Understanding IGHV1-58: An Antibody That Plays A Role in The Immune Response

Target Name: IGHV1-58

NCBI ID: G28464

IGHV1-58

Other Name(s): immunoglobulin heavy variable 1-58 | Immunoglobulin heavy variable 1-58 | IGHV158 | VH

Understanding IGHV1-58: An Antibody That Plays A Role in The Immune Response

IGHV1-58, also known as immunoglobulin heavy variable 1-58 (IgHV1-58), is a type of antibody that is produced by B cells in the human body. It is one of the proteins that make up the immunoglobulin molecule, which is the main component of antibodies. This protein is found in the blood, lymph nodes, spleen, and Peyer's patches of the gut.

IGHV1-58 is a single chain protein that consists of 58 amino acids. It has a molecular weight of 180 kDa and a pre-fusion width of 12.5 kDa. The protein has a monomeric structure and is made up of two heavy chains and two light chains. The heavy chains contain four constant (C) regions and one variable (V) region, while the light chains contain one variable (V) region and one constant (C) region.

IGHV1-58 is a type of immunoglobulin heavy variable protein (IgHV1-58), which is one of the five subclasses of antibodies based on their variable region. The other subclasses include IgG, IgM, IgA, IgE, and IgD. These antibodies have different functions in the immune system, depending on the specific subclass.

IGHV1-58 is produced by B cells in response to the presence of foreign antigens, such as bacteria, viruses, or other substances that the body recognizes as foreign. When an antigen binds to a B cell, it stimulates the B cell to undergo a process called clonal expansion and differentiate into an antibody-secreting plasma cell. During this process, the B cell produces a single class of antibody, which is specific for the antigen.

IGHV1-58 is one of the proteins that are involved in the immune response to infections. It is part of the complement system, which is a group of proteins that work together to help the immune system recognize and respond to infections. When an infection is detected, the immune system produces antibodies to fight it off. These antibodies include IGHV1-58, which work together with other antibodies in the complement system to help destroy the infection.

In addition to its role in the immune response, IGHV1-58 has also been shown to have potential as a drug target. Researchers are interested in using it as a biomarker for certain types of cancer, as well as for monitoring the effectiveness of certain treatments . This is because IGHV1-58 has been shown to be expressed in a variety of tissues and cells, including cancer cells, which makes it a potential target for cancer therapies.

IGHV1-58 has also been shown to have potential as a therapeutic agent for a variety of autoimmune diseases, such as rheumatoid arthritis, lupus, and multiple sclerosis. These diseases are characterized by the immune system attacking the body's own tissues, and IGHV1-58 has been shown to play a role in this process.

In addition to its potential as a drug target and biomarker, IGHV1-58 is also of interest to researchers because of its structure and function. Studying IGHV1-58 has helped researchers gain insights into the immune system and how it works. This can provide valuable information for the development of new treatments and therapies.

Overall, IGHV1-58 is a protein that is produced by B cells in response to the presence of foreign antigens. It is a part of the complement system and has been shown to play a role in the immune response to infections and cancer. In addition , IGHV1-58 has also been shown to have potential as a drug target and biomarker for a variety of autoimmune diseases. Further research is needed to fully understand its role and potential in these areas.

Protein Name: Immunoglobulin Heavy Variable 1-58

Functions: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:20176268, PubMed:17576170)

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