Product Pathways - Chromatin Regulation / Epigenetics
SirT5 (D5E11) Rabbit mAb #8779
|8779S||100 µl (10 western blots)||---||In Stock||---|
|8779||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Monkey||Endogenous||30||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
SirT5 (D5E11) Rabbit mAb recognizes endogenous levels of total SirT5 protein. This antibody does not cross-react with other sirtuin proteins.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a recombinant protein specific to the full-length human SirT5 protein.
Western blot analysis of extracts from 293 cells, expressing either nontargeting shRNA (293 shNT) or shRNA targeting SirT5 (293 shSirT5), and HCT 116, Raw 264.7, and COS-7 cells using SirT5 (D5E11) Rabbit mAb (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower). 293 shNT and 293 shSirT5 cells were kindly provided by David Lombard, University of Michigan.
The Silent Information Regulator (SIR2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as Class III histone deacetylases. The first discovered and best characterized of these genes is Saccharomyces cerevisiae Sir2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT5, a mammalian homolog of Sir2, is localized to the mitochondria and has been implicated in the regulation of cell metabolism (2,3). SirT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1) in the mitochondrial matrix and increases its activity in response to fasting, allowing for adaptation to increased amino acid catabolism (4). SirT5 has also been shown to deacetylate cytochrome c in the mitochondrial intermembrane space (5). In addition to its deacetylase activity, SirT5 contains lysine desuccinylase and demalonylase activity (6,7). Succinyl-lysine and malonyl-lysine modifications occur in a variety of organisms and these post-translational modifications are found on many metabolic enzymes (6-8). Like phosphorylation of serine, threonine, and tyrosine residues, lysine succinylation and malonylation induces a change of two negative charges from a +1 to a -1 charge at physiological pH, and are thought to serve similar functions in the regulation of protein activity, protein-protein interactions, and protein stability. SirT5 knockout mice show increased levels of succinyl-lysine and malonyl-lysine protein modifications in the liver, including increased succinylation of CPS1, a known target of SirT5, suggesting that SirT5 functions to regulate metabolic enzymes through its deacetylase, desuccinylase, and demalonylase activities (6,7).
- Guarente, L. (1999) Nat Genet 23, 281-5.
- Newman, J.C. et al. (2012) J Biol Chem , .
- He, W. et al. (2012) Trends Endocrinol Metab 23, 467-76.
- Nakagawa, T. et al. (2009) Cell 137, 560-70.
- Schlicker, C. et al. (2008) J Mol Biol 382, 790-801.
- Du, J. et al. (2011) Science 334, 806-9.
- Peng, C. et al. (2011) Mol Cell Proteomics 10, M111.012658.
- Zhang, Z. et al. (2011) Nat Chem Biol 7, 58-63.
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