Discovering The Fascinating IGHV3-38 Protein (G28429)

Target Name: IGHV3-38

NCBI ID: G28429

Other Name(s): immunoglobulin heavy variable 3-38 (non-functional) | IGHV338 | VH | Immunoglobulin heavy variable 3-38 (non-functional)

Discovering The Fascinating IGHV3-38 Protein

IGHV3-38, also known as immunoglobulin heavy variable 3-38 (non-functional), is a protein that is expressed in many tissues of the body, including the liver, spleen, and Peyer's patches in the gut. It is a type of immunoglobulin, which is a protein that is made by the immune system to help fight off infections and other harmful substances that enter the body.

One of the things that makes IGHV3-38 so interesting as a drug target is its unique structure. IGHV3-38 is made up of four polypeptide chains that are held together by disulfide bonds. These chains are arranged in a specific pattern, which is called a disulfide-rich region. This unique structure allows IGHV3-38 to have a number of different functions in the immune system.

One of the key functions of IGHV3-38 is its role in the formation of antibodies. Antibodies are proteins that are made by the immune system to help identify and fight off foreign substances like viruses and bacteria. IGHV3-38 is one of the proteins that is involved in this process. It helps to stimulate the production of antibodies by the B cells, which are a type of immune cell that is responsible for making antibodies.

Another important function of IGHV3-38 is its role in the regulation of the immune response. IGHV3-38 helps to keep the immune system in check by preventing it from becoming too active. This is important because when the immune system becomes too active, it can cause problems, such as inflammation and autoimmune diseases.

IGHV3-38 is also interesting as a potential biomarker for certain diseases. For example, studies have shown that IGHV3-38 levels are often elevated in people with multiple sclerosis, a progressive neurodegenerative disease. This suggests that IGHV3-38 may be a useful biomarker for tracking the progress of this disease.

In addition to its role in the immune system, IGHV3-38 is also interesting as a potential drug target. Because it has a unique structure and is involved in the formation of antibodies, it may be possible to develop new treatments for a variety of diseases by targeting IGHV3-38. For example, researchers are currently working on developing new treatments for cancer by targeting IGHV3-38.

Overall, IGHV3-38 is a fascinating protein that is involved in many different functions in the immune system. Its unique structure and ability to stimulate the production of antibodies make it an attractive target for new treatments. As more research is done on IGHV3-38, it is likely to become a valuable tool for the treatment of a wide range of diseases.

Protein Name: Immunoglobulin Heavy Variable 3-38 (non-functional)

Functions: Probable non-functional open reading frame (ORF) of V region of the variable domain of immunoglobulin heavy chains (PubMed:24600447). Non-functional ORF generally cannot participate in the synthesis of a productive immunoglobulin chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level) (PubMed:9619395). 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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