Monoclonal Antibody Glycan Library Products

Comprehensive Monoclonal Antibody Glycan Library

In the rapidly evolving landscape of biopharmaceuticals, the need for absolute analytical precision is paramount. Manufacturing monoclonal antibodies (mAbs) requires rigorous quality control over inherently complex structures. Our monoclonal antibody glycan Library is designed not just as analytical tools, but as essential infrastructure for any lab engaged in cutting-edge mAb development, quality control, and comparability studies. Creative Biolabs provides the certified molecular keys to unlock the complexity of protein glycosylation.

mAbs are the dominant class of biotherapeutics; yet, their efficacy, safety, and pharmacokinetics are critically dependent on their N-glycosylation profile, primarily located in the Fc region. This glycosylation pattern is inherently heterogeneous, making consistent measurement a formidable challenge. In addition, regulatory bodies demand highly resolved and validated glycan profile data to ensure product consistency and safety. Our comprehensive mAbs glycan library provides the traceable standards necessary to ensure the highest level of confidence, reproducibility, and compliance in your analytical data. Our mAbs glycan library is meticulously derived from high-quality antibody scaffolds, typically immunoglobulin G (IgG), ensuring biological relevance to therapeutic pipelines. These products are certified glycan reference standards meticulously purified, structurally validated, and characterized for use in routine quantitative and qualitative analysis. Each batch is subjected to rigorous quality control processes to confirm purity, structure, and accurate concentration.

Fig.1 The structure of human IgG.¹

Unique Monoclonal Antibody Glycan Standard Products

Leveraging high-resolution liquid chromatography and rigorous structural identification, Creative Biolabs provides a complete set of fully characterized monoclonal antibody (mAb) N-glycan library standards to ensure the highest level of accuracy and reliability in your biopharmaceutical quality control and R&D processes.

Glycan Standard Products
CAT#: GLJF-1125-HX619	CAT#: GLJF-1125-HX620	CAT#: GLJF-1125-HX621	CAT#: GLJF-1125-HX622
CAT#: GLJF-1125-HX623	CAT#: GLJF-1125-HX624	CAT#: GLJF-1125-HX625	CAT#: GLJF-1125-HX626
CAT#: GLJF-1125-HX627	CAT#: GLJF-1125-HX628	CAT#: GLJF-1125-HX629	CAT#: GLJF-1125-HX630
CAT#: GLJF-1125-HX631	CAT#: GLJF-1125-HX632	CAT#: GLJF-1125-HX633	CAT#: GLJF-1125-HX634
CAT#: GLJF-1125-HX635	CAT#: GLJF-1125-HX636	CAT#: GLJF-1125-HX637	CAT#: GLJF-1125-HX638

The Library Portfolio-Solutions for Every Analytical Platform

Glycomics is a multifaceted discipline, requiring specialized tools for optimal results. Our Glycan Library Product Line recognizes this diversity by offering specialized libraries optimized for maximum performance across the most demanding separation and detection platforms. Whether your lab relies on chromatographic separation for throughput or direct mass measurement for high resolution, we have the gold-standard solution.

Understanding the Biological Impact of mAbs Glycan Structure

Every library we produce is meticulously manufactured and accompanied by comprehensive documentation to ensure absolute confidence in your results and compliance with global guidelines.

Enzymatic Release Control

Glycans are released from the high-quality source material using highly specific, certified enzymes (e.g., PNGase F) to ensure intact structures and minimize non-specific linkage artifacts.

Chromatographic Purification

Extensive sequential purification steps, including high-performance hydrophilic interaction liquid chromatography (HILIC-HPLC) and ion-exchange, are employed to isolate individual glycan species to a certified purity level.

Structural Validation

Each species is confirmed using multiple orthogonal methods, including high-resolution mass spectrometry for linkage and sequence data, and exoglycosidase digestions to confirm linkage and anomeric configuration.

Quantitative Certification

The final concentration of the reference standard is precisely determined using certified methods, enabling accurate absolute quantification in the customer's workflow.

The core library is built around the fundamental bi-antennary N-glycan structures found on the human IgG Fc fragment. These standards allow precise mapping and quantification of critical structural elements whose presence directly impacts drug functionality, half-life, and immunogenicity. All standards are based on the common core pentasaccharide structure (Man3GlcNAc2). Variations occur primarily at three biologically critical points: fucosylation, galactosylation, and sialylation. Precise monitoring of these variations is non-negotiable for biopharma success and therapeutic performance.

Table 1 A diverse core library.

Our standards contain purified and quantified samples of these individual, complex species. This critical resource allows you to accurately assign chromatographic peaks and mass signals in your unknown mAb sample, guaranteeing correct structural identification and reliable absolute quantification. In addition, we also provide other glycan libraries, including N-Glycan, O-Glycan, HMO-Glycan, Mannose Glycan Libraries, etc., to support your project research.

How to Contact Us

Are you currently struggling with method transfer failures, inconsistent batch release data, or long development times for generating reliable in-house standards? Your solution is Creative Biolabs here. Incorporate our monoclonal antibody glycan library into your analytical workflow today. We provide the highest-purity, traceable standards you need to ensure reliable, high-quality data for your critical biopharmaceutical projects. Please contact our dedicated technical team today to request a quote or schedule a complimentary consultation on seamlessly integrating these gold-standard standards into your specific analytical platform.

Reference

1. Mesonzhnik, Natalia et al. "Enhanced N-Glycan Profiling of Therapeutic Monoclonal Antibodies through the Application of Upper-Hinge Middle-Up Level LC-HRMS Analysis." Antibodies (Basel, Switzerland) vol. 13,3 66. 6 Aug. 2024. Distributed under an Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/antib13030066