IGHV4-30-2: A Potential Drug Target and Biomarker (G28398)

Target Name: IGHV4-30-2

NCBI ID: G28398

IGHV4-30-2

Other Name(s): immunoglobulin heavy variable 4-30-2 | IGHV4302 | IGHV4-3 | Immunoglobulin heavy variable 4-30-2

IGHV4-30-2: A Potential Drug Target and Biomarker

IGHV4-30-2 (Immunoglobulin Heavy Variable 4-30-2) is a protein that is expressed in various tissues of the body, including the liver, spleen, and peripheral blood. It is a type of immunoglobulin, which is a protein that is produced by B cells in response to the presence of foreign substances in the body. There are several different types of immunoglobulins, each with a different function.

IGHV4-30-2 is a type of heavy variable immunoglobulin, which means that it consists of a heavy chain and a light chain. The heavy chain consists of four subunits, while the light chain consists of one subunit. The heavy chain of IGHV4-30-2 consists of the variable regions of the immunoglobulin molecule, which are responsible for the antibody's ability to bind to and neutralize foreign substances.

IGHV4-30-2 has been identified as a potential drug target in several studies. For example, researchers have found that IGHV4-30-2 is highly expressed in various tissues of the brain, and that it is involved in the development and progression of several neurological diseases, including Alzheimer's disease and Parkinson's disease.

Additionally, IGHV4-30-2 has also been shown to be involved in the immune response to infections. For example, studies have found that IGHV4-30-2 is expressed in the immune cells that are responsible for fighting off infections, and that it plays a role in the development of autoimmune diseases.

Despite the potential implications of IGHV4-30-2 as a drug target or biomarker, further research is needed to fully understand its role in the immune system and its potential therapeutic uses.

Protein Name: Immunoglobulin Heavy Variable 4-30-2

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)

The "IGHV4-30-2 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about IGHV4-30-2 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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