Glycosylated Non-IgG Antibodies Service

Our Service Highlights Background FAQs Resource Quotation and Ordering

The glycosylation modifications to the constant domain are crucial to antibody activities and their effector functions since glycosylation alters the affinity of antibodies to Fc receptors. With integrated antibody development and engineering techniques, Creative Biolabs offers comprehensive glycosylation services for non-IgG antibodies (IgA, IgM, and IgE). We tailor our services to develop high-quality glycosylated antibodies applied for multiple hot diagnostics. They direct against a variety of disease targets with low cross-reactivity, promoting the development of immunology methods to meet the needs of our valued clients.

Our Service

Through our antibody glycoengineering platform, Creative Biolabs offers tailored glycosylation services for IgA, IgM, and IgE antibodies. Modifications to glycan structures on the Fc region of these antibodies can lead to significant changes in their effector functions, including complement-dependent cytotoxicity (CDC), antibody-dependent cell-mediated cytotoxicity (ADCC), and antibody-dependent cell-mediated phagocytosis (ADCP). Our glycosylation services are designed to optimize these bioactivities and improve the therapeutic effects of non-IgG antibodies.

Both IgA1 and IgA2 subclasses are heavily glycosylated, with more glycosylation sites and more complex structures than IgG. These modifications include both N- and O-glycosylation, contributing to the antibody's functional diversity. We provide comprehensive IgA glycosylation services to support the development of IgA antibodies with improved performance in diagnostics and therapeutics.

IgM antibodies, particularly polymeric IgM, are characterized by extensive glycosylation, with five N-linked glycosylation sites in each heavy chain, plus an additional glycosylation site in the J chain. These glycosylation sites are essential for IgM secretion, complement activation, and B cell presentation. Our glycosylation services for IgM are aimed at optimizing these features for better therapeutic efficacy.

Human IgE antibodies are the most heavily glycosylated of all antibody isotypes, with seven glycosylation sites per heavy chain. This modification accounts for approximately 12% of the IgE molecular weight. Notably, glycosylation patterns in human IgE differ significantly from murine IgE, making glycosylation optimization an important step in developing more effective IgE-based therapies.

Highlights

  • Comprehensive Glycosylation Optimization
    Glycosylation services are designed to enhance the bioactivity and effector functions of non-IgG antibodies (IgA, IgM, IgE). These services focus on modifying glycan structures to improve antibody binding affinity to Fc receptors and to optimize therapeutic outcomes.
  • Advanced Engineering and Development
    Utilizing cutting-edge antibody development platforms, the glycosylation process for non-IgG antibodies is precisely engineered to tailor each modification, ensuring high-quality and functionally optimized antibodies suitable for various diagnostic and therapeutic applications.
  • Diverse Therapeutic and Diagnostic Applications
    Glycosylated antibodies are developed for a wide range of diseases, enhancing their utility in diagnostic tests and targeted therapies. These antibodies are specifically engineered to address multiple disease markers with high precision, aiding in the advancement of both clinical diagnostics and therapeutic research.
  • Customized Solutions for Research Needs
    The glycosylation services are highly customizable and designed to meet the unique requirements of each project. Whether for early-stage research, therapeutic development, or diagnostic applications, these tailored solutions ensure that each antibody is optimized for its specific function.
  • Expert Consultation and Support
    Throughout the glycosylation optimization process, an expert team is available to offer guidance and technical support. This ensures the delivery of high-quality, functional antibodies that align with the research or therapeutic goals, providing clients with confidence and assurance in the results.

Background

Glycosylation, a type of post-translational modification, is an enzymatic process in which glycan sugars are attached to a functional group of other glycans, lipids, proteins, or other organic molecules. In the body, glycosylation mainly takes place in the Golgi apparatus and endoplasmic reticulum, which occurs as the result of the synchronized action of glycosylation enzymes. O-linked and N-linked glycosylation are the two most common mechanisms through which glycans can be linked to lipids and proteins. Due to the difference in structure, length, composition, and glycosidic bond of the glycans, glycosylation engineering greatly increases diversity in the proteins and finely affects the activity of the modified molecules.

Fig. 1 Overview of glycosylation sites of different immunoglobulins.Fig. 1 Overview of glycosylation sites of different Ig: IgA, IgG. IgM, IgD, and IgE in individual colors.1

Therapeutic antibody is a class of monoclonal antibodies (mAbs) that bind to cells or proteins mono-specifically, which has achieved great success through technological breakthroughs. Glycosylation modifications of the Fc region, or the Fab region in some cases, can further enhance the effector functions and have a profound impact on the diversity, safety, immunogenicity, stability, and clinical efficacy of these therapeutic antibodies. Antibody glycoengineering is an important method to improve the pharmacological properties of therapeutic mAbs. However, the majority of approved or under-researched therapeutic antibodies are IgG isotypes, and engineering techniques have focused on IgG mAb glycol modification over the past decades. Actually, the glycosylation sites and glycoengineering of five antibody isotypes are quite different. The most obvious difference is that the glycosylation sites of these non-IgG antibodies are more than IgG isotype. Development of glycosylated non-IgG antibodies (mainly IgA, IgM, and IgE) to improve their performance and therapeutic effects is necessary and imperative.

FAQs

Q1: What are the differences in glycosylation between IgA, IgM, and IgE antibodies?

A: IgA antibodies are heavily glycosylated with both N- and O-linked glycosylation, more complex than that of IgG. IgM antibodies have multiple N-linked glycosylation sites, essential for complement activation and immune function. IgE antibodies are the most glycosylated of all antibody isotypes, with seven N-linked glycosylation sites, making them particularly important in allergy and immunotherapy applications.

Q2: How do glycosylation modifications improve the therapeutic efficacy of non-IgG antibodies?

A: Glycosylation modifications can enhance the antibody's ability to bind to Fc receptors more effectively, increasing its capacity to mediate immune responses such as ADCC, CDC, and ADCP. These modifications can also improve the stability, half-life, and overall pharmacokinetic properties of the antibodies, leading to more effective therapies.

Q3: What is the difference between N-linked and O-linked glycosylation?

A: N-linked glycosylation refers to the attachment of glycans to the nitrogen atom of asparagine residues in proteins, while O-linked glycosylation involves the attachment of glycans to the oxygen atom of serine or threonine residues. Both types of glycosylation play key roles in altering antibody structure and function, with N-linked glycosylation often affecting the stability and immune interactions, and O-linked glycosylation influencing the antibody's activity and specificity.

Q4: How can glycosylation services be tailored to meet specific research or therapeutic needs?

A: Glycosylation services are highly customizable, with modifications designed to meet the precise requirements of a particular project. This includes adjusting the glycosylation patterns to optimize effector functions, improve binding affinity, or enhance stability for specific diagnostic or therapeutic goals. Clients can work closely with experts to ensure the antibodies are optimized for their unique research or clinical applications.

Q5: How are glycosylation profiles analyzed and characterized?

A: Glycosylation profiles are analyzed through advanced techniques such as mass spectrometry, high-performance liquid chromatography (HPLC), and glycan microarray analysis. These techniques allow for the detailed characterization of glycan structures, enabling the optimization of glycosylation for specific therapeutic and diagnostic applications.

Resource

Youtube A Brief Introduction to Non-IgG Antibody - Creative Biolabs spotify A Brief Introduction to Non-IgG Antibody - Creative Biolabs

Creative Biolabs specializes in the development of antibodies that are suitable for a number of disease detection and analysis. Given the potential for glycosylation to benefit therapeutics, now we provide a full range of non-IgG glycosylated antibodies (IgA, IgM, and IgE) that are produced by specific expression systems. Moreover, we offer related non-IgG antibody products and customized application services for our clients to meet every specific research requirement. Please contact us to experience our first-class expert services.

Quotation and Ordering

Our customer service representatives are available 24/7/365. You may contact us anytime for assistance. Orders can be placed online, over the phone, by email, or by fax.

Fill out and submit the online inquiry form.
A Technical Account Manager will respond within 24 hours to discuss the service details and finalize the quote.
Sign the order.
Your project services will commence immediately.
A Project Manager will stay in touch with you throughout the production process to provide updates on the project's progress.
Deliverables will be provided along with the relevant experimental data.

Reference

  1. Zlatina, Kristina, and Sebastian P. Galuska. "Immunoglobulin Glycosylation–An Unexploited Potential for Immunomodulatory Strategies in Farm Animals." Frontiers in Immunology 12 (2021): 753294. Distributed under the Open Access license CC BY 4.0, without modification.
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