The Abundant Resource for Glycobiology: Blood Group Antigens Library (BGAL)
Decipher the critical "Sugar Code" that governs cell recognition, immunity, and disease with our premier BGAL. Our comprehensive, rigorously synthesized Glycan Library provides the necessary gold standard tools for precision glyco-analysis across all research and commercial domains.
Historically, researchers and IVD manufacturers have struggled with antigens derived from natural sources (e.g., human red blood cells or biological fluids). These sources introduce insurmountable issues that stifle commercial and clinical development:
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Extreme batch-to-batch variability: Natural glycans are complex mixtures, often containing incomplete or heterogeneous glycosylation patterns, leading to irreproducible results in sensitive assays and diagnostic kits. Our synthetic approach guarantees a single, defined isomer, eliminating this inherent variation.
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Biohazard and regulatory risk: Reliance on human or animal sources carries potential risks of transmitting viruses or other adventitious agents, creating significant and costly hurdles in regulatory approval processes.
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High cost: Isolating and purifying low-abundance natural glycans is prohibitively expensive and inefficient. Synthetic production offers a lower, scalable unit cost critical for high-volume commercial applications, maximizing your return on investment.
Creative Biolabs developed abundant BGAL resources according to cutting-edge chemoenzymatic and total chemical synthesis, resolving various challenges, ensuring:
Specialized BGAL Products
Creative Biolabs is an accredited technical partner committed to the success and compliance of your most demanding projects, from early-stage discovery to final regulatory approval. The table below shows the structures of common compounds in BGAL.
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Common BGAL Structures
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CAT#: GLJF-1125-HX577
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CAT#: GLJF-1125-HX578
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CAT#: GLJF-1125-HX579
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CAT#: GLJF-1125-HX580
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CAT#: GLJF-1125-HX581
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CAT#: GLJF-1125-HX582
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CAT#: GLJF-1125-HX583
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CAT#: GLJF-1125-HX584
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CAT#: GLJF-1125-HX585
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CAT#: GLJF-1125-HX586
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CAT#: GLJF-1125-HX587
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CAT#: GLJF-1125-HX588
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CAT#: GLJF-1125-HX589
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CAT#: GLJF-1125-HX590
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CAT#: GLJF-1125-HX591
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CAT#: GLJF-1125-HX592
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CAT#: GLJF-1125-HX593
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CAT#: GLJF-1125-HX594
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CAT#: GLJF-1125-HX595
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CAT#: GLJF-1125-HX596
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CAT#: GLJF-1125-HX597
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CAT#: GLJF-1125-HX598
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CAT#: GLJF-1125-HX599
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CAT#: GLJF-1125-HX600
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CAT#: GLJF-1125-HX601
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CAT#: GLJF-1125-HX602
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CAT#: GLJF-1125-HX603
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CAT#: GLJF-1125-HX604
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CAT#: GLJF-1125-HX605
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CAT#: GLJF-1125-HX606
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CAT#: GLJF-1125-HX607
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CAT#: GLJF-1125-HX608
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CAT#: GLJF-1125-HX609
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CAT#: GLJF-1125-HX610
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CAT#: GLJF-1125-HX611
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CAT#: GLJF-1125-HX612
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CAT#: GLJF-1125-HX613
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CAT#: GLJF-1125-HX614
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CAT#: GLJF-1125-HX615
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CAT#: GLJF-1125-HX616
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CAT#: GLJF-1125-HX617
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CAT#: GLJF-1125-HX618
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Unparalleled Structural Diversity
The immense biological specificity of blood group antigens is encoded in subtle structural nuances, dictated by specific glycosidic linkages and the underlying core chain. Our library meticulously captures this diversity, offering precisely synthesized structures. We provide single-isomer glycans of uncompromising chemical purity. This purity is vital for establishing gold-standard binding kinetics and thermodynamics using surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC).
Table 1 Specialized blood group antigens library and applications.
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Structural Family
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Description
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Example Structures
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Fucosylated structures (H and Lewis series)
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Core to the ABO and Lewis systems. These α 1-2 and α 1-3 fucosylated structures are involved in defining precursor chains and are critically implicated in epithelial pathogen adhesion, inflammation, and as tumor-associated carbohydrate antigens (TACAs) like Lewis-y and Lewis-x. Our library includes antigens based on both type 1 and type 2 core chains.
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Structures based on the type 2 H-antigen, Lewis-a, Lewis-b, and key α2 and α4 fucosylation motifs. Our library enables discrimination between Lewis-a and Lewis-b antibodies with unprecedented precision.
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A and B antigens
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The most clinically significant structures due to their high immunogenicity. Used extensively as core reference standards for characterizing IgM and IgG anti-A/B antibodies responsible for acute and delayed hemolytic transfusion reactions. Our collection includes A and B epitopes synthesized on type 1, type 2, and branched (type 4) core chains, mimicking natural presentation complexity.
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Structures based on type 2 B-antigen, type 2 A-antigen, Branched A/B antigens, and various α3 GalNAc and α3 Gal linkages that define A and B specificity.
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Extended and branched structures
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These structures are vital for investigating parvovirus B19 receptor binding (P-antigen) and for detailed analysis. Branched structures precisely simulate the high-density presentation on the red cell membrane.
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P1-antigen fragments, various β3 and β4 galactose motifs, α2 fucosylation patterns, and extended I-antigen structures.
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We guarantee the correct anomeric configuration (α or β) and the precise glycosidic linkage geometry. Quality control involves advanced nuclear magnetic resonance (NMR), high-resolution mass spectrometry (HRMS), and multi-mode high-performance liquid chromatography (HPLC). This level of verification is non-negotiable, ensuring biological activity and regulatory acceptance.
Tailored for Commercialization and Discovery
We offer the BGAL in different strategically functionalized formats to seamlessly support every phase of your research and commercialization pipeline. Our synthetic glycan antigens are the gold-standard analytical tools, provided with flexible C3-C6 spacer arms or in PEGylated form for enzyme kinetics. Secondly, glycoconjugates (neoglycoproteins and neoglycolipids) act as powerful immunogen engines, coupling antigens to high-density carriers (KLH or BSA) for glyco-conjugate vaccine development and accurate membrane biophysics studies. The BGAL is an indispensable asset for translational research, providing solutions to clinical and commercial challenges across multiple sectors.
Infectious disease and microbiology
Many clinically significant pathogens exploit blood group antigens as primary host receptors for initial attachment and infection. Our highly defined synthetic glycan library enables researchers to perform precise epitope mapping, allowing for the identification of high-affinity binding sites. This fundamental knowledge is crucial for the rational design and development of effective countermeasures.
Cancer glycobiology
The synthetic purity of our products is vital for generating highly specific monoclonal antibodies, engineering next-generation CAR-T cells, and creating powerful therapeutic cancer vaccines designed to induce robust, T-cell-mediated immune responses against these abnormal glycan markers.
Immunology
Our library plays a critical role in understanding the mechanisms of molecular mimicry in autoimmune disorders. Specific blood group structures share critical homology with autoantigens like gangliosides, implicated in conditions such as Miller Fisher Syndrome. Utilizing our pure antigens, researchers can accurately diagnose and differentially analyze pathological antibodies, advancing the development of targeted diagnostics and superior immunoglobulin preparations with enhanced neutralizing activity.
Request A Personalized Quotation
Ready to establish a new gold standard in your diagnostic kit, drug discovery, or vaccine program? Partner with Creative Biolabs for reliable, scalable, and structurally verified synthetic glycans. We possess a rich library of glycans, including N-Glycan, O-Glycan, Mannose Glycan, etc. Please contact us to inquire about your personalized quotation today!