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Merck
CN

5.30648

SIRT2 Inhibitor, AEM2

Synonym(s):

SIRT2 Inhibitor, AEM2, Sirtuin 2 Inhibitor

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About This Item

Empirical Formula (Hill Notation):
C27H27N3O
CAS Number:
Molecular Weight:
409.52
UNSPSC Code:
12352200
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assay

≥98% (HPLC)

form

solid

potency

3.8 μM IC50

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
protect from light

color

white

solubility

DMSO: 50 mg/mL

storage temp.

2-8°C

Quality Level

Biochem/physiol Actions

Cell permeable: yes
Primary Target
SIRT2
Reversible: yes

Disclaimer

Toxicity: Standard Handling (A)

General description

A cell permeable methanophenanthridine derivative that acts a selective inhibitor of SIRT2 (IC50 = 3.8 µM) and exhibits ~30 fold greater selectivity over SIRT1 (IC50 >100 µM) and SIRT3. Blocks SIRT2-induced p53 deacetylation and thereby elevates p53 levels and causes increased expression of CDKN1A, PUMA, and NOXA in non-small cell lung cancer (NSCLC) A549 cells. Also shown to reduce NSCLC cell viability by 50% (~20 µM) and inhibit their proliferation. Sensitizes A549 cancer cell line to etoposide (~1 µM) induced DNA damage in a p53-dependent manner.

Please note that the molecular weight for this compound is batch-specific due to variable water content.

Other Notes

Hoffmann G., et al. 2014. J. Biol. Chem.289, 5208.

Packaging

Packaged under inert gas

Preparation Note

Following reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 1 month at -70°C.
Use only fresh DMSO for reconstitution.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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Gesine Hoffmann et al.
The Journal of biological chemistry, 289(8), 5208-5216 (2014-01-01)
Sirtuin 2 (SIRT2) is an NAD(+)-dependent protein deacetylase whose targets include histone H4 lysine 16, p53, and α-tubulin. Because deacetylation of p53 regulates its effect on apoptosis, pharmacological inhibition of SIRT2-dependent p53 deacetylation is of great therapeutic interest for the

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