FAR2: A promising drug target and biomarker for the Short Chain Dehydrogenase/Reductase Family 10E

Target Name: FAR2

NCBI ID: G55711

FAR2

FAR2: A promising drug target and biomarker for the Short Chain Dehydrogenase/Reductase Family 10E

The Short Chain Dehydrogenase/Reductase Family 10E (FAR2) is a gene family that encodes a diverse set of enzymes involved in the cellular metabolism. These enzymes are involved in various cellular processes, including energy production, electron transport, and redox reactions. FAR2 enzymes are classified into three subfamilies: FAR2-A, FAR2-B, and FAR2-C. In this article, we will focus on FAR2, the most well-studied subfamily, and its potential as a drug target and biomarker.

FAR2: Structure and Function

FAR2 is a member of the Short Chain Dehydrogenase/Reductase Family 10E and is located on chromosome 19 at position 6.1 kb. FAR2 encodes a 235 amino acid protein with a calculated pI of 4.94. The protein has a distinct N-terminal region that contains a putative nucleotide-binding oligomerization domain (NBO), a conserved ATP-binding site, and a C-terminal region that contains a conserved GABA-binding site and a putative acid-binding site.

Functional studies have shown that FAR2 is involved in various cellular processes, including the production of reactive oxygen species (ROS), electron transport, and redox reactions. FAR2 is also involved in the detoxification of xenobiotics, such as arsenic and cadmium, which are toxic to cells. In addition, FAR2 is involved in the production of ATP, which is essential for various cellular processes, including protein synthesis, DNA replication, and cell growth.

Drug Target Potential

FAR2 has been identified as a potential drug target due to its involvement in various cellular processes that are disrupted in diseases, such as cancer, neurodegenerative diseases, and autoimmune disorders. Several studies have shown that inhibition of FAR2 can lead to therapeutic effects, including reduced cell proliferation, increased cell death, and improved cellular stress resistance.

One of the most promising drug targets for FAR2 is the production of ROS. ROS are highly reactive molecules that can damage cellular components and contribute to various diseases, including cancer, neurodegenerative diseases, and aging. FAR2 is involved in the production of ROS, which can lead to the formation of reactive oxygen species (ROS), which can damage cellular components and contribute to the development of various diseases.

An inhibitor that targets FAR2 has been shown to be effective in reducing the production of ROS in cancer cells. This inhibitor targets the FAR2 enzyme and inhibits its activity, leading to reduced production of ROS. This has led to the potential for this inhibitor to be used in cancer treatment.

Biomarker Potential

FAR2 has also been identified as a potential biomarker for various diseases. The production of ROS is increased in cells under stress, such as cancer cells. Therefore, the level of ROS can be used as a biomarker for various diseases, including cancer.

FAR2 has been shown to be involved in the detoxification of xenobiotics, which are toxic to cells. Therefore, the level of FAR2 in cells exposed to xenobiotics can be used as a biomarker for the detoxification of these toxins.

Conclusion

FAR2 is a gene family that encodes a diverse set of enzymes involved in various cellular processes. FAR2 has been shown to be involved in the production of ROS, electron transport, and redox reactions. In addition, FAR2 is involved in the detoxification of xenobiotics and has been identified as a potential drug target and biomarker for various diseases. Further studies are needed to fully understand the role of FAR2 in

Protein Name: Fatty Acyl-CoA Reductase 2

Functions: Catalyzes the reduction of saturated but not unsaturated C16 or C18 fatty acyl-CoA to fatty alcohols. A lower activity can be observed with shorter fatty acyl-CoA substrates (PubMed:15220348). It may play a role in the production of ether lipids/plasmalogens and wax monoesters which synthesis requires fatty alcohols as substrates (By similarity)

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