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Need a reliable method for discovering high-quality antibodies to diagnose or treat human autoimmune diseases?
Discover our world’s first human autoimmune antibody phage display library. These unique libraries are a rich source of high-affinity antibodies targeting specific autoimmune antigens, ready to be developed into the next ground-breaking autoimmune conditions
Interested in customizing your autoimmune antibody?
Optimize your antibody’s developability and take benefit from our advanced customization options tailored to your specific requirements. Get a comprehensive solution for all your custom autoimmune disease diagnostics and therapies with the help of our antibody experts!
Experience accelerated target therapy discovery and market entry with our unique human autoimmune library.
You have exclusive ownership of the custom-generated monoclonal antibodies targeting autoimmune diseases.
Get at minimum three distinct antibodies specifically binding to your autoimmune-specific antigen(s).
Streamline your process and save valuable time and resources by leveraging our pre-built human autoimmune phage display libraries.
Take advantage from our expertise and get your fully human clinical antibodies, without the need for humanization.
Minimize your efforts with our additional services, including customized antigen production and comprehensive antibody developability assessment. We handle it all for you!
Safeguard your antibody investment through milestone-based services designed for complex and high-risk projects.
Take advantage from our pre-built autoimmune libraries offering the advantages of customized libraries from immunization, combined with the efficiency of reduced delivery time found in naïve libraries.
2. Autoimmune Library Screening and Biopanning
3. ELISA Screening of Single Phage Binders
4. DNA Extraction & Antibody Sequencing
Recombinant antibody production
Therapeutic antibody production
Stable Cell Line Development
ADC development
Bispecific and Trispecific Antibodies
Antibody Developability
Are you in search of a game-changing solution for developing custom anti-autoimmune antibodies ? Look no further than antibody phage display, a revolutionary technology that is transforming the field of antibody discovery. Antibody phage display can produce tailor-made antibodies targeting autoimmune disease-specific antigens. Here are some reasons why this antibody discovery method is most suited for identifying novel autoimmune antibodies :
Antibody phage display libraries offer a vast repertoire of diverse antibodies for precise targeting of autoimmune antigens.
Antibody phage display enables the isolation of high-affinity, specific antibodies with minimized risk of off-target effects.
Streamlined processes and expertise ensure faster delivery of custom anti-autoimmune antibodies.
Access our team of antibody experts for personalized support throughout the development process.
The benefits of antibody phage display for making custom monoclonal anti-autoimmune antibodies are not possible without the perfect phage display library.
The probability that antibody phage display will deliver high-performing human autoimmune therapeutic or diagnostic antibodies is significantly increased when the library is engineered using the following factors :
ProteoGenix is proud to state that our antibody experts made such a library. In fact, we made the world’s first human autoimmune antibody phage display library designed to supercharge human autoimmune antibody discovery and market entry.
This pre-built antibody library represents an array of high-affinity autoimmune-specific antibodies. Unlike traditional custom libraries derived from immunized (non-human) hosts, our libraries offer a rich source of diverse antibodies. Here’s why our libraries are a game-changer:
With over 10^11 unique antibody clones and an exceptional in-frame frequency exceeding 94%, our libraries provide an expansive range of novel autoimmune immunotherapies waiting to be explored.
Our pre-built human autoimmune antibody libraries offer the advantage of swift delivery and cost reduction. We eliminate the time-consuming process of custom library construction, enabling you to access high-performing antibodies quickly and efficiently.
| Library Name | Species | Clone Number |
|---|---|---|
| LiAb-SFAUTOIMMTM Library | Human Donors (42 patients with 7 different autoimmune diseases):
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With ProteoGenix’s cutting-edge human autoimmune libraries, you can rapidly discover high-performing monoclonal antibodies that bind specific autoantigens. Our antibody phage display service also provides exclusive access to IP-free DNA sequences for three high-affinity binders tailored to your target autoantigen.
Experience unmatched efficiency with our streamlined project timeline. From antigen design and purification to delivery of antibody DNA sequences, we can complete each project in just 8 weeks. This rapid turnaround sets us apart in the market, saving you valuable time and ensuring prompt progress.
ProteoGenix goes the extra mile to minimize your efforts by offering additional services that cater to your needs:
We provide stable cell line expression of antibody-encoding DNA sequences, ensuring the reliable production of your anti-autoimmune antibody.
Our experts assess the developability profile of your antibody, determining its clinical suitability and optimizing its potential.
We specialize in enhancing the developability of your anti-autoimmune antibody, maximizing its effectiveness in clinical applications.
Tailor your anti-autoimmune antibodies to meet your specific requirements. We offer customization services such as antibody-drug complex (ADC) development and bispecific antibody development.
By entrusting your challenging autoimmune immunotherapy projects to our team of antibody experts, you can free up your valuable time, resources, and costs. With the added advantage of our antibody expression, developability assessment, and customization services, you’ll expedite your journey to the clinic while maximizing your efficiency and success.
Kappa and lambda light chains are merged during processing, limiting clone diversity and introducing construction bias.
Kappa and lambda light chains are processed separately, unlocking unparalleled clone diversity with minimal construction bias.
Greater odds of finding high-affinity binders
Even against autoimmune neoantigens and conserved human antigens
Antibodies built to advance into clinical development
In the early stages of autoimmune disease, a breach in self-tolerance drives the immune system to attack the body’s own healthy tissue.Loss of self-tolerance
The immune system loses the ability to distinguish self-antigens from non-self antigens, breaching self-tolerance.
The immune system loses the ability to distinguish self-antigens from non-self antigens, breaching self-tolerance.
2. Autoreactive T and B cells expand
This breakdown drives the expansion of autoreactive T cells and B cells. B cells mount an antibody-dependent attack against healthy tissue.
3. Antibodies captured for clinical use
B cells collected from the blood of an autoimmune patient provide a diverse repertoire of autoreactive antibodies, ready for clinical use.
An immune phage display library sourced from autoimmune patients offers a diverse repertoire of antibodies that have already undergone natural affinity maturation and selection against autoimmune antigens — giving exceptional binding affinity and therapeutic potential that surpasses naive libraries built from healthy donors.
Because the library is human-derived, the risk of immune reactions and adverse effects in therapeutic applications is significantly reduced compared to non-human sources — a key step toward safer, more effective autoimmune treatments.
Antibodies derived from our human autoimmune phage display libraries represent a uniquely valuable resource for your therapeutic development program, thanks to their inherent ability to target autoantigens with exceptional precision. Having likely undergone affinity maturation within the autoimmune microenvironment itself, these antibodies are naturally optimized to deliver more precise and potent therapeutic interventions than antibodies sourced from healthy or immunized donors.
Each library we generate is an untapped source of diverse, highly specific antibodies, giving you a genuine competitive advantage in the development of groundbreaking treatments for autoimmune conditions and opening pathways to therapeutic candidates that would be difficult to obtain through conventional approaches.
| Naive Antibody Library (Human Donor) | Immune Antibody Library (Human Donor) | Immune Library (Non-Human Host) | |
|---|---|---|---|
| Source | Healthy Human Donors | Autoimmune Patients | Immunized Animals (non-human) |
| Antibody Diversity | Broad | Autoimmune Antigen Skewed | Immunized Antigen Skewed |
| Target Specificity | Limited Antigen-specific Antibodies | Increased Autoimmune-specific Antibodies | Increased Antigen-specific Antibodies |
| Affinity Maturation | Minimal Affinity Maturation | Affinity Maturation to Autoantigens | Affinity Maturation to Immunized Antigen |
| Immunogenicity Risk | Fully Human – Minimal Immunogenicity Risk | Fully Human – Minimal Immunogenicity Risk | Risk of an Immune System Reaction |
| Clinical Translation | May Require Additional Optimization and Engineering | Accelerated Leads for Autoimmune-Specific Therapies and Diagnostics | May require further Characterization and Optimization |
Autoimmunity refers to the immune system attack of healthy cells, tissues, and other normal components of the body in the field of immunology. When this immune response results in a disease, it is known as an “autoimmune disease.”
Autoimmunity refers to the presence of antibodies or T cells that react with the body’s proteins. It is observed in all individuals, even in a healthy state. However, if this self-reactivity leads to tissue damage, it can result in autoimmune diseases.
Notable examples of such diseases include celiac disease, post-infectious irritable bowel syndrome (IBS), type 1 diabetes mellitus, Henoch–Schönlein purpura (HSP), sarcoidosis, systemic lupus erythematosus (SLE), Sjögren syndrome, eosinophilic granulomatosis with polyangiitis, Hashimoto’s thyroiditis, Graves’ disease, idiopathic thrombocytopenic purpura, Addison’s disease, rheumatoid arthritis (RA), ankylosing spondylitis, polymyositis (PM), dermatomyositis (DM), and multiple sclerosis (MS). The most common treatment for autoimmune diseases are steroids.
Loss of self-tolerance can lead to autoimmunity because it disrupts the immune system’s ability to distinguish between “self” and “non-self” antigens. In a healthy immune system, there are mechanisms in place to recognize and tolerate the body’s cells and tissues, while mounting an immune response against foreign substances or pathogens.
Self-tolerance is primarily maintained through a process called central tolerance, which occurs in the thymus and bone marrow. During this process, immune cells called T cells and B cells undergo education and selection to eliminate those that would react against the body’s proteins. However, in some cases, this process can be imperfect, leading to the survival of self-reactive lymphocytes.
Additionally, peripheral tolerance mechanisms function outside the primary lymphoid organs to prevent autoreactive lymphocytes from causing harm. These mechanisms include regulatory T cells that suppress immune responses against self-antigens.
When self-tolerance is compromised, autoreactive lymphocytes can escape elimination or regulation and recognize and attack the body’s cells and tissues. This results in chronic inflammation and tissue damage, characteristic of autoimmune diseases. While the exact mechanisms causing loss of self-tolerance are not fully understood they likely involve genetic predispositions, environmental triggers, and dysregulation of immune checkpoints.
mRNA is extracted from human or animals B-cells and reverse-transcribed into cDNA
2. Amplify variable regions
PCR generates the heavy and light chain variable regions using the antibody cDNA as a template
3. Insert into phage vector
The variable regions are inserted into a modified phage display vector. This vector is designed to express the antibody variable regions as a fusion protein alongside a coat protein on the phage’s surface. The antibodies are “displayed” on the phage’s exterior, while the DNA encoding the antibody remains enclosed inside the phage particle.
4. Screen, isolate & sequence
A naive library is built by incorporating genes from an organism that has never encountered the antigen of interest. It offers a broad assortment of antibodies that have not undergone any antigen driven selection. This lack of prior selection increases the potential for discovering novel antibodies with distinctive binding properties, since the full diversity of the immune repertoire remains available.
An immune library is built by incorporating genes from an organism that has been immunized with the antigen of interest. It consists of antibodies that have already undergone selection based on their capacity to bind that specific antigen. This makes immune libraries particularly valuable for swiftly identifying antibodies with high affinity.
The primary distinction between the two lies in the origin of the genes used in their construction. Naive libraries draw on a wide range of antibodies that have never encountered the antigen of interest, while immune libraries comprise antibodies specifically chosen for their proven ability to bind that particular antigen.
A single-chain variable fragment (scFv) is a fusion protein composed of the variable regions of the heavy (VH) and light chains (VL) of immunoglobulins. It is connected by a brief peptide linker, typically consisting of approximately 10 to 25 amino acids. The linker peptide is often rich in glycine, which imparts flexibility and may contain serine or threonine to enhance solubility. The linker serves to connect either the N-terminus of the variable heavy chain (VH) to the C-terminus of the variable light chain (VL), or vice versa.
Single-chain variable fragments (scFv) offer a range of advantages compared to the parental monoclonal antibody (mAb) format, as highlighted below:
scFv molecules have a compact structure, enabling better tissue penetration and improved access to target sites.
The smaller size of scFv simplifies production and purification processes, resulting in higher yields and cost savings.
scFv can be produced using recombinant DNA technology, allowing for efficient and scalable production in various expression systems.
scFv molecules can be engineered to have multimeric forms and/or multivalency, enhancing their binding affinity and specificity compared to the parental mAb.
scFv antibody fragments can be effective in neutralizing the activity of specific autoantigens.
These advantages make scFv an attractive choice for therapeutic and diagnostic applications, offering improved properties and potential for optimization in antibody-based treatments
The fragment antigen-binding (Fab) region is a segment of an antibody that links to antigens. It comprises one variable and one constant domain from both the heavy and light chains. The variable domain encompasses the paratope, which is part of the antibody that binds to the antigen and contains a group of complementarity-determining regions located at the N-terminus of the monomer. This arrangement enables each arm of the Y-shaped antibody to attach to an epitope on the antigen.
The fragment antigen-binding (Fab) antibody format provides several advantages compared to full-length monoclonal antibodies (mAbs), as outlined below:
Fab fragments are significantly smaller than full-length mAbs, enabling improved tissue penetration and accessibility to target sites.
The smaller size of Fab fragments reduces the likelihood of triggering an immune response, making them less immunogenic.
Fab fragments can be produced more efficiently and cost-effectively compared to full-length mAbs, leading to potential cost savings.
Fab fragments exhibit high specificity for their target antigens, allowing for precise and targeted binding.
Fab fragments can be engineered for various applications, including drug delivery, imaging, and targeting specific antigens in tumors or other tissues.
The high specificity and tissue penetration of Fab fragments make them valuable in diagnostic assays and as potential therapeutics for diseases such as autoimmune and infectious diseases.
Neutralizing capacity: Fab antibody fragments can be effective in neutralizing the activity of specific autoantigens.
The unique features of the Fab antibody format position it as an attractive option for various applications, offering improved performance, versatility, and cost-effectiveness compared to full-length mAbs.