Target Name: IGHV8-51-1
NCBI ID: G28343
Review Report on IGHV8-51-1 Target / Biomarker Content of Review Report on IGHV8-51-1 Target / Biomarker
IGHV8-51-1
Other Name(s): 3-51.1P | Immunoglobulin heavy variable (III)-51-1 (pseudogene) | IGHVIII-51-1 | immunoglobulin heavy variable IGHV8-51-1 (non-functional) | IGHVIII511

Unique IGHV8-51-1 Protein: Potential Drug Target

IGHV8-51-1 (3-51.1P) is a protein that is expressed in most tissues of the body. It is a member of the interleukin-8 (IL-8) family and is involved in the regulation of immune responses, inflammation , and tissue repair. The IGHV8-51-1 protein has been identified as a potential drug target (or biomarker) due to its unique structure, function, and potential clinical applications.

The IGHV8-51-1 protein is a 144 amino acid long protein that is expressed in most tissues of the body, including the skin, hair, nails, heart, lungs, liver, and kidney. It is a member of the IL-8 family, which includes proteins that are involved in the regulation of cytokine signaling, immune responses, and inflammation. The IGHV8-51-1 protein is characterized by a unique structure, which consists of a catalytic domain, a regulatory domain, and a variable region.

The catalytic domain of IGHV8-51-1 is responsible for the catalytic activity of the protein. It consists of a single proteinase active center (PAC) that is optimized for the specific cleavage of the target protein. The catalytic domain is responsible for the formation of a covalent bond between the PAC and the target protein, which is necessary for the protein to be cleaved.

The regulatory domain of IGHV8-51-1 is responsible for regulating the activity of the protein. It consists of a single N-terminal alpha helix that is responsible for the stability and retention of the protein in the cell. The regulatory domain is also involved in the regulation of the activity of the catalytic domain, which is necessary for the protein to be cleaved.

The variable region of IGHV8-51-1 is responsible for the recognition of specific ligands. It consists of a single alpha helix that is responsible for the recognition of the unique ligand specificity of the protein. The variable region is also involved in the regulation of the activity of the catalytic domain, which is necessary for the protein to be cleaved.

The IGHV8-51-1 protein has been shown to have a wide range of physiological functions. It is involved in the regulation of cytokine signaling, which is responsible for the signaling of various cellular processes in the body. It is also involved in the regulation of immune responses, which is necessary for the immune system to protect the body against infection and disease. Additionally, IGHV8-51-1 is involved in the regulation of tissue repair, which is necessary for the body to repair damaged tissue after injury or disease.

The IGHV8-51-1 protein has also been shown to have potential clinical applications. For example, it has been shown to be involved in the regulation of the immune response, which may make it a potential target for cancer therapies. Additionally, IGHV8- 51-1 has been shown to be involved in the regulation of skin health, which may make it a potential target for skin care therapies.

In conclusion, IGHV8-51-1 is a unique and highly conserved protein that is involved in the regulation of a wide range of physiological functions. Its catalytic, regulatory, and variable regions make it a potential drug target (or biomarker) with a wide range of potential clinical applications. Further research is needed to fully understand the role of IGHV8-51-1 in the regulation of various physiological processes and to develop effective therapies based on its unique structure and function.

Protein Name: Immunoglobulin Heavy Variable IGHV8-51-1 (non-functional)

The "IGHV8-51-1 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 IGHV8-51-1 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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