Non-IgG Therapeutic Antibodies Engineering Service
One-stop IgA, IgE and IgM antibody engineering services, customized according to your needs.
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Direct-targeting monoclonal antibodies (mAbs) approved for usage in oncology mainly belong to the immunoglobulin (Ig) G class currently. In fact, non-IgG therapeutic antibodies come of age with major progress in different kinds of human diseases, such as cancers and chronic inflammation. IgG mAb is no longer the only player in the therapeutic fields owing to antibody engineering technique, which is further driving the development of novel antibody formats. Besides, genetically modified cell-based therapies that harness the power of the immune system, together with non-IgG therapeutic antibodies, have improved cures in intractable human diseases. As an acknowledged antibody service provider, Creative Biolabs now offers various non-IgG therapeutic antibody engineering services to help our customers obtain ideal results and promote their research and projects successfully.
Chimeric Non-IgG Antibody
Chimeric antibodies are modified antibodies that combine the antigen-binding regions of one species with the constant domains of another to reduce immunogenicity. A key early use was transforming mouse monoclonal antibodies into mouse-human chimeric antibodies, retaining antigen specificity while enhancing compatibility. These antibodies offer advantages over original ones, including longer half-life, reduced immunogenicity, and improved complement-dependent cytotoxicity (CDC) and antibody-dependent cell-mediated cytotoxicity (ADCC). Since the introduction of this technology in 1984, the FDA has approved several chimeric antibody drugs, such as Infliximab, Cetuximab, and Abciximab, which are all IgG isotypes used to treat inflammation, autoimmune diseases, and tumors. To address the limitations of non-human antibodies, Creative Biolabs applies recombinant technology to create non-IgG chimeric antibodies.
| Our Service | Learn More |
|---|---|
| Chimeric IgA Antibody Engineering Service | |
| Chimeric IgM Antibody Engineering Service | Engineered IgM/IgG Chimeric Antibody |
| Chimeric IgE Antibody Engineering Service |
Schematic diagram of
chimeric antibody construction1
Humanized Non-IgG Antibodies
Antibody humanization is essential for reducing immunogenicity, improving pharmacokinetics, and preserving the affinity and specificity of therapeutic monoclonal antibodies (mAbs) derived from non-human systems. Techniques such as complementarity determining the region (CDR) grafting, chain shuffling, and resurfacing are commonly used for this purpose. As non-IgG antibodies like IgA, IgM, and IgE gain importance in diagnosis and treatment, Creative Biolabs offers advanced humanization services. Using recombinant DNA technologies, we optimize non-IgG antibodies by inserting CDR segments into human frameworks, enhancing their therapeutic potential.
| Our Service |
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| Antibody Humanization Design |
| Vector Synthesis and Cloning |
| Transient Expression |
| Stable Expression of Cell Lines |
Glycosylated Non-IgG Antibody
Glycosylation, a post-translational modification, involves attaching glycan sugars to proteins, lipids, or other molecules through enzymatic processes in the Golgi apparatus and endoplasmic reticulum. The two primary types are O-linked and N-linked glycosylation, contributing to protein diversity and influencing molecular activity. Therapeutic antibodies benefit from glycosylation modifications, especially in the Fc and sometimes Fab regions, enhancing functions such as stability, safety, and efficacy. While most glycoengineering efforts focus on IgG antibodies, non-IgG antibodies like IgA, IgM, and IgE possess unique glycosylation sites, with more glycan sites than IgG. Developing glycosylated non-IgG antibodies is essential for improving their therapeutic performance and expanding their clinical potential.
| Our Service | Our Platform |
|---|---|
| IgA Glycosylation Service | Antibody GlycoOpitimize Platform |
| IgM Glycosylation Service | |
| IgE Glycosylation Service |
Bi-specific Non-IgG Antibody
Bispecific antibodies (BsAbs) are specialized antibodies capable of binding two different targets simultaneously, such as antigens, receptors, or cells. BsAbs come in various formats, including IgG-like (with Fc regions) and non-IgG-like structures. They are widely used in diagnosis, drug delivery, and therapy, particularly in cancer immunotherapy, due to their ability to link cytotoxic cells with specific targets for enhanced therapeutic effects. Several BsAbs have been approved for cancer treatment, with many others in clinical trials. Creative Biolabs focuses on advancing non-IgG BsAbs, leveraging the unique properties of antibodies like IgA, IgM, and IgE, such as mucosal immunity and complement activation. This strategy addresses a gap, as most BsAbs in clinical use are based on IgG isotypes. By integrating BsAbs with non-IgG antibodies, Creative Biolabs aims to optimize therapeutic performance and expand treatment possibilities.
| Our Service | |
|---|---|
| BsAb Design | Target Binding |
| Isotype Selection | |
| Mode of Action | |
| Optimization to Improve Properties | Half-life |
| Size | |
| Stability | |
| Production in Quantities | Recombinant DNA Technology |
| Hybrid-Hybridoma Technology | |
| Isotype Converting | |
| Conjugation | |
Half-life Extension for Non-IgG Antibody
Half-life refers to the time required to eliminate 50% of an antibody from the body, impacting the dosage and frequency of therapeutic agents. Prolonging antibody half-life improves efficacy, reduces treatment cycles, and lowers costs, which are critical in the growing therapeutic antibody market. Both IgG and non-IgG antibodies show species-specificity in target binding and stability, with Fc regions playing a crucial role in long-term stability. However, non-IgG antibodies lack binding sites for FcRn, limiting their half-life. Solutions such as glycoengineering, albumin fusion, and constructing hybrid antibodies can extend non-IgG antibody retention, enhancing their pharmacokinetics and therapeutic potential. Creative Biolabs leverages these strategies to develop functional non-IgG antibodies with improved exposure and efficacy.
Antibody Isotype Switching
Selecting the appropriate antibody isotype is crucial for effective therapies, as different immunoglobulins (IgG, IgA, IgE, IgM, and IgD) play distinct roles in immune responses. Class switching occurs naturally when B cells transition from producing IgM to other isotypes, with the variable region of the antibody remaining unchanged to retain antigen specificity. This switch allows antibodies to engage different immune mechanisms, enhancing their ability to combat pathogens. In vitro, class-switch recombination (CSR) involves modifying the constant region of the heavy chain through DNA recombination processes initiated by activation-induced cytidine deaminase. Aided by antibody engineering techniques, we provide isotype switching services among the IgG, IgA, IgE, and IgM isotypes.
Mechanism of class-switch recombination that allows isotype
switching in activated B cells
Non-IgG Antibody Drug Conjugates
Antibody-drug conjugates (ADCs) are advanced biopharmaceuticals that combine mAbs with cytotoxic agents to target cancer cells while minimizing harm to healthy tissue. Traditional chemotherapy drugs, with low selectivity, damage both tumor and normal cells, and many approved antibody therapies require combination with chemical drugs. ADCs address this by attaching cytotoxic agents to human or humanized mAbs through chemical linkers, ensuring targeted delivery of the drug within cancer cells. Despite the growing interest in ADCs, current developments focus exclusively on IgG antibodies, overlooking the unique therapeutic potential of non-IgG antibodies due to production challenges. Creative Biolabs offers comprehensive design and development services for non-IgG ADCs, aiming to unlock new therapeutic possibilities beyond traditional IgG-based platforms.
| Our Service | |
|---|---|
| Non-IgG ADC design | |
| Linker and Conjugation Services | Linkers Synthesis |
| Linkers Modification | |
| Assembly | |
| Evaluation Services | In Vitro Evaluation |
| In Vivo Evaluation | |
Follow the pace of industry leaders and accelerate your research progress with tailored solutions and detailed data reports.
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Service Advantages
- Comprehensive Non-IgG Expertise - Extensive experience in IgA, IgM, and IgE antibody engineering.
- Short Turnaround Time - Rapid project completion with efficient workflows ensures results in the shortest possible timeframe.
- Competitive Pricing - Cost-effective solutions are offered without compromising quality, with flexible pricing options to fit various budgets.
- Detailed Data Reports - Each project includes detailed data analysis and reports, covering experimental design, methodologies, and results to ensure full transparency.
- Customized Solutions - Antibody engineering strategies are tailored to specific needs, maximizing experimental success and efficiency.
- High Reproducibility and Consistency - Advanced platforms and rigorous quality control deliver consistent, reliable results.
- Flexible Project Management - Real-time updates and adaptable communication channels keep projects on track with room for adjustments when necessary.
- Broad Application Scope - Services cover diverse fields like oncology and chronic inflammation, providing comprehensive research support.
- Compliance and Data Security - All processes adhere to international standards, ensuring regulatory compliance and data protection throughout.
- Customizable Production Platforms - Offers both transient and stable expression systems to meet research needs.
FAQs
Q1: Why should I consider non-IgG antibodies for my therapeutic project?
A: Non-IgG antibodies, such as IgA, IgM, and IgE, have emerged as essential tools for treating complex human diseases like cancer and chronic inflammation. These antibodies possess unique properties, including distinct glycosylation patterns, mucosal immunity and complement activation, making them valuable alternatives to traditional IgG antibodies.
Q2: What role does glycosylation play in non-IgG antibody performance?
A: Glycosylation, a post-translational modification, enhances the stability, safety, and efficacy of non-IgG antibodies. Non-IgG antibodies contain unique glycosylation sites, offering distinct therapeutic advantages. Adjusting glycosylation patterns through engineering can significantly improve antibody functionality and clinical outcomes.
Q3: How do bispecific non-IgG antibodies enhance therapeutic efficacy?
A: Bispecific non-IgG antibodies can simultaneously bind to two distinct targets, such as antigens or receptors, facilitating enhanced therapeutic effects. These antibodies are particularly useful in cancer immunotherapy, as they bridge cytotoxic cells with specific targets. Non-IgG bispecific formats leverage the unique immune properties of antibodies like IgA and IgM, expanding therapeutic options beyond traditional IgG-based antibodies.
Q4: Why is antibody humanization important for non-IgG antibodies?
A: Humanization of non-IgG antibodies minimizes immune responses in humans by grafting key antigen-binding regions onto human frameworks. This process maintains antibody specificity and improves pharmacokinetics, enabling safer and more effective treatments. Humanized non-IgG antibodies, like those based on IgA, IgM, and IgE, are increasingly being applied in diagnostics and therapies.
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Reference
- Xiao, Yan, et al. "A therapeutic chimeric IgG/IgA expressed by CHO cells for oral treatment of PED in piglets." Frontiers in Microbiology 13 (2022): 1018748. Distributed under the Open Access license CC BY 4.0, without modification.
KINDLY NOTE
!! For Research Use Only. Our products and services are NOT intended for diagnostic or therapeutic applications.
