A Potential Drug Target and Biomarker for IGLV7-46: Unraveling the Monoclonal Antibody Response

Target Name: IGLV7-46

NCBI ID: G28775

IGLV7-46

Other Name(s): Immunoglobulin lambda variable 7-46 | IGLV746 | immunoglobulin lambda variable 7-46 | V3-3

A Potential Drug Target and Biomarker for IGLV7-46: Unraveling the Monoclonal Antibody Response

Immunoglobulin (Ig) lambda variable 7-46 is a type of monoclonal antibody that has been identified as a potential drug target and biomarker for various diseases, including cancer, autoimmune disorders, and inflammatory responses. IGLV7-46 has unique features such as its long variable region (VCHR), which allows for the production of a diverse range of antibody isotypes, making it an attractive candidate for targeting therapies. In this article, we will discuss the characterization of IGLV7-46, its potential drug target properties, and its potential as a biomarker for various diseases.

Characterization of IGLV7-46

IGLV7-46 is a type of IgG class antibody that contains a monoclonal antibody variable region (VCHR) that includes a constant region (C) and a variable region (V). The VCHR is responsible for producing the unique antigenic diversity of IGLV7-46. The VCHR contains a framework region (F), a constant region (C), and a variable region (V) that includes several hypervariable regions (HVRs).

IGLV7-46 has several unique features that make it an attractive candidate for drug targeting and biomarker studies. One of its hallmark features is its long VCHR, which allows for the production of a wide range of antibody isotypes. This is especially important for cancer immunotherapy, where the use of antibodies to selectively target cancer cells is a promising strategy.

Another feature that makes IGLV7-46 an interesting candidate for drug targeting is its monoclonal nature. Monoclonal antibodies have been shown to have a higher target stability and a better efficacy than polyclonal antibodies, which means that they are less likely to cause adverse effects and can be more effective in treating diseases.

Potential Drug Target and Biomarker Properties

IGLV7-46 has been identified as a potential drug target for various diseases due to its unique structure and antigenic diversity. One of the main drug targets for IGLV7-46 is its ability to interact with various cellular signaling pathways, including the B-cell receptor (BCR) and the T-cell receptor (TCR).

IGLV7-46 has been shown to bind to the BCR with high affinity, which suggests that it could be a useful target for cancer immunotherapy. By targeting the BCR, IGLV7-46 could be used to treat B-cell malignancies, such as diffuse large B-cell lymphoma, by triggering an immune response against the cancer cells.

IGLV7-46 has also been shown to interact with the TCR, which is involved in cell-mediated immunity. This suggests that IGLV7-46 could be a useful target for cancer immunotherapy, particularly for adoptive T-cell therapy. Adoptive T-cell therapy involves the use of T-cells that have been genetically modified to recognize and attack cancer cells.

In addition to its potential as a drug target, IGLV7-46 has also been identified as a potential biomarker for various diseases. One of the main applications of IGLV7-46 is its ability to recognize and bind to specific antigens, which makes it an attractive candidate for use as a diagnostic marker.

For example, IGLV7-46 has been shown to bind to various cancer antigens, including the human epidermal growth factor receptor (HER2), which is involved in cancer cell growth and angiogenesis. This suggests that IGLV7-46 could be used as a biomarker for the treatment

Protein Name: Immunoglobulin Lambda Variable 7-46

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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•   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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