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Updated: May 24, 2025

Analyzing Tumor and Tissue Distribution of Target Antigen Specific Therapeutic Antibody
Published on: May 16, 2020
Design, Production, and Optimization of Antigen-Specific Recombinant Antitumor Dimeric IgA Antibody
Baishali Tamuli1, Rutik Ghagare2, Gunjan Mandal3
1Cancer Immune Environment and Therapeutics Lab, Tumor Immunology and Immunotherapy, Advanced Centre for Treatment, Research and Education in Cancer (ACTREC), Tata Memorial Centre, Navi Mumbai, India.
Abstract:
Available cancer immunotherapies are currently restricted to extracellular targets, while chemotherapy is the only option for intracellular targets, such as mutant KRAS. Antibodies are serum immunoglobulins, each having high binding specificity against particular antigens. Patients produce antibody responses against abnormally expressed self-proteins and neoantigens presented by the cancer cells. However, despite their infiltration into the tumor beds, many times the magnitude of the antitumor antibodies produced by spontaneously infiltrated B lymphocytes remains insufficient to control tumor growth. Recent work has established that dimeric IgA antibodies can target intracellular targets inside cancer cells expressing the polymeric immunoglobulin receptor (pIgR). Here, we thoroughly discuss the entire process of recombinant production of intracellular antigen-specific dimeric IgA antibodies that could be utilized for targeting oncodrivers inside tumor cells.
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Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure and Classes
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.

