SIRT2


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Cat.No.:  PE-3066
Product Name:  SIRT2
Description:  SIRT2 catalyzes the deacetylation of protein acetyllysine residues in a reaction that forms nicotinamide and O-acetyl-ADP-ribose from the co-substrate NAD+ and the lysine’s acetyl function. In contrast to SIRT1, which is the closest human homolog to yeast Sir2, SIRT2 is the ortholog of another yeast sirtuin, Hst2, which like Sir2, but independently of it, mediates yeast replicative lifespan extension by calorie restriction. While SIRT2 is primarily located in the cytoplasm, where it can form a complex with HDAC6 and function as an a-tubulin deacetylase, it can also undergo cell cycle-linked nucleo-cytoplasmic shuttling and deacetylate various histone and non-histone, cytoplasmic and nuclear substrates. SIRT2’s connections to mitotic regulatory processes include its phosphorylation by Cdk1/cyclin B1, its dephosphorylation by CDC14A/B and its enhancement, via deacetylation of both SET8 (PR-Set7) and histone H4K16, of SET8 monomethylation of histone H4K20, an essential event in cell cycle progression. Depending on the particular cancer type and context, it appears that SIRT2 may act as either a tumor suppressor or tumor promoter. There is evidence that SIRT2 inhibition may be beneficial for neurodegenerative disorders, including Parkinson’s disease and Huntington’s disease, possibly by decreasing sterol biosynthesis via inhibition of SREBP-2 translocation to the nucleus and/or effects on microtubule-mediated translocation of neurotoxic proteins such as oligomeric a-synuclein.
Storage:  Store at 4℃ if entire vial will be used within 2-4 weeks. Store at -20℃ or -80℃ for longer periods of time. Avoid multiple freeze-thaw cycles.
Molecular Weight:  36.5 kDa
Species:  Human
Formulation:  Solution of purified recombinant protein in 50 mM Tris/HCl pH 7.5, 500 mM NaCl, 1 mM TCEP, 10% glycerol (v/v).
Accession#:  NM_012237
Tag:  His
Protein Length:  50-389 (C-term.)
Warning:  This product is for research use only. Not for use in diagnostic or therapeutic procedures.

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