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Cat. Number
065874702808409
Chemical Name
SIRT2 Direct Fluorescent Screening Assay Kit
References
Stability 1 year
Storage -80°C
Shipping Dry ice in continental US; may vary elsewhere

Background Reading

Strahl, B.D., and Allis, D. The language of covalent histone modifications. Nature 403 41-45 (2000 Jan 6).

Finnin, M.S., Donigian, J.R., and Pavletich, N.P. Structure of the histone deacetylase SIRT2. Nat Struct Biol 8(7) 621-625 (2001).

Dali-Youcef, N., Lagouge, M., Froelich, S., et al. Sirtuins: The 'magnificent seven', function, metabolism and longevity. Ann Med 39 335-345 (2007).

North, B.J., Marshall, B.L., Borra, M.T., et al. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11 437-444 (2003).

Hiratsuka, M., Inoue, T., Toda, T., et al. Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene. Biochem Biophys Res Commun 309 558-566 (2003).

Grunstein, M. Histone acetylation in chromatin structure and transcription. Nature 389 349-352 (1997 Sep 25).

Cheung, W.L., Briggs, D.B., and Allis, C.D. Acetylation and chromosomal functions. Curr Opin Cell Biol 12 326-333 (2000 Jan 1).

Tanny, J.C., and Moazed, D. Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product. Proc Natl Acad Sci USA 98(2) 415-420 (2001).

Frye, R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273 793-798 (2000).

Imai, S., Armstrong, C.M., Kaeberlein, M., et al. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403 795-800 (2000).

Dryden, S.C., Nahhas, F.A., Nowak, J.E., et al. Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol Cell Biol 23(9) 3173-3185 (2003).

Tang, B.L., and Chua, C.E.L. SIRT2, tubulin deacetylation, and oligodendroglia differentiation. Cell Motil Cytoskeleton 65 179-182 (2008).

Tanner, K.G., Landry, J., Sternglanz, R., et al. Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc Natl Acad Sci USA 97(26) 14178-14182 (2000).

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700280-96well
Half Volume 96-Well Solid Plate (white)
96-Well Cover Sheet
SIRT2 Direct Assay Buffer (10X) 1 ea
SIRT2 (human recombinant) Direct Assay Reagent 2 × 1 ea
SIRT2 Direct Peptide 2 × 1 ea
SIRT2 Direct NAD+ 1 ea
SIRT2 Direct Nicotinamide 1 ea
SIRT2 Direct Developer 1 ea
SIRT2 Direct Fluorophore 1 ea
Size Global Purchasing
96 wells  

Description

The sirtuins represent a distinct class of trichostatin A-insensitive lysyl-deacetylases (class III HDACs) that catalyze a reaction coupling lysine deacetylation to the formation of nicotinamide and O-acetyl-ADP-ribose. Cayman’s SIRT2 Direct Fluorescent Screening Assay provides a fluorescence-based method for screening SIRT2 inhibitors or activators. The procedure requires only two easy steps, both performed in the same microplate. In the first step, the substrate, which comprises the p53 sequence Gln-Pro-Lys-Lys(ε-acetyl)-AMC, is incubated with human recombinant SIRT2 along with its cosubstrate NAD+. Deacetylation sensitizes the substrate such that treatment with the Developer in the second step releases a fluorescent product.
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