Peptide mapping to the carboxy terminal domain of human SIRT1.
Formulation:
This antibody is provided in phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide and 0.2% gelatin.
Preparation:
This antibody was purified by affinity chromatography.
Storage & Handling:
The antibody solution should be stored undiluted at 4°C. DO NOT FREEZE..
Application:
IP* - *This application has been reported in the literature.
Recommended Usage:
Each lot of this antibody is quality control tested by Western blotting. Western blotting suggested working dilution(s): Use 10 µl per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
Description:
SIRT1, the human homolog of the S. cerevisiae Sir2 protein, functions as an NAD-dependent deacetylase of a number of nonhistone substrates including p53. In response to DNA damage, SIRT1 binds and deacetylates the p53 protein at c-terminal Lys382 residue and attenuate p53-mediated functions. When overexpressed in mouse embryo fibroblasts, SIRT1 antagonizes PML-induced acetylation of p53 and rescues PML-mediated premature cellular senescence. In mammalian cells, SIRT1 appears to control the cellular response to stress by regulating the FOXO family of forkhead transcription factors. The Poly6343 antibody has been shown to be useful for western blotting and immunoprecipitation ofhuman SIRT1 protein.
Other Names:
NAD-dependent deacetylase sirtuin-1, SIR2-like protein 1, hSIRT1, hSIR2 < SIR2-like protein 1, SIR2L1>
Structure:
Belongs to the sirtuin family, contains 1 deacetylase sirtuin-type domain.
p53, E1A binding protein p300, HEY2, NF-kB3, Transcription factor HES-1, Forkhead box protein O3A, and PML.
Bioactivity/Activities:
SIRT1 involved in various nuclear events such as transcription, DNA replication, and DNA repair. SIRT1 binds and deacetylates the p53 protein at c-terminal Lys382 residue and attenuate p53-mediated functions. When overexpressed in mouse embryo fibroblasts
Antigen References:
1. Frye, R. A., et al. 1999. Biochem. Biophys. Res. Commun. 260: 273
