"SIRT3" Related Products


Recombinant Human SIRT3

Cat. No. : SIRT3-341H
Description : Sirtuins are pylogenetically conserved from bacteria to humans and regulate cell functions beyond silencing. The proteins show a relevance to cancer, obesity, muscle differentiation, inflammation and neuro-degeneration. In addition, Sirtuin activity may extend the lifespan of several organisms. Human Sirtuin 3 (Sirt3) is a mitochondrial member of Class III of the protein deacetylases family (historically called histone deacetylases family). Class III deacetylases utilize NAD+ as cosubstrate and act either as deacetylases or as ADP-ribosyltransferases. Sirt3 regulates mitochondrial function and thermogenesis; the enzyme can deacetylate and thereby activate the mitochondrial acetyl-CoA synthetase 2 which enables mitochondria to activate acetate for metabolic reactions. MW=32.2kDa (292 amino acids).
Source : E.coli.
Form : Purified recombinant protein in 20mM Tris-HCl pH7.8, and 150mM NaCl.
Activity : >20units/μg 1 unit is defined as that amount of enzyme required to catalyze 1 pmol of product per minute at 37℃, 100μM Fluor de Lys-SIRT2 Substrate (Biomol) and 500μM NAD+.
Purity : >90% by SDS-PAGE.
Usage : For in vitro use only.
Storage : Quality guaranteed for 12 months, store at -80℃. Avoid freeze / thaw cycles.
Publication :
Gene Name : SIRT3 sirtuin (silent mating type information regulation 2 homolog) 3 (S. cerevisiae) [ Homo sapiens ]
Synonyms : SIRT3; sirtuin (silent mating type information regulation 2 homolog) 3 (S. cerevisiae); SIR2L3; NAD-dependent deacetylase sirtuin-3, mitochondrial; EC 3.5.1.-; SIR2-like protein 3; hSIRT3; mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase 2; silent mating type information regulation 2, S.cerevisiae, homolog 3; sir2-like 3; sirtuin (silent mating type information regulation 2, S.cerevisiae, homolog) 3; sirtuin 3; sirtuin type 3
Gene ID : 23410
mRNA Refseq : NM_001017524
Protein Refseq : NP_001017524
MIM : 604481
UniProt ID : Q9NTG7
Chromosome Location : 11p15.5
Function : NAD binding; NAD+ ADP-ribosyltransferase activity; hydrolase activity; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; metal ion binding; protein binding; zinc ion binding

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