Product Details
| Alternative Name: | Sirtuin 2 |
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| MW: | 43 kDa |
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| Source: | Produced in E. coli. Contains a N-terminal His-tag. |
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| UniProt ID: | Q8IXJ6 |
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| Formulation: | Liquid. In 25mM TRIS, pH 7.5, containing 100mM NaCl, 5mM DTT and 10% glycerol. |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Specific Activity: | One unit will deacetylate 1pmol/min of FLUOR DE LYS®-SIRT2 substrate (Prod. No. BML-KI179). |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Scientific Background: | Due to their roles in gene silencing, aging, and oxidative stress responses, it is believed that sirtuins (NAD-dependent lysine deacetylases) play a crucial role in cell metabolism. Human SIRT2 is a class I sirtuin, although not as closely related to Sir2 and human SIRT1. Its catalytic core has the same basic two-domain architecture and central groove as other sirtuins and an interaction with the homeobox transcription factor HOXA10. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Identification of Diketopiperazine-Containing 2-Anilinobenzamides as Potent Sirtuin 2 (SIRT2)-Selective Inhibitors Targeting the "Selectivity Pocket", Substrate-Binding Site, and NAD+-Binding Site: P. Mellini, et al.; J. Med. Chem.
62, 5844 (2019),
Abstract;
Pharmacophore modeling and virtual screening studies to identify novel selective SIRT2 inhibitors: G. Eren, et al.; J. Mol. Graph. Model.
10, 1313 (2019),
Abstract;
Discovery of bicyclic pyrazoles as class III histone deacetylase SIRT1 and SIRT2 inhibitors: E. Therrien, et al.; Bioorg. Med. Chem. Lett.
25, 2514 (2015),
Abstract;
Role of deleted in breast cancer 1 (DBC1) protein in SIRT1 deacetylase activation induced by protein kinase A and AMP-activated protein kinase: V. Nin, et al.; J. Biol. Chem.
287, 23489 (2012),
Abstract;
Full Text
A mechanism-based potent sirtuin inhibitor containing Nε-thiocarbamoyl-lysine (TuAcK): B.M. Hirsch, et al.; Bioorg. Med. Chem. Lett.
21, 4753 (2011),
Abstract;
Full Text
