IGHV2-70D: A Potential Drug Target and Biomarker (G102723168)

Target Name: IGHV2-70D

NCBI ID: G102723168

IGHV2-70D

Other Name(s): immunoglobulin heavy variable 2-70D | Immunoglobulin heavy variable 2-70D

IGHV2-70D: A Potential Drug Target and Biomarker

Immunoglobulin heavy variable 2-70D (IGHV2-70D) is a protein that is expressed in various tissues of the body, including the liver, spleen, and peripheral blood cells. It is a type of immune globulin (IG), which is a protein produced by B cells that plays a critical role in the immune response. IGHV2-70D has been identified as a potential drug target and biomarker due to its unique structure and expression pattern in various tissues.

The IGHV2-70D protein is composed of five constant (C1) and four variable (C2) regions. The C1 region contains a variable fragment (VF) that is responsible for the antigen recognition, while the C2 region contains a constant fragment (CF) that is involved in the clustering of the IGHV2 family. IGHV2-70D has a length of 110 amino acids and a molecular weight of 17.9 kDa.

IGHV2-70D has been shown to play a critical role in the immune response by regulating the activation and proliferation of B cells. B cells are responsible for producing antibodies, which are essential for the immune response to pathogens. The IGHV2-70D protein has been shown to regulate the switching of B cells from a state of quiescence to an activated state, which is critical for the production of antibodies.

In addition to its role in B cell regulation, IGHV2-70D has also been shown to play a critical role in the immune response to cancer. IGHV2-70D has been shown to be upregulated in various types of cancer, including lung, breast, and ovarian cancer. This upregulation is associated with the development of cancer stem cells (CSPs), which are cells that have the ability to self-replicate and give rise to new cancerous tumors.

IGHV2-70D has also been shown to be involved in inflammation. IGHV2-70D has been shown to play a critical role in the regulation of inflammation, as it has been shown to downregulate the production of pro-inflammatory cytokines. This downregulation of pro-inflammatory cytokines is important for the regulation of the immune response and the prevention of chronic inflammatory diseases.

Due to its unique structure and expression pattern, IGHV2-70D has been identified as a potential drug target. IGHV2-70D has been shown to be expressed in various tissues of the body, including the liver, spleen, and peripheral blood cells, which makes it an attractive target for small molecule inhibitors. In addition, IGHV2-70D has a low expression level in most tissues, which suggests that it may be a good biomarker for monitoring the effectiveness of drug treatments.

IGHV2-70D has also been shown to be involved in the regulation of the immune response in autoimmune diseases. IGHV2-70D has been shown to play a critical role in the regulation of autoimmune diseases, as it has been shown to downregulate the production of autoantibodies. This downregulation of autoantibodies is important for the regulation of the immune response and the prevention of autoimmune diseases.

In conclusion, IGHV2-70D is a protein that has been identified as a potential drug target and biomarker due to its unique structure and expression pattern. IGHV2-70D plays a critical role in the immune response and has been shown to be involved in the regulation of B cell activation, cancer stem cell development, inflammation, and autoimmune diseases. Therefore, IGHV2-70D is a protein that may be a valuable target for small molecule inhibitors. Further research is needed to

Protein Name: Immunoglobulin Heavy Variable 2-70D

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 "IGHV2-70D 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 IGHV2-70D 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;
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•   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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