IGLV3-16: A Potential Drug Target and Biomarker (G28799)

Target Name: IGLV3-16

NCBI ID: G28799

IGLV3-16

Other Name(s): IGLV316 | immunoglobulin lambda variable 3-16 | V2-11 | Immunoglobulin lambda variable 3-16

IGLV3-16: A Potential Drug Target and Biomarker

IGLV3-16 (Immunogenic Growth Factor-VIII) is a single-chain fragment of the immunoglobulin gene, which is expressed in various tissues and organs, including the liver, spleen, and lymph nodes. IGLV3-16 has been identified as a potential drug target and biomarker due to its unique structure and expression patterns. In this article, we will discuss the IGLV3-16 molecule, its potential drug targeting properties, and its potential as a biomarker for various diseases.

Structure and Expression

The IGLV3-16 molecule is a single-chain fragment that contains 16 constant and 2 variable regions. It has a molecular weight of approximately 180 kDa and a calculated pI of 7.9. IGLV3-16 is expressed in various tissues and organs, including the liver, spleen, and lymph nodes. The expression of IGLV3-16 has been shown to be dependent on the immune response, which suggests that it plays a role in the immune system.

Drug Targeting

IGLV3-16 has been identified as a potential drug target due to its unique structure and expression patterns. IGLV3-16 has a unique N-terminus that contains a putative transmembrane domain and a unique C-terminus that contains a conserved Asp-Glu-Pro-Asn-Asp loop. This unique structure suggests that IGLV3-16 may have unique interactions with intracellular signaling pathways and proteins. Additionally, IGLV3-16 has been shown to interact with several protein partners, including the transcription factor, NF-kappa-B, and the protein kinase, MAPK. These interactions suggest that IGLV3-16 may play a role in the regulation of cellular processes, including inflammation and immune response.

IGLV3-16 has also been shown to have a unique expression pattern. IGLV3-16 is primarily expressed in the liver and spleen, and its expression is highly dependent on the immune response. This suggests that IGLV3-16 may play a role in the immune response and may be a useful biomarker for evaluating the effectiveness of immunomodulatory drugs.

Biomarker Potential

IGLV3-16 has been identified as a potential biomarker for various diseases due to its unique expression pattern and structure. IGLV3-16 has been shown to be expressed in a variety of tissues and organs, including the liver, spleen, and lymph nodes, which suggests that it may be a useful biomarker for evaluating the effectiveness of drugs targeting these tissues. Additionally, IGLV3-16's unique structure and expression patterns may make it a useful target for small molecules with unique interactions with IGLV3-16.

Conclusion

IGLV3-16 is a unique molecule that has been identified as a potential drug target and biomarker. Its unique structure and expression patterns suggest that IGLV3-16 may play a role in the regulation of cellular processes, including inflammation and immune response. Further research is needed to fully understand the potential of IGLV3-16 as a drug target and biomarker.

Protein Name: Immunoglobulin Lambda Variable 3-16

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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•   general information;
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•   expression level;
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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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