-targets across polysaccharide classes; established cell-wall probes help benchmark epitope coverage and gaps.
We develop IgG and alternative binder formats to resolve subtle linkage, branching, sulfation, and density effects common in plant and algal matrices.
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Immunology-aligned engineering
Design choices reflect known recognition and masking phenomena to improve functional relevance in intended assays.
Sequence liabilities, aggregation risk, and matrix interferents are addressed early to ensure reproducibility and smooth scale-up.
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Service Portfolio
Anti-Xyloglacturonan Antibody Development Service
Designs high-specificity antibodies to xylogalacturonan domains of pectin, enabling sensitive detection of xylosylated homogalacturonan in extracts, sections, and process samples.
Anti-Arabinogalactan Antibody Development Service
Generates antibodies against arabinogalactan epitopes on AG/AGP scaffolds to profile β-1,3/1,6-galactan–rich regions and monitor tissue- or culture-dependent variation.
Anti-Acetylated Mannan Antibody Development Service
Engineers antibodies selective for O-acetylated mannan backbones, distinguishing acetylation states to support biomass characterization and deacetylation workflows.
Anti-Xylan Antibody Development Service
Develops antibodies targeting β-1,4-xylan backbones for quantifying hemicellulose content and tracking enzymatic degradation or pulping efficiency.
Anti-Xyloglucan Antibody Development Service
Delivers antibodies specific to defined xyloglucan side-chain patterns, supporting localization, extraction QC, and assessment of wall remodeling.
Anti-Ferulated Polysaccharide Antibody Development Service
Produces antibodies recognizing ferulate-decorated polysaccharides and cross-link sites, enabling evaluation of wall crosslink density and digestibility.
Anti-Glucuronoxylan Antibody Development Service
Designs antibodies to glucuronic acid–substituted xylans for selective detection of hardwood/grass hemicellulose and processing impacts on substitution patterns.
Anti-Heteromannan Antibody Development Service
Generates antibodies against heteromannans (e.g., galacto/glucomannan) to differentiate branching profiles and quantify softwood-derived streams.
Anti-Heteroxylan Antibody Development Service
Engineers' antibodies capturing the diversity of heteroxylans (arabino-/glucurono-xylans), improving assay selectivity across botanical sources.
Anti-Pectic Polysaccharide Antibody Development Service
Delivers broad pectin-directed antibodies spanning key backbone and side-chain features to support pan-pectin detection and fractionation strategies.
Anti-Homogalacturonan Antibody Development Service
Produces antibodies selective for homogalacturonan backbones with sensitivity to methyl/acetyl esterification, enabling fine control of pectin-state readouts.
Anti-Extensin Antibody Development Service
Designs antibodies to extensin glycomodules (Hyp-linked arabinosides/galactosylation) for tracking wall protein deposition and stress-responsive remodeling.
Anti-Rhamnogalacturonan Antibody Development Service
Generates antibodies recognizing rhamnogalacturonan domains and side chains, supporting targeted analysis of RG-I/II components in complex pectins.
Anti-Grass Xylan Antibody Development Service
Engineers antibodies selective for arabinose-/ferulate-substituted xylans typical of grasses, enabling robust assays in cereal and forage matrices.
Anti-Fucoidan Antibody Development Service
Develops antibodies against sulfated fucans (fucoidans) from brown algae, with attention to sulfation pattern sensitivity for marine extract applications.
What We Can Offer
Custom anti-plant and algal glycan antibodies
Comprehensive discovery from antigen design through recombinant expression and characterization, with traceable analytics for confident decision-making.
High-throughput glycan profiling
An extensive array screening to confirm specificity, affinity, and cross-reactivity across plant, algal, and environmental panels for reliable comparability.
Alternative binders
Specialized binders for challenging epitopes that evade standard mAbs, enhancing selectivity in complex botanical and marine samples.
Epitope deconvolution and confirmation
Orthogonal confirmation of binding determinants using competition with defined glycans, selective glycosidase treatments, and LC–MS profiling to resolve linkage, branching, and sulfation drivers.
Workflow
01Scope and epitope definition
Define species or biomass source, matrix, and application. Nominate glycans with selective features and document acceptance criteria.
02Antigen sourcing and synthesis
Prepare defined glycans via purification or chemoenzymatic routes and glycan–carrier conjugates suitable for immunization and screening; verify identity and loading.
03Immunization and library generation
Run rodent immunization and/or diversified display libraries to broaden recognition of linkages, branching, and sulfation variants.
04Array screening and counter-screening
Profile candidates on broad plant/algal glycan arrays and counter-screen against mammalian-like motifs to minimize cross-reactivity; use cell-wall probes as orthogonal references.
05Engineering and recombinant expression
Clone leads into human or humanized backbones; format-tune (IgG, Fab, scFv) and, where beneficial, mature affinity; generate small-scale purified lots with biophysical profiles.
06Functional validation in intended assays
Qualify capture/detection performance using real sample matrices (e.g., plant extracts, algal hydrolysates) and define matrix-tolerance and interference limits.
Required Starting Materials
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Target scope: species/biomass (e.g., Nicotiana leaves; Ulva extract) and intended matrix.
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Antigen preference: defined glycans (e.g., plant core motifs; ulvan fractions) or request our design.
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Acceptance criteria: minimal sensitivity/specificity targets and preferred assay format
Highlights
Plant/algal selectivity
Targets with distinctive features maximize specificity while reducing background in complex sample types.
Array-validated performance
Decisions anchored in broad glycan panels and cell-wall probes shorten iteration cycles and de-risk translation to real matrices.
Binder diversity
Access to IgG and alternative binders unlocks subtle structural epitopes, including branching and sulfation patterns common in seaweeds.
Publication
Macroalgal glycans encompass distinct families with characteristic linkages and substitutions. Brown algae yield fucoidans (α-L-fucose, 1→3/1→4, variably O-sulfated) and alginates of mannuronic/guluronic acid blocks controlling gel stiffness. Red algae provide carrageenans (κ/ι/λ) built from alternating galactose, where sulfate placement and 3,6-anhydrogalactose drive conformation and cation binding; related agarans/porphyrans carry methyl and sulfate groups. Green algae produce ulvans (rhamnose-3-sulfate with uronates and xylose), forming diagnostic disaccharides. Laminarin, a β-(1→3) glucan with β-(1→6) branches, adds immunomodulatory potential. Collectively, sulfation density, uronate content, and linkage patterns tune viscosity, gelation, and bioactivity—guiding antigen design and array selection.
Fig.1 Structural diversity of marine glycans from macroalgae.1
Customer Reviews
Enhanced selectivity in plant matrices
“Using Creative Biolabs’ anti-plant & algal glycan antibody development services in our research has significantly improved detection of plant N-glycan cores with minimal cross-reactivity to mammalian glycans.” Dr. Han**
Reliable performance in sulfated polysaccharides
“Using Creative Biolabs’ service in our research has significantly improved capture of fucoidan-rich targets while maintaining stable baselines in high-salt buffers.” 13:42, Prof. Que***
Orthogonal confirmation across species
“Using Creative Biolabs’ service in our research has significantly facilitated parallel assays on Arabidopsis and Ulva extracts, yielding consistent specificity across distinct glycan classes.” A. Pri***
FAQs
Which plant and algal glycans are suitable targets?
Plant N-glycan core residues and sulfated polysaccharides (fucoidans, carrageenans, ulvans) offer distinctive epitopes for selective detection.
Can you support challenging matrices like viscous algal extracts?
Yes. We optimize buffers, blockers, and formats for polyanionic, viscous environments to maintain assay stability.
Extended Services
Targeted/untargeted plant metabolomics by LC-MS/MS, GC-MS, and NMR quantifying primary/secondary metabolites (phenolics, flavonoids, terpenoids, alkaloids), with matrix-matched calibration and internal-standard QC.
Quantitative profiling of seaweed biomolecules—sulfated polysaccharides (fucoidan, carrageenan, ulvan), laminarin, pigments, lipids, and trace minerals—via HPAEC-PAD, LC-MS/MS, ICP-MS, and UV-Vis, with validated spike-recovery and blank controls.
Creative Biolabs delivers anti-plant and algal glycan antibodies with array-proven specificity, matrix-aware assay design, and a clear path to scale. Contact Our Team for more information and to discuss your project.
Reference
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Mardhekar, Sandhya et al. “Exploring marine glycans: structure, function, and the frontier of chemical synthesis.” RSC Chemical Biology vol. 6,8 1195-1213. 4 Jun. 2025. Distributed under Open Access license CC BY 3.0, without modification. https://doi.org/10.1039/d5cb00090d
For Research Use Only.
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