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SIRT5 (human), (recombinant) (His-tag)

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BML-SE555-0050 50 kU 356.00 USD
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Product Specification

Alternative Name:Sirtuin 5, Sir2-like protein 5, SIR2L5, NAD-dependent deacetylase Sirtuin-5
Source:Produced in E. coli.
UniProt ID:Q9NXA8
Formulation:Liquid. In 25mM TRIS, pH 7.5, 100mM sodium chloride, 5 mM DTT, containing 10% (v/v) glycerol.
Purity:≥95% (SDS-PAGE)
Purity Detail:Purified by multi-step chromatography.
Specific Activity:One unit = 1 pmol/min at 37°C, 200µM FLUOR DE LYS® Succinyl, Desuccinylase Substrate (Prod. No. BML-KI590), 2mM NAD+.
Application Notes:Useful for studies of enzyme kinetics, modulator activity, drug discovery.
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Use/Stability:The enzyme is stable on ice for the time typically required to set up an experiment (30-60 min.), but may lose activity with prolonged storage on ice. It is recommended that thawing and dilution of the enzyme be done within as short a time as possible before start of the assay. The remaining, unused enzyme should be refrozen quickly by, for example, snap freezing in a dry/ice ethanol bath or liquid nitrogen. The enzyme is stable to at least 4 freeze/thaw cycles. To minimize the number of freeze/thaw cycles, aliquot the SIRT5 into separate tubes and store at -80° C.NOTE: When stored under the above conditions, this enzyme is stable at the concentration supplied, in its current storage buffer. Procedures such as dilution of the enzyme followed by refreezing, could lead to loss of activity.
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
Scientific Background:SIRT5, along with SIRTs 3 and 4, is one of three human mitochondrial sirtuins (homologs of yeast Sir2). SIRT5, which is localized to both the mitochondrial matrix and the intermembrane space, is an NAD+-dependent lysine deacetylase (class III HDAC). SIRT5's only known physiological target is the intermembrane space protein, cytochrome c, suggesting the possibility of regulatory roles in metabolism and/or apoptosis. SIRT5 has also been shown to deacetylate and thereby upregulate the matrix urea cycle enzyme carbamoyl phosphate synthetase 1. This implies an important role for SIRT5 in ammonia detoxification and adaptation to elevated amino acid catabolism during starvation, calorie restriction or a high protein diet. SIRT5 is most strongly expressed in thymus, lymphoblasts and heart muscle cells and its chromosomal location (6p23) has been implicated in chromosomal abnormalities associated with malignancies. SIRT5 deacetylase activity may be measured with the FLUOR DE LYS® Desuccinylase (Prod. No. BML-KI590) or SIRT1 (Prod. No. BML-KI177) substrates, and, like SIRT1, its activity is stimulated by polyphenols such as resveratrol and fisetin. Two SIRT5 crystal structures have been determined, one as a complex with ADP-ribose and the other a complex with the inhibitor suramin. This recombinant preparation, expressed in E. coli, comprises residues 37-310 of SIRT5 isoform 1, with an N-terminal His-tag. Recombinant human mitochondrial processing protease cleaves full-length SIRT5 after residue thirty-six, suggesting that the mature, in vivo form may begin with residue 37. Consistent with this, N-terminal sequence of mouse SIRT5 processed in 293T cells also commences at residue 37.
BML-SE555 Figure 1
Figure 1
SDS-PAGE Analysis: Lane 1: MWM; Lane 2: 1.0 µg of purified SIRT5 protein.
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BML-SE555 Figure 1 BML-SE555 SDS-PAGE

Product Literature References

Investigating the Sensitivity of NAD+-Dependent Sirtuin Deacylation Activities to NADH: A.S. Madsen, et al.; J. Biol. Chem. 291, 7128 (2016), Application(s): Incubation, measurement of hydrolase activity, 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

General Literature References

SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle: T. Nakagawa, et al.; Cell 137, 560 (2009), Abstract;
Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activity: J.A. Pfister, et al.; PLoS ONE 3, e4090 (2008), Abstract;
Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5: C. Schlicker, et al.; J. Mol. Biol. 382, 790 (2008), Abstract;
Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin: A. Schuetz, et al.; Structure 15, 377 (2007), Abstract;
Assignment of the NAD-dependent deacetylase sirtuin 5 gene (SIRT5) to human chromosome band 6p23 by in situ hybridization: U. Mahlknecht, et al.; Cytogenet. Genome Res. 112, 208 (2006), Abstract;
Compositions and methods for selectively activating human sirtuins: K.T. Howitz & R.E. Zipkin; U.S. Patent Application 20060014705, (2006),
Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins: E. Michishita, et al.; Mol. Biol. Cell 16, 4623 (2005), Abstract;
The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase:: B.J. North, et al.; Mol. Cell 11, 437 (2003), Abstract;
Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity: R.A. Frye; Biochem. Biophys. Res. Commun. 260, 273 (1999), Abstract;

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