SIRT1 protein – Human SIRT1 recombinant protein

General Information On SIRT1 protein:

SIRT1 protein stands for sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae). This protein, also known as NAD-dependent deacetylase sirtuin-1 is encoded by SIRT1 gene in humans. SIRT1 acts as an enzyme that deacetylates proteins involved in cellular regulation (reaction to stressors, longevity)

This protein is a member of the sirtuin family of proteins which are homologs of the Sir2 gene coded proteins in S. cerevisiae. Members of the sirtuin family are characterized by a sirtuin core domain that consists of a large and a small domain. The large domain contains a Rossmann fold which binds to NAD+. The small domain consists of two insertions in Rosmann fold which form a helical and a zinc binding modules. This NAD-dependent participates in the coordination of several cellular functions such as response to DNA damage, metabolism, cell cycle apoptosis and autophagy. SIRT1 protein is involved in histone deacetylation which can promote alterations in DNA and histone methylation. This process can lead to transcriptional repression and can modulate chromatin function. SIRT1 protein is responsible for the deacetylation of a broad range of transcription factors and cofactors, thus regulating gene expression negatively or positively. MAPK8/JNK1 and RPS19BP1/AROS complex act as positive regulators of deacetylation activity of SIRT1 protein.

Sirtuin 1 protein is inhibited by nicotinamide. However, the protein is activated by resveratrol (also known as 3,5,4′-trihydroxy-trans-stilbene), butein (also known as 3,4,2′,4′-tetrahydroxychalcone), piceatannol (also known as 3,5,3′,4′-tetrahydroxy-trans-stilbene), Isoliquiritigenin (also known as 4,2′,4′-trihydroxychalcone), fisetin (also known as 3,7,3′,4′-tetrahydroxyflavone) and quercetin (also known as 3,5,7,3′,4′-pentahydroxyflavone). MAPK8/JNK1 and RPS19BP1/AROS act as positive regulators of deacetylation activity whereas CCAR2 acts as negative regulators.

SIRT1 protein is recruited to the nuclear bodies via its interaction with PML protein. In the nucleus, SIRT1 protein is colocalized with APEX1 complex. Sirtuin 1 protein can be located in the nucleolus, in nuclear euchromatin, heterochromatin as well as inner membrane. This protein is thought to shuttles between nucleus and cytoplasm.