IGHV1-46: A Key Regulator of The Immune System (G28465)

Target Name: IGHV1-46

NCBI ID: G28465

IGHV1-46

Other Name(s): immunoglobulin heavy variable 1-46 | Immunoglobulin heavy variable 1-46 | IGHV146

IGHV1-46: A Key Regulator of The Immune System

IGHV1-46, also known as human Ighv1-46, is a type of immunoglobulin heavy variable chain protein that is expressed in many tissues throughout the body. It is a glycoprotein that consists of four polypeptide chains, each of which has a different function in the immune system. IGHV1-46 is a key regulator of the immune response and has been identified as a potential drug target in the treatment of various diseases.

The immune system is a critical component of the body that protects it against infection, inflammation, and damage. The immune system is made up of a variety of different types of cells and molecules, including T cells, B cells, natural killer cells, and many others. These cells work together to detect and respond to foreign substances in the body, such as viruses, bacteria, and cancer cells.

One of the key proteins that plays a critical role in the immune system is the immunoglobulin heavy variable chain (IgHV1-46). This protein is made up of four polypeptide chains, each of which has a different function in the immune response. The first chain consists of a variable region that contains the two heavy chains and the light chain. The second chain consists of a constant region that contains a single constant molecule. The third chain consists of a variable region that contains the two heavy chains and the light chain , while the fourth chain consists of a constant region that contains a single constant molecule.

The IGHV1-46 protein is expressed in many tissues throughout the body and plays a critical role in the immune response. It is a key regulator of the complement system, which is a set of proteins that work together to help the immune system respond to foreign substances in the body. The IGHV1-46 protein helps to regulate the activity of the complement system by interacting with the protein CR2 (complement receptor 2).

IGHV1-46 has also been identified as a potential drug target in the treatment of various diseases. For example, studies have shown that IGHV1-46 has been expressed at high levels in the brains of individuals with Alzheimer's disease, which is a degenerative brain disorder that is characterized by the progressive loss of brain cells. Researchers have also shown that IGHV1-46 is highly expressed in the breasts of women with breast cancer, which is a cancer that can be a deadly disease.

In addition to its potential as a drug target, IGHV1-46 has also been shown to have a variety of other biological functions. For example, it is a key regulator of the immune response, and has been shown to play a critical role in the regulation of inflammation in the body. IGHV1-46 has also been shown to play a critical role in the regulation of cell signaling, and has been shown to interact with a variety of different proteins in the body.

Overall, IGHV1-46 is a protein that has a variety of different functions in the immune system and has been identified as a potential drug target in the treatment of various diseases. Further research is needed to fully understand the role of IGHV1-46 in the immune system and its potential as a drug target.

Protein Name: Immunoglobulin Heavy Variable 1-46

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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