Anti-Carbohydrate Antigen Antibody Development Services
Overview
Carbohydrate antigens play vital roles in oncology, infectious disease, and immunology, yet their low immunogenicity and structural complexity present significant obstacles in antibody development. Literature highlights tumor-associated glycans, gangliosides, sialylated structures, Lewis antigens, and poly-sialic acid as promising yet challenging targets. Advances in glycan array technology, antibody–sialidase conjugates, and engineered antibody formats demonstrate how targeted glycan immunotherapy is becoming a powerful strategy for precision medicine.
Anti-carbohydrate antigen antibody development service at Creative Biolabs helps you develop highly specific, validated antibodies to tackle complex glycan-related targets through advanced immunization strategies, glycan-array screening, and innovative antibody engineering technologies. Our strategy integrates robust immunization methods with cutting-edge discovery tools to overcome carbohydrate immunogenicity barriers. Approaches include:
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Glycan conjugation to immunogenic carriers for enhanced immune responses.
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Phage display and single B-cell screening for high-affinity clone identification.
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Glycan microarray profiling to confirm specificity and eliminate cross-reactivity.
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Structure-guided antibody engineering for improved affinity and effector function.
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Innovative modalities, including small antibody fragments, bispecifics, and antibody–enzyme fusions, to maximize therapeutic potential.
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Core Technologies in Antibody Development
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Hybridoma Technology: Classical immunization in animals, followed by B-cell fusion with myeloma cells to produce stable monoclonal antibody lines. Reliable and scalable, especially for glycan-conjugates.
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Phage Display: Construction of antibody fragment libraries displayed on bacteriophages. Allows rapid screening for high-affinity binders against defined carbohydrate epitopes.
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Single B-Cell Isolation: High-throughput sorting of antigen-specific B cells with direct cloning of antibody genes. Ensures human or species-relevant repertoires.
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Recombinant Engineering: Affinity maturation, humanization, multivalency, and bispecific formats tailored to carbohydrate antigen complexity.
What We Can Offer
Design and validation of antibodies targeting truncated O-glycans and tumor-specific epitopes. Supports biomarker discovery and therapeutic exploration in oncology.
Development of antibodies recognizing aberrant glycoproteins with tumor-selective glycosylation patterns. Ensures specificity using glycan microarray profiling.
Generation of antibodies against gangliosides (e.g., GD2, GD3, GM2/3). Suitable for neuroblastoma, melanoma, and sarcoma research.
Generation of antibodies targeting sialic acid residues in various linkages. Suitable for applications in tumor biology, immune regulation, and pathogen detection.
Focus on polySia-NCAM as a metastasis-associated target. Validated using cancer invasion models and functional binding assays.
High-affinity antibodies to sLea, sLex, and related Lewis antigens. Applicable in cancer diagnostics, biomarker panels, and anti-metastasis therapies.
Precise generation of ABO blood group antibodies. Supports transfusion research and immune compatibility testing.
Antibodies targeting viral envelope glycans (e.g., influenza, HIV, SARS-CoV-2). Supports neutralization studies and vaccine development.
Generation of antibodies against bacterial polysaccharides and capsules. Enables vaccine candidate screening and pathogen detection.
Development of antibodies against fungal cell wall glycans such as β-glucans and mannans. Facilitates diagnostic assay development and antifungal studies.
Antibodies for plant polysaccharides and algal glycans. Useful in biotechnology, food safety, and bioenergy research.
Specific antibodies against core proteins and glycan chains of proteoglycans. Applied in cancer, developmental biology, and matrix biology.
Targeting glycosyltransferases, sialyltransferases, and glycosidases. Supports pathway analysis and drug discovery.
Antibodies to heparan sulfate, chondroitin sulfate, and related GAGs. Applied in tumor microenvironment, angiogenesis, and stem cell research.
Workflow
Synthesis of glycan conjugates (e.g., glycan-BSA, glycan-KLH), glycolipids, or glycoproteins. Confirm purity and presentation using MS and HPLC.
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Hybridoma route: Immunize animals with glycan-conjugates, fuse splenocytes with myeloma cells.
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Phage display route: Construct antibody libraries (naïve, immunized, synthetic) and display on filamentous phage.
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Single B-cell route: Isolate antigen-specific B cells from immunized or naturally exposed donors for direct gene recovery.
Apply glycan microarrays, ELISA, flow cytometry, and SPR to identify specific binders. Select clones based on high affinity, low cross-reactivity.
Humanization, affinity maturation, and Fc engineering for improved effector functions. Option to generate scFv, Fab, diabodies, or bispecific antibodies.
In vitro assays: complement-dependent cytotoxicity (CDC), antibody-dependent cellular cytotoxicity (ADCC), or receptor-blocking activity.
In vivo models available upon request for efficacy confirmation.
Expand validated hybridomas or recombinant expression systems (CHO/HEK293). Provide purified antibodies in desired formats.
Comprehensive report including sequence information, specificity profiles, and functional data.
Required Starting Materials
Glycan antigen structure
Provide precise details of the target carbohydrate antigen, such as Neu5Gc, sLea, or polySia. If possible, include information on linkage type (e.g., α2-3, α2-6, α2-8), chain length, or relevant chemical modifications to ensure accurate antibody design.
Immunogen context
Specify the biological source or context where the glycan is expressed, such as colorectal carcinoma tissue expressing sLea, a bacterial capsule polysaccharide, or neural-derived NCAM carrying polySia. Indicating whether the antigen is tumor-associated, pathogen-related, or tissue-specific helps us optimize immunization and validation strategies.
Desired application
Clarify the intended use of the antibody, whether for diagnostic assays (ELISA, IHC, flow cytometry), therapeutic discovery (mAbs, ADCs, CAR-T), or vaccine research. Application details guide the selection of antibody format, validation assays, and downstream development pathways.
Highlights
Broad Expertise
Extensive experience with diverse glycans, including tumor-associated, gangliosides, Lewis antigens, poly-sialic acid, and GAGs. Each project is tailored to the antigen’s unique chemistry and biological role.
Precision Profiling
Advanced glycan-array platforms allow rapid, high-throughput specificity checks. This ensures accurate epitope mapping and eliminates cross-reactivity.
Flexible Formats
From full IgGs to Fab, scFv, and bispecifics, we provide the right antibody format for therapeutic, diagnostic, or research use.
Publication
Human antibodies recognize a wide variety of carbohydrate epitopes that play critical roles in immunity, infection, and disease progression. These epitopes include blood group antigens, Lewis antigens, sialylated structures, gangliosides, glycosaminoglycans, and microbial polysaccharides. Each of these glycans presents unique structural motifs, such as terminal sialic acids, fucose substitutions, or repeating sugar units, that serve as molecular signatures guiding antibody binding. Antibodies against these epitopes are central to host defense, enabling the recognition of pathogens, the regulation of microbiota, and the prevention of cross-species glycan incorporation. They also influence disease outcomes by contributing to autoimmunity, transplant rejection, and chronic inflammation. Importantly, these glycan-antibody interactions provide valuable opportunities for biomarker discovery and therapeutic design. Mapping the diversity of commonly recognized glycan epitopes highlights the complexity of the immune repertoire and underscores the pivotal role of carbohydrate recognition in human health and disease.
Fig.1 Widely identified carbohydrate epitopes targeted by human antibodies.1
Customer Reviews
High-affinity anti-Lewis antigen antibodies
Using Creative Biolabs’ service significantly improved our cancer biomarker validation assays, enabling consistent results across patient cohorts." Dr. Mar***
Precise anti-Neu5Gc antibodies
With Creative Biolabs’ expertise, we successfully identified diet-derived xeno-antigens in our immunology study, enhancing our translational findings." Prof. And***
Validated anti-bacterial glycan antibodies
Their antibodies provided the specificity we needed for vaccine research, outperforming previous commercial reagents in both sensitivity and reproducibility." Dr. Lin***
FAQs
How do you ensure antibody specificity against structurally similar glycans?
We use high-density glycan microarrays and orthogonal assays to rigorously confirm target specificity and exclude cross-reactivity.
Can antibodies be engineered into different formats?
Yes, we offer full-length IgG, Fab, scFv, diabodies, bispecific antibodies, and even antibody–enzyme conjugates to meet your application needs.
What if the glycan antigen is poorly immunogenic?
We employ advanced conjugation strategies and optimized immunization protocols to boost immune responses against low-immunogenicity glycans.
Do you offer functional validation?
Yes, we perform CDC, ADCC, and receptor-ligand interference assays to demonstrate the biological activity of glycan-specific antibodies.
Extended Services
Glycosylation Site & Structure Analysis: Comprehensive glycan profiling, glycomic analysis, sequencing, and site mapping using lectin microarrays, LC‑MS, HPLC, and MS. Ensures your glycoprotein antigen is fully characterized for site-specific antibody targeting.
Analyze glycosylation patterns of your antibodies (especially Fab/Fc domains) using advanced MS, LC-MS, HPLC, and electrophoresis methods to ensure functionality, stability, and safe.
Creative Biolabs provides end-to-end anti-carbohydrate antigen antibody development services, enabling you to overcome the unique challenges of glycan immunology. From antigen design to validated antibodies, we deliver precision, reliability, and innovation tailored to your project.
Contact our team for more information and to discuss your Project.
Reference
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Kappler, Katharina, and Thierry Hennet. “Emergence and significance of carbohydrate-specific antibodies.” Genes and immunity vol. 21,4 (2020): 224-239. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.1038/s41435-020-0105-9
For Research Use Only.
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