- CITATIONS: 2
|Other Names||NAD-dependent protein deacetylase sirtuin-3, mitochondrial, hSIRT3, 351-, Regulatory protein SIR2 homolog 3, SIR2-like protein 3, SIRT3, SIR2L3|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6242a was selected from the C-term region of human SIRT3 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||NAD-dependent protein deacetylase. Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues. Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA and the ATP synthase subunit ATP5O. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels.|
|Cellular Location||Mitochondrion matrix|
|Tissue Location||Widely expressed.|
Provided below are standard protocols that you may find useful for product applications.
SIRT3 is a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The SIRT3 is included in class I of the sirtuin family.
Onyango, P., et al., Proc. Natl. Acad. Sci. U.S.A. 99(21):13653-13658 (2002).Schwer, B., et al., J. Cell Biol. 158(4):647-657 (2002).Frye, R.A., Biochem. Biophys. Res. Commun. 273(2):793-798 (2000).Frye, R.A., Biochem. Biophys. Res. Commun. 260(1):273-279 (1999).
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