Anti-SIRT2 Antibody, clone 7G5

Clone 7G5 is a rat monoclonal antibody that detects SIRT2. It recognizes both the unphosphorylated SIRT2 as well as serine 331 phosphorylated SIRT2. It detects both isoforms 1 and 2.

A linear peptide corresponding to 14 amino acids surrounding phosphoserine 331 and 335 in human SIRT2.

Quality Control Testing

Evaluated by Western Blotting in Human cerebral cortex tissue extracts.

Western Blotting Analysis: A 1:500 dilution of this antibody detected SIRT2 in Human cortex tissue extract.

Tested Applications

Western Blotting Analysis: A representative lot detected SIRT2 in Western Blotting application. (Pandithage, R., et al. (2008). J Cell Biol. 180(5):915-29).

Immunoprecipitation Analysis: A representative lot immunoprecipitated SIRT2 in Immunoprecipitation application (Pandithage, R., et al. (2008). J Cell Biol. 180(5):915-29).

Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user.

NAD-dependent protein deacetylase sirtuin-2 (UniProt: Q8IXJ6; also known as EC:2.3.1.286, NAD-dependent protein defatty-acylase sirtuin-2, Regulatory protein SIR2 homolog 2, SIR2-like protein 2) is encoded by the SIRT2 (also known as SIR2L, SIR2L2) gene (Gene ID: 22933) in human. SIRT2 is a NAD-dependent protein deacetylase that deacetylates internal lysines on histone and -tubulin as well as several key transcription factors. Its deacetylase domain is localized in amino acids 57-338 and its nuclear export signal motif is in amino acids 41-51. SIRT2 participates in the modulation of multiple and diverse biological processes, including cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. It serves as an antephase checkpoint that prevents early mitotic entry in response to microtubule stress agents and control of cell cycle progression and genomic stability. It is reported to specifically deacetylate histone H4 at lysine 16 (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression. SIRT2 is phosphorylated at serine 368 by CDK1/cyclin B at the G2/M transition and this phosphorylation regulates the delay in cell-cycle progression. However, phosphorylation at serine 368 by Cdk2/cyclin E complex inactivates SIRT2-mediated -tubulin deacetylation, and negatively regulates cell adhesion, cell migration, and neurite outgrowth during neuronal differentiation. Phosphorylation at serine 331 (isoforms 2 and 3) by Cdk2/cyclin E and Cdk2/cyclin A is reported to inhibit the catalytic activity of SIRT2. SIRT2 levels are up-regulated in response to low levels of glucose and anoxia-reoxygenation stress and down-regulated in response to high levels of glucose. It regulates blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase. (Ref.: Pandithage, R., et al. (2008). J. Cell Biol. 180(5); 915-929; North, BJ., and Verdin, E. (2007). J. Biol. Chem. 282(27); 19546-19555; North, BJ., et al. (2003). Mol. Cell. 11(2); 437-444; Dryden SC., et al. (2003). Mol. Cell Biol. 23(9); 173-185).

Purified rat monoclonal antibody IgG2a in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

1.0 mg/mL. Please refer to guidance on suggested starting dilutions and/or titers per application and sample type.

Recommended storage: +2°C to +8°C.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.