Recombinant Human Sirtuin 3/SIRT3 Protein, CF Summary
Details of Functionality
Measured by its ability to remove the acetyl group from a fluorogenic peptide substrate Ac-RGK(Ac)-AMC (Catalog # ES016) in a coupled assay. The specific activity is >2 pmol/min/μg, as measured under the described conditions.
E. coli-derived human Sirtuin 3/SIRT3 protein Ser101-Lys399, with an N-terminal Met and 6-His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<1.0 EU per 1 μg of the protein by the LAL method.
34 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
30-33 kDa, reducing conditions
Read Publication using 7488-DA in the following applications:
SIR2L3silent mating type information regulation 2, S.cerevisiae, homolog 3
SIR2-like protein 3
sirtuin (silent mating type information regulation 2 homolog) 3 (S. cerevisiae)
sirtuin (silent mating type information regulation 2, S.cerevisiae, homolog) 3
sirtuin type 3
Sirtuin 3 (SIRT3) is a NAD+-dependent class III histone deacetylase. It is primarily compartmentalized to mitochondria (1) and activates mitochondrial target proteins, including ACSS1, IDH2 and GDH by deacetylating key lysine residues (2-4). SIRT3 plays an important role in regulating mitochondrial metabolism and energy production and thus has emerged as a potential therapeutic target to treat metabolic and neurological diseases (5). Polymorphisms in human SIRT3 have been linked to survivorship among the elderly, suggesting a possible involvement of SIRT3 in age-related phenomena (6).
North, B. J. et al. (2004) Genome Biology 5:224.
Schwer, B. et al. (2006) Proc. Natl. Acad. Sci. 103:11224.
Schlicker, C. et al. (2008) J. Mol. Biol. 382:790.
Ahn, B.-H. et al. (2008) Proc. Natl. Acad. Sci. 105:14447.
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