Unlocking IGLV4-69: A Novel Drug Target and Biomarker for Autoimmune Disorders

Target Name: IGLV4-69

NCBI ID: G28784

IGLV4-69

Other Name(s): immunoglobulin lambda variable 4-69 | IGLV469 | V5-6 | Immunoglobulin lambda variable 4-69

Unlocking IGLV4-69: A Novel Drug Target and Biomarker for Autoimmune Disorders

Unraveling the Potential Drug Target and Biomarker IGLV4-69: A novel Monoclonal Antibody for the Treatment of Autoimmune Disorders

Abstract:

Autoimmune diseases have a significant impact on millions of people worldwide, leading to chronic inflammation and various health complications. One of the key hallmarks of autoimmune disorders is the production of antibodies that recognize and attack the body's own tissues. In this article, we discuss the research on IGLV4-69, a novel immunoglobulin lambda variable 4-69 fragment that has shown promise in targeting autoimmune diseases. We review the current understanding of IGLV4-69's structure, function, and potential use as a drug target or biomarker.

Introduction:

Autoimmune diseases, such as rheumatoid arthritis (RA), lupus, and multiple sclerosis, are characterized by the production of antibodies that target the body's own tissues. These antibodies, known as autoantibodies, can cause inflammation, pain, and damage to various organs, leading to serious medical consequences. The exact cause of autoimmune diseases is not yet fully understood, but it is thought to involve a complex interplay of genetic and environmental factors.

One potential solution to treating autoimmune disorders is to target specific antibodies that are associated with disease progression. One such approach is to identify biomarkers that can predict the likelihood of disease progression or response to treatment. One such biomarker is IGLV4-69, a novel immunoglobulin lambda variable 4-69 fragment that has shown promise in targeting autoimmune diseases.

Structure and Function of IGLV4-69:

IGLV4-69 is a monoclonal antibody that is derived from the variable region of human IgG antibodies. It consists of 69 amino acid residues and has a molecular weight of approximately 76 kDa. IGLV4-69 has a variable region that includes several unique features, such as a hypervariable loop (HVL) and a constant region that is distinct from other antibodies.

The HVL is a region of the variable region that is highly conserved and is known to play a key role in antibody diversity. IGLV4-69 has an HVL that is similar to that of other IgG antibodies, but it has a longer extension on the left side of the HVL. This longer extension is known as the \"Fc region\" and is responsible for the antibody's strong binding affinity for its target.

IGLV4-69 has also been shown to have a unique function as an autoantibody. In studies using cell-based assays, IGLV4-69 has been shown to cause a strong positive impact on the expression of pro-inflammatory cytokines, such as interleukin-1 (IL-1), interleukin-6 (IL-6), and nuclear factor kappa B (NF-kappa-B), in human immune cells. These cytokines are key drivers of the immune response and have been implicated in the development and progression of autoimmune diseases.

Potential Use as a Drug Target or Biomarker:

The unique function of IGLV4-69 as an autoantibody makes it a promising drug target or biomarker for the treatment of autoimmune diseases. By targeting IGLV4-69 with small molecules or antibodies, it may be possible to reduce the production of pro-inflammatory cytokines and improve the immune response.

In addition to its potential as a drug target, IGLV4-69 may also be used as a biomarker for monitoring disease progression. The HVL region of IGLV4-69 is highly conserved across different antibodies, which suggests that it may be a reliable biomarker for tracking the immune response to an

Protein Name: Immunoglobulin Lambda Variable 4-69

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 "IGLV4-69 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 IGLV4-69 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;
•   related patent analysis;
•   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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