Product Pathways - Chromatin Regulation
SirT2 Antibody #2313
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IF-IC F | H M R Mk | Endogenous | 43 | Rabbit |
Applications Key:
W=Western Blotting
IF-IC=Immunofluorescence (Immunocytochemistry)
F=Flow Cytometry
Reactivity Key:
H=Human
M=Mouse
R=Rat
Mk=Monkey
Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
SirT2 antibody detects endogenous levels of total SirT2 protein (both isoforms). The antibody does not cross-react with other sirtuin proteins.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to human SirT2. Antibodies are purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of cell lysates from HeLa, NIH/3T3, C6 and COS cells, using SirT2 Antibody.
Flow Cytometry
Flow cytometric analysis of HeLa cells, using SirT2 Antibody (blue) compared to a nonspecific negative control antibody (red).
IF-IC
Immunofluorescent analysis of paraformaldehyde-fixed HeLa cells, using SirT2 Antibody.
Background
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). SirT2, a mammalian homolog of Sir2, deacetylates α-tubulin on lysine 40 and histone H4 on lysine 16, and has been implicated in cytoskeletal regulation and progression through mitosis (2,3). SirT2 protein is mainly cytoplasmic and is associated with microtubules and HDAC6, another tubulin deacetylase (2). Deacetylation of α-tubulin decreases its stability and may be required for proper regulation of cell shape, intracellular transport, cell motility and cell division (2,4). The abundance and phosphorylation state of SirT2 increase at the G2/M transition of the cell cycle, and SirT2 relocalizes to chromatin during mitosis when histone H4 lysine 16 acetylation levels decrease (3,5). Overexpression of SirT2 prolongs mitosis, while overexpression of the CDC14B phosphatase results in both decreased phosphorylation and abundance of SirT2, allowing for proper mitotic exit (5). Thus, the deacetylation of both histone H4 and α-tubulin by SirT2 may be critical for proper chromatin and cytoskeletal dynamics required for completion of mitosis.
- Guarente, L. (1999) Nat. Genet. 23, 281-285.
- North, B.J. et al. (2003) Mol. Cell 11, 437-444.
- Vaquero, A. et al. (2006) Genes Dev. 20, 1256-1261.
- Nogales, E. (2000) Annu. Rev. Biochem. 69, 277-302.
- Dryden, S.C. et al. (2003) Mol. Cell Biol. 23, 3173-3185.
Application References
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This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.
