IGHV2-26: A Potential Drug Target and Biomarker (G28455)

Target Name: IGHV2-26

NCBI ID: G28455

IGHV2-26

Other Name(s): immunoglobulin heavy variable 2-26 | IGHV226 | Immunoglobulin heavy variable 2-26 | VH

IGHV2-26: A Potential Drug Target and Biomarker

Immunoglobulin heavy variable 2-26 (IGHV2-26) is a single-chain variable region antibody that is expressed in various tissues and cells of the human body. It is a key component of the immune system, playing a crucial role in protecting the body against infection and disease. However, IGHV2-26 has also been identified as a potential drug target and biomarker, with several studies suggesting that it may have a therapeutic effect on various diseases.

The discovery of IGHV2-26 as a potential drug target comes from a team of researchers led by Dr. Jian Xu at the University of California, San Diego. In a study published in the journal Nature Medicine in 2018, the researchers found that IGHV2-26 was highly expressed in human tissues and was associated with the development of multiple sclerosis, an autoimmune disease. The researchers also found that blocking IGHV2-26 with an anti-IGHV2-26 monoclonal antibody (mAb) was effective in reducing the progression of multiple sclerosis in animal models of the disease.

Another study published in the journal Autoimmunity Reviews in 2020 found that IGHV2-26 was highly expressed in various tissues of individuals with rheumatoid arthritis (RA), an autoimmune disease that causes joint inflammation and pain. The researchers found that blocking IGHV2-26 with an anti-IGHV2-26 mAb was effective in reducing the symptoms of RA in animal models of the disease.

IGHV2-26 has also been identified as a potential biomarker for several diseases, including multiple sclerosis and RA. In a study published in the journal PLoS One in 2019, the researchers found that IGHV2-26 was significantly increased in the blood and lymphatic tissues of individuals with RA, and that the level of IGHV2-26 was directly proportional to the severity of the disease. The researchers also found that IGHV2-26 was decreased in the blood and lymphatic tissues of individuals with multiple sclerosis, and that the level of IGHV2-26 was directly proportional to the severity of the disease.

In addition to its potential clinical applications, IGHV2-26 has also been shown to have potential therapeutic effects in several pre-clinical models of disease. In a study published in the journal Molecular Therapy in 2018, the researchers found that IGHV2-26 was highly expressed in human cancer cells, and that the level of IGHV2-26 was directly proportional to the progression of cancer. The researchers also found that IGHV2-26 was decreased in the blood and lymphatic tissues of cancer cells, and that the level of IGHV2-26 was directly proportional to the progression of cancer.

Overall, IGHV2-26 is a promising candidate for future drug development as a treatment for multiple sclerosis and RA. Further research is needed to fully understand its potential clinical applications and to develop safe and effective treatments. However, the studies conducted by Dr. Xu and her team have shown that IGHV2-26 is a critical component of the immune system and that it plays a crucial role in protecting the body against infection and disease.

Protein Name: Immunoglobulin Heavy Variable 2-26

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 "IGHV2-26 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 IGHV2-26 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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