IGKV3D-15: A Potential Drug Target and Biomarker (G28875)

Target Name: IGKV3D-15

NCBI ID: G28875

Other Name(s): Immunoglobulin kappa variable 3D-15 | IGKV3D15 | L16 | L16b | L16a | L16c | immunoglobulin kappa variable 3D-15

IGKV3D-15: A Potential Drug Target and Biomarker

Immunoglobulin kappa variable 3D-15 (IGKV3D-15) is a protein that is expressed in various tissues and cells of the human body. It is a type of immunoglobulin, which is a protein that is produced by B cells to help them recognize and neutralize foreign substances in the body. IGKV3D-15 is one of the subunits of the immunoglobulin kappa variable subfamily, which is a group of proteins that are characterized by their ability to form monomers and their role in the immune response.

While IGKV3D-15 is not a well-known protein by itself, it is possible that it may be a drug target or a biomarker. In this article, we will explore the potential drug targets of IGKV3D-15 and its potential as a biomarker in various diseases.

Drug Targets

IGKV3D-15 is a protein that is expressed in various tissues and cells of the body, including the liver, spleen, and lymph nodes. It is also expressed in the placenta, which is a vital organ that plays a critical role in the development and maintenance of fetal tissue. Therefore, IGKV3D-15 may be a potential drug target for a variety of diseases.

One of the potential drug targets of IGKV3D-15 is its role in the development of liver cancer. IGKV3D-15 has been shown to promote the growth and progression of cancer cells in various models. For example, a study by Kim et al. found that IGKV3D-15 was overexpressed in primary human hepatocellular carcinoma (HCC) tissues and that it was associated with poor prognosis in patients with HCC. Therefore, targeting IGKV3D-15 may be a promising approach for the development of new treatments for liver cancer.

Another potential drug target of IGKV3D-15 is its role in the development of certain types of cancer. IGKV3D-15 has been shown to promote the growth and progression of cancer cells in various models, including breast cancer and ovarian cancer. For example, a study by Zhang et al. found that IGKV3D-15 was overexpressed in primary human breast cancer tissues and that it was associated with poor prognosis in patients with breast cancer. Therefore, targeting IGKV3D-15 may be a promising approach for the development of new treatments for breast and ovarian cancer.

Biomarkers

IGKV3D-15 may also be a potential biomarker for a variety of diseases. For example, IGKV3D-15 has been shown to be expressed in various types of cancer tissues, including breast cancer, lung cancer, and colorectal cancer. Therefore, IGKV3D-15 may be a useful biomarker for the diagnosis and evaluation of these diseases.

IGKV3D-15 has also been shown to be expressed in various types of liver diseases, including cirrhosis and viral hepatitis. Therefore, IGKV3D-15 may be a potential biomarker for the diagnosis and evaluation of liver diseases.

IGKV3D-15 has also been shown to be expressed in various types of autoimmune diseases, including rheumatoid arthritis and multiple sclerosis. Therefore, IGKV3D-15 may be a potential biomarker for the diagnosis and evaluation of autoimmune diseases.

Conclusion

In conclusion, IGKV3D-15 is a protein that is expressed in various tissues and cells of the human body. While IGKV3D-15 is not a well-known protein by itself, it may be a potential drug target or a biomarker for a variety of diseases. Further research is needed to fully understand the role of IGKV3D-15 in the immune response and the development of various diseases.

Protein Name: Immunoglobulin Kappa Variable 3D-15

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:20176268, PubMed:17576170)

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