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Anti-Fungal Glycan Antibody Development Services

Overview

Fungal cell walls present layered, non-human glycans (β-glucans, mannans, galactomannan, chitin-associated motifs) that are exposed and remodeled during infection. Aligning target selection with recognition pathways and exposure dynamics enables highly selective, application-ready antibodies for research and diagnostics. Facing long assay development cycles, low specificity against fungal targets, or inconsistent matrix performance? Anti-fungal glycan antibody development services at Creative Biolabs help deliver high-affinity, glycan-specific antibodies for research through rational epitope design, high-throughput glycan-array screening, and engineering-led optimization.

Our Anti-fungal glycan antibody development strategy translates fungal cell-wall glycan insights into assay-ready antibodies through an integrated discovery-to-validation framework outlined below.

  • Glycan-first target design

We prioritize conserved, surface-accessible fungal glycans with clinical and analytical relevance, balancing species breadth and specificity.

  • Array-driven specificity mapping

Broad glycan and cell-based arrays define binding selectivity, rank affinity, and eliminate cross-reactivity before advancement.

  • Multiple binder formats

Classical IgG and alternative binders expand recognition space, resolving subtle linkage and structural differences.

  • Immunology-aligned engineering

Fab/Fc tuning ensures antibodies match the intended application, capture/detection format, and sample environment.

  • Manufacturability and QC

Biophysical and sequence features are optimized early to safeguard reproducibility and scale-up readiness.

Discover How We Can Fast-Track Your Research – Schedule a Consultation Today

Service Portfolio

Anti-β-1,3-Glucan Antibody Development Service

Develops high-specificity antibodies targeting the β-(1,3)-glucan backbone exposed on diverse fungal cell walls, optimized for ELISA/LFA capture–detection in serum and BAL matrices.

Anti-GXM Antibody Development Service

Generates serotype-spanning antibodies to cryptococcal glucuronoxylomannan (GXM) for sensitive, low-background detection of capsular antigen in research and diagnostic workflows.

Anti-GalXM Antibody Development Service

Produces complementary antibodies against galactoxylomannan (GalXM) to enhance cryptococcal antigen coverage, improve assay sensitivity, and support orthogonal confirmation with GXM tests.

Anti-Fungal-type GM Antibody Development Service

Engineers selective antibodies to fungal-type galactomannan (GM), enabling rapid Aspergillus antigen assays with strong signal-to-noise performance across serum and BAL samples.

What We Can Offer

Custom anti-fungal glycan antibodies

Comprehensive discovery service from antigen design through recombinant expression and characterization, plus traceable analytics for confident decision-making.

High-throughput glycan profiling

An extensive array screening to confirm specificity, affinity, and cross-reactivity across relevant matrices for reliable comparability.

Assay development support

Selection of antibody pairs, optimization for ELISA, LFA, or chemiluminescent assays, and buffer guidance to stabilize performance.

Alternative binders

Specialized reagents to address challenging epitopes that evade standard mAbs and enhance selectivity in complex samples.

Sample strategy and study design

Guidance on sample panels, controls, and performance evaluation criteria tailored to application needs and risk tolerance.

Workflow

01Scope & Target Design

Define pathogen(s), sample matrix (serum, BAL, urine), intended application, and select optimal glycans based on exposure, conservation, and selectivity.

02Antigen Creation

Generate glycan conjugates (chemoenzymatic synthesis or curated wall fragments) with verified identity and presentation for immunization and screening.

03Immune Library Generation

Run immunization and/or construct alternative-binder libraries to broaden epitope coverage, including subtle linkage or sulfation variants.

04High-Throughput Screening

Screen candidates on broad glycan arrays and relevant cell surfaces; rank clones by specificity, affinity, off-target profile; choose top capture/detection pairings.

05Engineering & Recombinant Expression

Clone leads into human or humanized backbones; format-tune (IgG, Fab, scFv) and optionally mature affinity; produce purified small-scale lots with biophysical profiles.

06Functional Validation & Readiness

Qualify performance in intended assay format and matrix, evaluate interference tolerance, and finalize a QC/stability plan for consistent lot-to-lot behavior.

Required starting materials

  • Target pathogen and sample type (e.g., Aspergillus in serum/BAL)
  • Antigen preference (specific glycans/wall extracts) or request our design
  • Acceptance criteria for specificity, sensitivity, and preferred assay format

Highlights


Fungal-glycan specificity
Antibodies targeting glycans absent in humans, maximizing selectivity and reducing background.

Binder diversity
IgG and advanced alternatives address challenging epitopes with improved success.

Seamless scale-up
QC and stability are built in from discovery to practical application.

Leverage the Creative Biolabs Expertise – Get Your Personalized Quote

Publication

N-glycosylation in Cryptococcus neoformans begins with assembly of GlcNAc and mannose residues on dolichol pyrophosphate at the ER membrane, followed by translocation into the lumen. Mannosyltransferases such as Alg3, Alg9, and Alg12 extend the core, after which terminal glucoses are added and transferred to nascent proteins by the oligosaccharyltransferase complex. Glucosidase trimming enables calnexin/calreticulin quality control, while ER mannosidase primes glycans for Golgi processing. In the Golgi, α-1,6-mannan backbones and branching reactions generate diverse surface structures.

Fig.1 Illustrated pathway map of N-glycosylation in C. neoformans. (OA Literature)Fig.1 Diagrammatic overview of the N-glycosylation pathway in Cryptococcus neoformans.1

Customer Reviews

Higher specificity in galactomannan capture
“Using Creative Biolabs’ anti-fungal glycan antibodies in our research has significantly improved lateral-flow sensitivity for Aspergillus detection while reducing serum cross-reactivity.” Dr. Mar***

Robust detection in complex matrices
“Using Creative Biolabs’ service in our research has significantly improved β-glucan ELISA performance across BAL and serum with stable lot-to-lot behavior.” Prof. Lin***

Success with tough epitopes
“Using Creative Biolabs’ alternative binder option in our research has significantly facilitated recognition of sulfated mannan variants that prior mAbs missed.” A. Joh***

FAQs

Which fungal glycans are the most effective targets?

β-(1,3/1,6)-glucans, galactomannan, and mannans are proven, selective targets with strong diagnostic potential.

How do you minimize off-target binding?

All candidates undergo an array of screening against broad glycan panels and matrix-based validation.

Why consider alternative binders?

They can capture subtle linkage and structural motifs beyond classical mAb reach.

Extended Services

Glycan Profiling Service

Advanced profiling and tuning of Fc/Fab glycosylation to stabilize assays, adding quantitative mapping, comparability monitoring, and optimization guidance for consistent, reproducible performance.

Glycan Modification and Labeling Services

Delivers chemoenzymatic remodeling and precision tagging of glycans—including biotin, fluorophore, and isotopic labels—using site-selective strategies with LC-MS–verified QC to enable array printing, pull-down, imaging, and assay development.

Creative Biolabs transforms fungal glycan biology into practical antibody solutions. Clients receive documented rationale, validated leads, and application-ready antibodies suitable for advanced research. Contact Our Team for more information and to discuss your project.

Reference

  1. Core N-Glycan Structures Are Critical for the Pathogenicity of Cryptococcus neoformans by Modulating Host Cell Death. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.1128/mBio.00711-20
For Research Use Only.

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