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SRP0116

Sigma-Aldrich

Sirtuin 2 human

recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

Synonym(s):

SIR2L2, SIRT2, sir2-like 2

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

assay

≥80% (SDS-PAGE)

form

aqueous solution

mol wt

35.5 kDa

packaging

pkg of 100 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

>0.02 mg/mL

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... SIRT2(22933)

General description

Silent information regulator 2 (Sir2) or sirtuin 2 is encoded by the gene mapped to human chromosome 19q13.2. It belongs to class Ib of sirtuin protein family. Sir2 is characterized with a catalytic domain containing two different domains that bind NAD and the acetyl-lysine substrate, respectively. Apart from this, it also constitutes variable NH2 and COOH-terminal domains involved in the regulation of subcellular localizations and catalytic activity. sirtuin 2 is mainly expressed in cytosol but its migration between cytosol and nucleus facilitates the deacetylation of both α-tubulin and histones.
Human Sirtuin 2, GenBank Accession No. NM_030593, amino acids 50-356 with C-terminal His tag, MW = 35.5kDa, expressed in Escherichia coli expression system.

Application

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Biochem/physiol Actions

Silent information regulator 2 (Sir2) acts as a nicotine adenine dinucleotide (NAD) dependent deacetylase and is implicated in various biological processes such as regulation of transcriptional repression, recombination, the cell-division cycle, microtubule organization, and cellular responses to DNA-damaging agents. In addition, sirtuins also regulate the process involved in aging. Sir2 plays a vital role in mammalian metabolic homeostasis and is considered to be a potent therapeutic target for the treatment of type 2 diabetes. Sir2 has a crucial role in reduction of microglial activation and brain inflammation. Therefore, loss of Sir2 activity increases the risk of susceptibility to neurodegenerative diseases.

Unit Definition

One unit is defined as the amount of enzyme required to deacetylate 1 pmol of substrate/min at 37°C.

Physical form

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 50% glycerol and 3 mM DTT.

Preparation Note

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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The NAD-dependent deacetylase sirtuin 2 is a suppressor of microglial activation and brain inflammation.
Pais TF
The Embo Journal, 32(19), 2603-2616 (2013)
Emerging Role of Sirtuin 2 in the Regulation of Mammalian Metabolism.
Gomes P
Trends in Pharmacological Sciences, 36(11), 756-768 (2015)
Yi Shi et al.
eLife, 3, e02349-e02349 (2014-06-19)
Recent studies suggested an essential role for seryl-tRNA synthetase (SerRS) in vascular development. This role is specific to SerRS among all tRNA synthetases and is independent of its well-known aminoacylation function in protein synthesis. A unique nucleus-directing domain, added at
Sirtuins: Sir2-related NAD-dependent protein deacetylases.
North BJ and Verdin E.
Genome Biology, 5(5), 224-224 (2004)
Ruwin Pandithage et al.
The Journal of cell biology, 180(5), 915-929 (2008-03-12)
Cyclin-dependent kinases (Cdks) fulfill key functions in many cellular processes, including cell cycle progression and cytoskeletal dynamics. A limited number of Cdk substrates have been identified with few demonstrated to be regulated by Cdk-dependent phosphorylation. We identify on protein expression

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