SIRT1 protein – Human SIRT1 recombinant protein

Description of SIRT1 protein / Human SIRT1 recombinant protein

Structure and Function of Human SIRT1 Recombinant Protein

Human SIRT1 recombinant protein, also known as NAD-dependent deacetylase sirtuin-1, is a key protein involved in regulating cellular processes such as metabolism, stress response, and aging. It belongs to the sirtuin family of proteins, which are highly conserved across species and have been extensively studied for their roles in various biological pathways. In this article, we will explore the structure, activity, and potential applications of human SIRT1 recombinant protein.

Structure of Human SIRT1 Recombinant Protein

The human SIRT1 recombinant protein is composed of 747 amino acids and has a molecular weight of approximately 81 kDa. It is primarily localized in the nucleus, but can also be found in the cytoplasm and mitochondria. The protein consists of several domains, including a catalytic domain, a NAD+ binding domain, and a C-terminal regulatory domain. The catalytic domain is responsible for the deacetylase activity of SIRT1, while the NAD+ binding domain is essential for its enzymatic function. The C-terminal regulatory domain plays a crucial role in regulating the activity of SIRT1 by interacting with other proteins.

Activity of Human SIRT1 Recombinant Protein

Human SIRT1 recombinant protein is a NAD+-dependent deacetylase, which means it requires the coenzyme NAD+ to remove acetyl groups from target proteins. This process, known as deacetylation, plays a critical role in regulating gene expression and protein function. SIRT1 primarily targets lysine residues on histones, which are proteins that help package DNA into chromatin. By deacetylating histones, SIRT1 can modulate gene expression and influence various cellular processes such as DNA repair, cell cycle regulation, and stress response.

In addition to histones, SIRT1 also deacetylates a variety of non-histone proteins, including transcription factors, enzymes, and structural proteins. This wide range of substrates allows SIRT1 to regulate diverse cellular pathways and maintain cellular homeostasis. Furthermore, SIRT1 has been shown to have both deacetylase and mono-ADP-ribosyltransferase activities, which further expand its functional repertoire.

Applications of Human SIRT1 Recombinant Protein

Due to its crucial role in regulating various cellular processes, human SIRT1 recombinant protein has been extensively studied as a potential drug target. Several studies have shown that modulating the activity of SIRT1 can have beneficial effects on age-related diseases such as cancer, neurodegenerative disorders, and metabolic disorders. For instance, activating SIRT1 has been shown to improve insulin sensitivity and delay the onset of age-related diseases in animal models. Therefore, developing drugs that target SIRT1 could have significant therapeutic potential.

In addition to its potential as a drug target, human SIRT1 recombinant protein is also used in research to study its role in various biological processes. Recombinant SIRT1 protein can be used to investigate its enzymatic activity, identify new substrates, and study its interactions with other proteins. Furthermore, recombinant SIRT1 can be used to generate mutant forms of the protein, allowing researchers to better understand its structure and function.

Conclusion

In summary, human SIRT1 recombinant protein is a highly conserved protein that plays a crucial role in regulating cellular processes such as metabolism, stress response, and aging. Its structure, activity, and potential applications make it a promising drug target for the treatment of age-related diseases. Further research on SIRT1 and its interactions with other proteins will provide a better understanding of its role in maintaining cellular homeostasis and may lead to the development of new therapeutic strategies.