Promising Cancer Treatment: IGLV8-61 (G28774)

Target Name: IGLV8-61

NCBI ID: G28774

Other Name(s): IGLV861 | Immunoglobulin lambda variable 8-61 | V3-4 | immunoglobulin lambda variable 8-61

Promising Cancer Treatment: IGLV8-61

IGLV8-61 (also known as IGLV861) is a drug candidate that is being developed for the treatment of various diseases, including cancer. It is a small non-coding RNA (ncRNA) that has been shown to have a variety of functions in both humans and animals.

One of the most promising aspects of IGLV8-61 is its ability to targets cancer cells. Cancer is a leading cause of death worldwide, and there is a high demand for new treatments that can effectively target this deadly disease. IGLV8-61 has been shown to be effective in preclinical studies against several types of cancer, including breast, lung, and ovarian cancer.

In addition to its potential as a cancer treatment, IGLV8-61 has also been shown to have a variety of other potential applications. For example, it has been shown to have anti-inflammatory effects, which can be useful in treating a variety of conditions such as autoimmune diseases and chronic obstructive pulmonary disease (COPD).

IGLV8-61 is also a potential biomarker for several types of cancer. By measuring the levels of IGLV8-61 in cancer cells, doctors can monitor the effectiveness of different treatments and identify potential biomarkers for cancer. This can help improve the overall treatment of cancer patients.

While IGLV8-61 is still in the early stages of development, it has already shown promise in preclinical studies. In addition, there is ongoing research to investigate its potential uses in human clinical trials.

Overall, IGLV8-61 is a promising drug candidate that has the potential to treat a variety of diseases, including cancer. With further research, it could become a valuable tool for the treatment of these deadly diseases.

Protein Name: Immunoglobulin Lambda Variable 8-61

Functions: V region of the variable domain of immunoglobulin light 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:20176268, PubMed:22158414). 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:17576170, PubMed:20176268)

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