Unlocking the Potential of IGLV3-10 as a Drug Target and Biomarker

Target Name: IGLV3-10

NCBI ID: G28803

IGLV3-10

Other Name(s): Immunoglobulin lambda variable 3-10 | IGLV310 | V2-7 | immunoglobulin lambda variable 3-10

Unlocking the Potential of IGLV3-10 as a Drug Target and Biomarker

Immunoglobulin (Ig) lambda variable 3-10 (IGLV3-10) is a type of antibody that plays a crucial role in the immune response against various pathogens. It is a glycoprotein that consists of five constant (C) regions and one variable (V) region. The IGLV3-10 molecule has been identified as a potential drug target and biomarker due to its unique structure and various biochemical properties.

Structure and Function

The IGLV3-10 molecule has a monomeric structure with a calculated molecular weight of approximately 180 kDa. It consists of a variable region that contains two constant regions: a first constant region (C1) and a second constant region (C2), and a variable region (V) that contains a unique constant domain (C3) and a variable domain (C4). The variable region is the site of interest for drug development as it contains the potential for drug binding.

One of the unique features of IGLV3-10 is its variable region, which is composed of a single constant domain (C3) and a variable domain (C4) that is responsible for the variable region's diverse functions. The C3 domain is known for its ability to form aggregates, which can enhance the activity of the antibody. The C4 domain is involved in the stability and modification of the antibody, and has been shown to play a role in the regulation of cellular processes.

IGLV3-10 has been shown to have various biochemical properties that make it an attractive drug target. For instance, it has a high avidity for its target protein, which means it can efficiently bind to and cleave the target protein. Additionally, IGLV3-10 has a long half-life, which allows for consistent drug administration and provides an opportunity for long-term therapy.

Drug Development

Several drugs have been developed to target IGLV3-10, including small molecules, antibodies, and chimeric antibodies. One of the most promising strategies is the use of small molecules that can modulate the activity of IGLV3-10. For instance, inhibitors of the C3 domain have been shown to reduce the activity of IGLV3-10, suggesting that this domain may be a promising target for small molecules. Similarly, antibodies that recognize and bind to the IGLV3-10 variable region have been developed. These antibodies have the potential to enhance the activity of IGLV3-10 and could be used for various applications, including cancer diagnosis and treatment.

Another approach to drug development is the use of chimeric antibodies, which are antibodies that contain all the characteristics of an individual antibody, but with modified or mutated regions. Chimeric antibodies have the potential to provide a more targeted and effective treatment than small molecules or antibodies. For instance, a chimeric antibody that recognizes and binds to IGLV3-10 has been developed and is currently in clinical trials.

Conclusion

IGLV3-10 is a unique molecule that has been identified as a potential drug target and biomarker. Its unique structure and various biochemical properties make it an attractive target for small molecules, antibodies, and chimeric antibodies. As research continues to advance, we can expect to see new and innovative treatments for various diseases that target IGLV3-10.

Protein Name: Immunoglobulin Lambda Variable 3-10

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 "IGLV3-10 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 IGLV3-10 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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