IGKV2-30: A Potential Drug Target and Biomarker (G28919)

Target Name: IGKV2-30

NCBI ID: G28919

Other Name(s): IGKV230 | Immunoglobulin kappa variable 2-30 | immunoglobulin kappa variable 2-30 | A17

IGKV2-30: A Potential Drug Target and Biomarker

Introduction

The IGKV2-30 protein is a member of the IGK family, which is known for its role in various cellular processes such as intracellular signaling, inflammation, and stress responses. The IGKV2-30 protein has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

Potential Drug Target

The IGKV2-30 protein is a potential drug target because of its unique structure and function. It has four transmembrane domains, which give it a unique structure that allows it to interact with various signaling molecules, including tyrosines, serines, and thalasins. Additionally, the IGKV2-30 protein has a high degree of homogeneity, which suggests that it has a similar function in different cell types.

One of the IGKV2-30 protein's transmembrane domains is known as the N-terminal domain, which contains a unique type of ion channel called the N-type ATP-dependent chloride channel. This channel is involved in the regulation of intracellular signaling, and its function is thought to be related to the regulation of cell proliferation and survival.

IGKV2-30 has also been shown to play a role in the regulation of inflammation and stress responses. It has been shown to interact with various signaling molecules, including nuclear factor kappa B (NF-kappa-B), which is a well-known regulator of inflammation and stress responses.

Potential Biomarkers

In addition to its potential as a drug target, IGKV2-30 has also been identified as a potential biomarker for various diseases. For example, IGKV2-30 has been shown to be overexpressed in various cancer types, which suggests that it may be a useful biomarker for cancer diagnosis and treatment.

IGKV2-30 has also been shown to be involved in the regulation of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. It has been shown to interact with various neurotransmitters, including dopamine, which is involved in the regulation of movement and mood.

Additionally, IGKV2-30 has been shown to be involved in the regulation of autoimmune disorders, such as rheumatoid arthritis and type 1 diabetes. It has been shown to interact with various immune cell signaling molecules, including T-cell receptor 4 (TCR- 4), which is involved in the regulation of immune responses.

Conclusion

In conclusion, IGKV2-30 is a protein that has unique structure and function, and has been shown to play a role in various cellular processes, including intracellular signaling, inflammation, and stress responses. Its potential as a drug target and biomarker make it an attractive target for further research and development. Further studies are needed to fully understand its role in various diseases and to develop effective treatments.

Protein Name: Immunoglobulin Kappa Variable 2-30

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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