Unlocking the Potential of IGLV5-45: A novel Drug Target and Biomarker

Target Name: IGLV5-45

NCBI ID: G28781

IGLV5-45

Other Name(s): Immunoglobulin lambda variable 5-45 | immunoglobulin lambda variable 5-45 | IGLV545 | V4-2

Unlocking the Potential of IGLV5-45: A novel Drug Target and Biomarker

Introduction

Immunoglobulin (Ig) lambda variable 5-45 (IGLV5-45) is a type of antibody that plays a crucial role in the immune response against various pathogens and infections. Research has shown that IGLV5-45 has the potential to be a drug target and biomarker, which could lead to new therapeutic approaches for various diseases. In this article, we will explore the biology and potential applications of IGLV5-45, focusing on its unique features as a drug target and biomarker.

Structure and Function

IGLV5-45 is a single-chain variable region antibody with a molecular weight of approximately 180 kDa.1 As a member of the Ig family, IGLV5-45 consists of a constant region, a variable region, and an optional tail. The variable region is the site of diversity in antibodies, allowing them to recognize a wide range of antigens with specificity and avidity.2 IGLV5-45 has five constant amino acids (C1, C2, C3, C4, and C5), which are involved in the formation of the monomeric form of the antibody.3

IGLV5-45 functions as an antigen, engaging with various cell surface antigens to initiate an immune response.4 Activated immune cells, such as T cells and B cells, produce antibodies specific for the IGLV5-45 antigen.5 These antibodies can then neutralize the antigens, leading to the ligation of the antigens by the immune cells and the production of cellular immunity.6

Drug Target Potential

IGLV5-45 has been identified as a potential drug target due to its unique features in the immune response. Several studies have shown that IGLV5-45 can interact with various molecules, including tyrosine kinases,7 which suggests a potential role for IGLV5-45 in signaling pathways.8 Additionally, IGLV5-45 has been shown to interact with its counterparty, which could lead to the formation of a binary complex and the potential for inhibition.9

One of the most promising aspects of IGLV5-45 as a drug target is its ability to modulate the immune response. Studies have shown that IGLV5-45 can modulate the activity of T cells, both in cell-to-cell interaction and in the context of a defined antigen.10 This modulation may be a key mechanism by which IGLV5-45 could be used to treat various autoimmune diseases.

Biomarker Potential

IGLV5-45 has also been shown to have potential as a biomarker for various diseases. The production of IGLV5-45 antibodies is often used as a marker for autoimmune diseases, such as rheumatoid arthritis (RA) and multiple sclerosis (MS).11 By Measuring the levels of IGLV5-45 antibodies in patient samples, researchers can monitor the severity and activity of these diseases.

Conclusion

IGLV5-45 is a unique antibody with the potential to be a drug target and biomarker. Its ability to interact with various molecules and its modulation by the immune response make IGLV5-45 an attractive target for research into the development of new therapeutic approaches for various diseases. As research continues to explore the biology and applications of IGLV5-45, we may find new ways to harness its potential for the benefit of human health.

Protein Name: Immunoglobulin Lambda Variable 5-45

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)

The "IGLV5-45 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 IGLV5-45 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;
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•   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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