Unlocking The Potential of IGHV1-45 as A Drug Target Or Biomarker

Target Name: IGHV1-45

NCBI ID: G28466

Other Name(s): Immunoglobulin heavy variable 1-45 | immunoglobulin heavy variable 1-45 | IGHV145 | VH

Unlocking The Potential of IGHV1-45 as A Drug Target Or Biomarker

IGHV1-45, also known as human IgG variable region fragment 1-45, is a single-chain protein that is found in the bloodstreams of humans. It is a type of immunoglobulin, which is a protein that is produced by the immune system to help fight off infections and other harmful substances that enter the body.

One of the things that makes IGHV1-45 an interesting drug target or biomarker is its structure. IGHV1-45 is made up of four constant genes, which are the same for all forms of human IgG. However, it has a variable region that is made up of 158 amino acids. This variable region is the part of the protein that is unique and allows IGHV1-45 to have different functions depending on the context in which it is found.

One of the functions of IGHV1-45 is as a receptor for antibodies. Antibodies are proteins that are produced by the immune system to help identify and neutralize foreign substances like viruses and bacteria. When an antibody binds to IGHV1-45, it can cause the protein to change shape and become more active. This allows IGHV1-45 to interact with the antibodies and help them to do their job more effectively.

Another function of IGHV1-45 is as a signaling molecule. IGHV1-45 can stimulate the activity of other proteins in the immune system, which can help to coordinate the immune response. This is important because when the immune system is triggered, it can cause a range of symptoms and reactions. By stimulating the activity of other proteins, IGHV1-45 can help to keep the immune response under control and avoid unnecessary reactions.

IGHV1-45 has also been shown to have potential as a biomarker for certain diseases. For example, some studies have suggested that IGHV1-45 may be a potential biomarker for multiple sclerosis, an autoimmune disorder that affects the central nervous system. In these studies, IGHV1-45 levels have been found to be elevated in individuals with multiple sclerosis, which suggests that it may be a useful diagnostic or predictive marker for this disease.

In addition to its potential as a drug target or biomarker, IGHV1-45 is also of interest to researchers because of its structure. The variable region of IGHV1-45 is made up of a series of unique amino acids, which makes it a useful study object for researchers. Researchers have been able to use various techniques, such as mass spectrometry, to analyze the structure of IGHV1-45 and understand its underlying mechanisms.

Overall, IGHV1-45 is a fascinating protein that has potential as a drug target or biomarker. Its unique structure and ability to stimulate the immune system make it an interesting study object for researchers, and its potential as a biomarker for certain diseases makes it a promising tool for the field of immunology. Further research is needed to fully understand the functions and potential of IGHV1-45, but it is clear that it is an important protein that has the potential to contribute to a wide range of scientific research.

Protein Name: Immunoglobulin Heavy Variable 1-45

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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