Unlocking the Potential of IGHV3-30 as a Drug Target and Biomarker

Target Name: IGHV3-30

NCBI ID: G28439

IGHV3-30

Other Name(s): Immunoglobulin heavy variable 3-30 | immunoglobulin heavy variable 3-30 | VH | IGHV330

Unlocking the Potential of IGHV3-30 as a Drug Target and Biomarker

Introduction

Immunoglobulin heavy variable 3-30 (IGHV3-30) is a single-chain antibody that plays a critical role in immune responses and inflammation. It is a highly conserved protein that is expressed in various tissues and cells, including the liver, spleen, and peripheral blood cells. IGHV3-30 has been identified as a potential drug target and biomarker due to its unique structure, stability, and expression pattern.

Structure and Localization

The IGHV3-30 protein is composed of a variable region and a constant region. The variable region consists of a variable domain that includes two immunoglobulin heavy chain alpha chains and two immunoglobulin light chain beta chains. The variable domain is responsible for the recognition of antigens and the formation of immune responses. The constant region consists of a constant region that includes a unique N-terminus, a D-terminus, and a mid-span region.

IGHV3-30 is expressed in various tissues and cells, including the liver, spleen, and peripheral blood cells. It is primarily expressed in the liver, where it plays a critical role in immune surveillance and inflammation. IGHV3-30 has been shown to localize to the endoplasmic reticulum (ER) and to be predominantly expressed in the hepatocytes.

Drug Target Potential

The unique structure and localization of IGHV3-30 make it an attractive drug target. IGHV3-30 has been shown to interact with various drug molecules, including small molecules, peptides, and antibodies. Additionally, IGHV3-30 has been shown to play a role in modulating cellular signaling pathways, including the JAK/STAT signaling pathway.

One potential drug that targets IGHV3-30 is pevonedistat, a NEDD8-activating enzyme 2 (NAD+-dependent) protein inhibitor.PEVNED2 has been shown to inhibit the activity of IGHV3-30 and prevent its activation in the JAK/STAT signaling pathway. This inhibition leads to the downregulation of STAT3 signaling, which is associated with various diseases, including autoimmune diseases and cancer.

Biomarker Potential

IGHV3-30 has also been identified as a potential biomarker for several diseases, including autoimmune diseases and cancer. IGHV3-30 has been shown to be expressed in various autoimmune diseases, including rheumatoid arthritis (RA), psoriasis, and multiple sclerosis. Additionally, IGHV3-30 has been shown to be involved in the development and progression of cancer, including breast cancer and colorectal cancer.

Expression and Diagnosis

IGHV3-30 has been shown to be expressed in various tissues and cells, including the liver, spleen, and peripheral blood cells. IGHV3-30 can be detected using various techniques, including Western blotting, immunofluorescence, and mass spectrometry. Additionally, IGHV3- 30 has been shown to be expressed in various disease tissues and has been used as a biomarker in several clinical trials.

Conclusion

In conclusion, IGHV3-30 is a unique and promising protein that has the potential to be a drug target and biomarker. Its unique structure and localization, as well as its expression pattern in various tissues and cells, make it an attractive target for drug development . Further research is needed to fully understand the role of IGHV3-30 in immune responses and inflammation, as well as its potential as a biomarker for various diseases.

Protein Name: Immunoglobulin Heavy Variable 3-30

Functions: V region of the variable domain of immunoglobulin heavy 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:22158414, PubMed:20176268). 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:20176268, PubMed:17576170)

The "IGHV3-30 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 IGHV3-30 comprehensively, including but not limited to:
•   general information;
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•   expression level;
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•   related combination drugs;
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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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