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Sirt3

Protein Deacetylase

human, recombinant, E. coli

Cat. No. Amount Price (EUR) Buy / Note
PR-170 50 μg 322,00 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped on dry ice

Storage Conditions: store at -80 °C
avoid freeze/thaw cycles

Shelf Life: 12 months

Molecular Weight: 32.2 kDa (292 amino acids)

Purity: > 90 % (SDS-PAGE)

Form: liquid (Supplied in 20 mM Tris-HCl pH 7.8 and 150 mM NaCl)

pH: 7.8

Activity: > 20 units/μg, 1 unit is defined as that amount of enzyme required to catalyze 1 pmol of product per minute at 37 °C, 100 μM Fluor de Lys-SIRT2 Substrate (Biomol) and 500 μM NAD+.

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.

Selected References:
Schlicker et al. (2008) Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5.J Mol Biol. 382:790.
Schwer et al. (2006) Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl. Acad. Sci. USA 103:10224.
Porcu et al. (2005) The emerging therapeutic potential of sirtuin-interacting drugs: from cell death to lifespan extension. Trends in Pharmacological Sciences 26.2:94.
Michishita et al. (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell 16:4623.