IGHV3-64: The Potential Drug Target and Biomarker (G28414)

Target Name: IGHV3-64

NCBI ID: G28414

IGHV3-64

Other Name(s): Immunoglobulin heavy variable 3-64 | immunoglobulin heavy variable 3-64 | IGHV364 | VH

IGHV3-64: The Potential Drug Target and Biomarker

Immunoglobulin heavy variable 3-64 (IGHV3-64) is a human monoclonal antibody that is derived from a single clone of B cells. It is one of the immunoglobulin genes that encode the heavy chains of antibodies, which are responsible for providing the antibody's effector functions, such as complement fixation, neutralization response, and mucosal immunity. IGHV3-64 has been identified as a potential drug target and biomarker for various diseases, including autoimmune disorders, cancer, and infectious diseases.

IGHV3-64 is a glycoprotein that consists of two heavy chains and an light chain. The heavy chains contain four constant (C) regions and one variable (V) region, while the light chain contains one variable (V) region and one constant ( C) region. IGHV3-64 has a molecular weight of approximately 180 kDa and a monomeric structure.

IGHV3-64 has been shown to play a critical role in various physiological processes, including immune responses, inflammation, and tissue repair. It is expressed in a variety of tissues and cells, including spleen, lymph nodes, bone marrow, and various immune cells , including B cells, natural killer cells, and dendritic cells. IGHV3-64 has also been shown to play a role in immune surveillance against infections, including both cellular and adaptive immunity.

As a potential drug target, IGHV3-64 has been identified with several unique features. Firstly, it is a monoclonal antibody, which means that it is produced from a single clone of B cells. This allows for a high degree of purity and consistency in its production, which is important for developing effective therapeutics. Secondly, IGHV3-64 has a long terminal variable region, which allows for the production of different isotypes of the antibody. This is important for ensuring that the antibodies have the desired effector functions, such as complement fixation or neutralization reaction. Finally, IGHV3-64 has a variable region that is involved in its antigen recognition, which is important for triggering an immune response.

In addition to its potential drug-targeting properties, IGHV3-64 has also been identified as a potential biomarker for various diseases. For example, IGHV3-64 has been shown to be elevated in the blood of patients with various autoimmune disorders, including rheumatoid arthritis , lupus, and multiple sclerosis. This suggests that IGHV3-64 may be a useful biomarker for these disorders. IGHV3-64 has also been shown to be elevated in the blood of patients with various cancers, including breast, lung, and ovarian cancer. This suggests that IGHV3-64 may be a useful biomarker for these cancers as well.

Another potential application of IGHV3-64 is its use as an immunotherapy. IGHV3-64 has been shown to be able to induce both antibody production and T-cell proliferation in primary cultures. This suggests that IGHV3-64 may be a useful immunotherapy for a variety of diseases, including autoimmune disorders and cancer. IGHV3-64 has also been shown to be able to effectively neutralize toxins in various cellular models, which suggests that it may be a useful agent for treating diseases where inflammation is involved.

In conclusion, IGHV3-64 is a unique and promising protein that has the potential to be a drug target and biomarker for a variety of diseases. Its monoclonal nature, long terminal variable region, and variable region make it an attractive candidate for development as a new immunotherapy. Further studies are needed to fully understand its potential applications in these fields.

Protein Name: Immunoglobulin Heavy Variable 3-64

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 "IGHV3-64 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 IGHV3-64 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;
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•   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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