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SRP0117

Sigma-Aldrich

Sirtuin 3 human

recombinant, expressed in E. coli, ≥70% (SDS-PAGE)

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Synonym(s):
Mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase, SIR2L3, SIRT3, Silent mating type information regulation 2, sir2-like 3
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

assay

≥70% (SDS-PAGE)

form

aqueous solution

mol wt

59 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 ... SIRT3(23410)

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SRP0119SRP0120SRP0121
Sirtuin 3 human recombinant, expressed in E. coli, ≥70% (SDS-PAGE)

SRP0117

Sirtuin 3 human

Sirtuin 5 human recombinant, expressed in E. coli, ≥50% (SDS-PAGE)

SRP0119

Sirtuin 5 human

Sirtuin 6 human recombinant, expressed in E. coli, ≥70% (SDS-PAGE)

SRP0120

Sirtuin 6 human

Sirtuin 7 human recombinant, expressed in E. coli, ≥70% (SDS-PAGE)

SRP0121

Sirtuin 7 human

biological source

human

biological source

human

biological source

human

biological source

human

assay

≥70% (SDS-PAGE)

assay

≥50% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

form

aqueous solution

form

aqueous solution

form

aqueous solution

form

aqueous solution

mol wt

59 kDa

mol wt

59.8 kDa

mol wt

65 kDa

mol wt

46 kDa

packaging

pkg of 100 μg

packaging

pkg of 100 μg

packaging

pkg of 100 μg

packaging

pkg of 100 μg

General description

Sirtuin 3 (SIRT3) is a member of a family of NAD+-dependent protein deacetylases called sirtuins (SIRTs). In mammals, there are seven types of SIRTs (SIRT1 to 7). SIRT 3 is present in mitochondrial matrix.

Application

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

Biochem/physiol Actions

Sirtuin 3 (SIRT3) is thought to be involved in metabolism as its expression is suppressed in muscles of diabetic animals and increased in white and brown adipose tissues during calorie restriction (CR). This protein modulates the degree of acetylation and activity of acetyl-coenzyme A synthetase 2, an enzyme thought to be involved in energy production during starvation conditions in mammals. Up-regulation of this gene influences the expression of genes involved in mitochondrial function. During fasting, SIRT3 controls mitochondrial intermediary metabolism and fatty-acid use by deacetylating long-chain acyl coenzyme A dehydrogenase (LCAD). It is an essential modulator of basal ATP, and therefore, overall energy homeostasis.

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 and 20% glycerol.

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.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis.
Ahn BH
Proceedings of the National Academy of Sciences of the USA, 105(38), 14447-14452 (2008)
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation.
Hirschey MD, et al.
Nature, 464(7285), 121-125 (2010)
Virtual Screening Combined with Enzymatic Assays to Guide the Discovery of Novel SIRT2 Inhibitors.
Scarano, et al.
International Journal of Molecular Sciences, 24 (2023)
David B Lombard et al.
Molecular and cellular biology, 27(24), 8807-8814 (2007-10-10)
Homologs of the Saccharomyces cerevisiae Sir2 protein, sirtuins, promote longevity in many organisms. Studies of the sirtuin SIRT3 have so far been limited to cell culture systems. Here, we investigate the localization and function of SIRT3 in vivo. We show
L Pacella-Ince et al.
Human reproduction (Oxford, England), 29(7), 1490-1499 (2014-04-29)
Is the activity of sirtuin 3 (SIRT3) altered in granulosa and cumulus cells from young women with reduced ovarian reserve or women of advanced maternal age? SIRT3 mRNA and active protein in granulosa and cumulus cells were decreased in women

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