Detection of Antibody

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1. Sandwich ELISA

Sandwich ELISA 실험 기법을 이용하여 분비된 antibody를 정량 및 정성 분석한다. Simulator로 α-IgM만 있는 condition, LPS만 있는 condition, α-IgM과 α-CD40이 있는 condition, 그리고 α-IgM과 α-CD40와 IL-4이 있는 condition에서 B cell을 culture한 후, 각 condition에서 어떤 isotype의 antibody가 얼만큼 분비되었는지 분석한다.
2. Antibody Structure

Antibody는 B cell이 생산한 immunoglobulin glycoprotein으로, antigen의 epitope 부분과 specific한 binding을 할 수 있다. 이들은 molecular weight가 더 작은 두 개의 light chain과 molecular weight가 더 큰 두 개의 heavy chain이 disulfide bond으로 연결되어 Y-shape를 이룬다. Y-shape의 양쪽 끝은 variable region으로, light chain과 heavy chain의 N-말단이 다양한 아미노산 sequence으로 이루어져 있어 그에 맞는 specific한 antigen과 결합한다. 그 외의 부분은 constant region으로, variable region과는 달리 아미노산 sequence가 고정되어 있다.
3. B Cell Activation

이를 통해 B cell activation과 class switching의 과정, humoral response,그리고 TI/TD antigen의 차이 등을이해한다.

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1. Sandwich ELISA

Sandwich ELISA is a widely used immunoassay technique that allows for the sensitive and specific detection and quantification of target analytes in complex biological samples. The key advantage of this method is its ability to capture the target analyte between two antibodies, providing a sandwich-like structure that enhances the specificity and sensitivity of the assay. The first antibody, known as the capture antibody, is immobilized on a solid support, such as a microtiter plate, and binds to the target analyte. The second antibody, called the detection antibody, is labeled with a reporter molecule, such as an enzyme or fluorescent dye, and binds to a different epitope on the target analyte. This sandwich configuration effectively captures the target analyte between the two antibodies, allowing for its accurate detection and quantification. Sandwich ELISA is particularly useful for the analysis of proteins, peptides, and other macromolecules, and has found widespread applications in various fields, including clinical diagnostics, drug discovery, and environmental monitoring. The technique's high sensitivity, specificity, and ease of use have made it an indispensable tool in modern analytical and biomedical research.
2. Antibody Structure

Antibodies are complex and highly versatile proteins that play a crucial role in the adaptive immune response. Their unique structure allows them to recognize and bind to a vast array of foreign molecules, known as antigens, with remarkable specificity. The basic structure of an antibody consists of two heavy chains and two light chains, which are held together by disulfide bonds and non-covalent interactions. The variable regions of the heavy and light chains form the antigen-binding site, which is responsible for recognizing and binding to the target antigen. The constant regions of the heavy chains, on the other hand, are responsible for effector functions, such as activating the complement system or recruiting other immune cells. This modular structure of antibodies allows for a high degree of diversity and flexibility, enabling the immune system to mount a tailored response to a wide range of pathogens and foreign substances. Understanding the intricate structure of antibodies has been crucial in the development of various therapeutic and diagnostic applications, including monoclonal antibodies, antibody-drug conjugates, and immunoassays. Continued research in this field promises to further expand our understanding of the immune system and lead to the development of more effective and targeted therapies.
3. B Cell Activation

B cell activation is a critical process in the adaptive immune response, as it leads to the production of antibodies that can neutralize or eliminate foreign pathogens. The activation of B cells involves a complex series of events that are triggered by the recognition of an antigen by the B cell receptor (BCR). When a naive B cell encounters an antigen that binds to its BCR, it becomes activated and undergoes a series of changes that ultimately lead to the production of antibody-secreting plasma cells and memory B cells. The initial activation of a B cell requires two signals: the first signal is provided by the binding of the antigen to the BCR, and the second signal is provided by co-stimulatory molecules expressed on the surface of antigen-presenting cells, such as T cells or dendritic cells. These co-stimulatory signals are essential for the full activation of the B cell and the initiation of the downstream signaling cascades that lead to proliferation, differentiation, and antibody production. Once activated, B cells can undergo further differentiation into plasma cells, which are specialized for the production and secretion of large quantities of antibodies, or memory B cells, which can rapidly respond to subsequent encounters with the same antigen. The ability of B cells to generate a diverse repertoire of antibodies and to maintain long-term memory of past infections is a crucial component of the adaptive immune response, and understanding the mechanisms of B cell activation is essential for the development of effective vaccines and immunotherapies.

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