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Developing antibodies against cancer targets? Discover the world’s first Human Cancer Phage Display Library
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!
The World's First Autoimmune Antibody Library
Experience accelerated target therapy discovery and market entry with our unique human autoimmune library.
IP free
You have exclusive ownership of the custom-generated monoclonal antibodies targeting autoimmune diseases.
Binders guaranteed
Get at minimum three distinct antibodies specifically binding to your autoimmune-specific antigen(s).
Pre-built phage display libraries
Streamline your process and save valuable time and resources by leveraging our pre-built human autoimmune phage display libraries.
Fully human antibodies
Take advantage from our expertise and get your fully human clinical antibodies, without the need for humanization.
Integrated Services
Minimize your efforts with our additional services, including customized antigen production and comprehensive antibody developability assessment. We handle it all for you!
Flexible Antibody Development
Safeguard your antibody investment through milestone-based services designed for complex and high-risk projects.
Decreased Time to Market
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.
Your autoimmune-specific antigen can be acquired by:
Autoimmune Library Screening and Biopanning
ELISA Screening of Single Phage Binders
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:
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 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:
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.
Tap into the unlimited possibilities antibody phage display has to offer with our proprietary antibody library. Unlike conventional methods that merge kappa and lambda light chains, our library takes a unique approach by segregating their processing. This breakthrough technique fosters an unparalleled diversity of distinct antibody clones while minimizing construction bias. Prepare to embark on a journey of enhanced antibody discovery and selection, fueled by the power of diversity.
Experience a paradigm-shifting methodology that significantly amplifies your chances of unearthing high-affinity antibodies with no cross-reactivity against challenging antigens such as autoimmune neoantigens and highly conserved human antigens. Our advanced approach propels ProteoGenix to deliver antibodies of superior quality, elevating the potential of your antibody to advance to the forefront of clinical development stages. Embrace this cutting-edge methodology and unlock the pathway to success.
During the initial stages in the development of an autoimmune disease the patient’s immune system loses the ability to distinguish self-antigen from non self-antigens. This results in a breach in self-tolerance resulting in the lymphocyte (T-cells and B-cells) attack of healthy tissue.
This inability to distinguish healthy tissue from foreign tissue results in the expansion of auto-reactive T cells and B cells. The later of which mounts an antibody-dependent attack of self-antigens.
B cells collected from the blood of an individual suffering from an autoimmune disease can be collected to capture a diverse repertoire of autoreactive antibodies for clinical use.
An immune phage display library sourced from autoimmune patients provides a diverse repertoire of antibodies that have undergone natural affinity maturation and selection against autoimmune antigens. This unique collection of antibodies has exceptional antigen-binding affinity and heightened therapeutic potential, surpassing those derived from a naïve library constructed from healthy donors.
By harnessing the power of a human-derived library, the risk of immunogenicity and adverse reactions during therapeutic applications is significantly reduced. By utilizing a human-derived library in autoimmune immunotherapy, the risk of immune reactions and adverse effects in therapeutic applications is greatly diminished. The use of human-derived antibodies enhances compatibility and reduces the potential for immunogenicity compared to non-human sources. This approach holds promise for safer and more effective treatments in autoimmune diseases.
The antibodies derived from our human autoimmune phage display libraries offer immense value due to their inherent ability to target autoantigens. These antibodies hold the potential for delivering more precise and potent therapeutic interventions, as they have likely undergone affinity maturation processes driven by the autoimmune microenvironment.
As a result, each library represents an untapped source of diverse and highly specific antibodies, opening new avenues for the development of groundbreaking and effective antibodies targeting autoimmune conditions.
The table below provides a concise overview of antibody characteristics from autoimmune donors, comparing them with those from healthy human donors and immunized hosts.
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.
Antibody phage display is a laboratory technique that explores the interactions between antibodies and various molecules, including antigens. It involves genetically modifying bacteriophages, which are viruses that infect bacteria, by combining antibody genes with a coat protein gene of the phage.
As a result of this genetic manipulation, the phage exhibits the antibody on its surface while retaining the antibody gene inside the bacteriophage. This connection between genotype and phenotype enables the identification of antibodies that interact with specific antigens by screening the displayed phages against these antigens. This process, akin to natural selection and called in vitro selection, facilitates the screening and amplification of extensive antibody libraries.
The first step in creating an antibody phage display library involves incorporating antibody variable region genes into a phage display vector. This process starts by extracting mRNA from B-cells obtained from an animal or human patient followed by reverse transcribing the mRNA into cDNA. Through PCR amplification, the variable regions of both the heavy and light chains of each antibody are generated using the antibody cDNA as a template.
Following amplification, 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.
Subsequently, the library can be subjected to screening against a specific target antigen to detect phages that exhibit antibodies capable of binding to the target. The phages that successfully bind to the target can be isolated, allowing for the elution of bound phages. By sequencing the DNA encoding the antibody from these phages, the desired antibody can be produced for further examination or therapeutic applications.
A naive antibody phage display library is generated by incorporating genes from an organism that has not encountered the specific antigen of interest. On the other hand, an immune antibody phage display library is created by incorporating genes from an organism that has been immunized with the specific antigen of interest.
Naive libraries encompass a broad assortment of antibodies that have not undergone selection driven by antigens. This characteristic enhances the potential for discovering novel antibodies with distinctive binding properties. In contrast, immune libraries consist of antibodies that have undergone selection based on their capacity to bind the specific antigen of interest. These libraries prove valuable for swiftly identifying antibodies with high affinity.
The primary distinction between naive and immune antibody phage display libraries lies in the origin of the genes utilized in their construction. Naive libraries consist of a wide range of antibodies that have not encountered the antigen of interest, whereas immune libraries comprise antibodies specifically chosen for their capability to bind to 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:
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:
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.
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