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SRP0119

Sigma-Aldrich

Sirtuin 5 human

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

Synonym(s):
NAD-dependent ADP-ribosyltransferase sirtuin-5, SIR2L5, SIRT5, sir2-like 5
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

Assay

≥50% (SDS-PAGE)

form

aqueous solution

mol wt

59.8 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 ... SIRT5(23408)

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

Sigma-Aldrich

SRP0119

Sirtuin 5 human

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

Sigma-Aldrich

SRP0120

Sirtuin 6 human

Sirtuin 4 human recombinant, expressed in E. coli, ≥70% (SDS-PAGE)

Sigma-Aldrich

SRP0118

Sirtuin 4 human

recombinant

expressed in E. coli

recombinant

expressed in baculovirus infected Sf9 cells

recombinant

expressed in E. coli

recombinant

expressed in E. coli

assay

≥50% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

form

aqueous solution

form

buffered aqueous glycerol solution

form

aqueous solution

form

aqueous solution

mol wt

59.8 kDa

mol wt

~39 kDa

mol wt

65 kDa

mol wt

59 kDa

packaging

pkg of 100 μg

packaging

-

packaging

pkg of 100 μg

packaging

pkg of 100 μg

General description

The sirtuin 5 (SIRT5) gene with eight exons is mapped to human chromosome 6p23. The gene exists in two isoforms codings for 310 amino acid and 299 amino acid protein, respectively. Sirtuin 5 is mainly present in heart muscle cells and in lymphoblasts. It is a member of the silent information regulator 2 (Sir2) family of sirtuin histone deacetylases (HDACs). Sirtuin 5 is a mitochondrial protein.
Human Sirtuin 5, GenBank Accession No. NM_012241), full length with N-terminal ST tag, MW = 59.8kDa, expressed in Escherichia coli expression system.

Application

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

Biochem/physiol Actions

Sirtuin 5 (SIRT5) catalyzes the degradation of negatively charged acylated substrates. It also possesses desuccinylase, demalonylase and deglutarylase activities. SIRT5 is a nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase and is overexpressed in non-small cell lung cancer (NSCLC) and may have a role in cancer growth. Members of sirtun family play a vital role in epigenetic gene silencing, DNA repair and recombination, cell-cycle, microtubule organization, and in the regulation of aging. SIRT5 has been involved in regulation of the carbamoyl phosphase synthase 1 activity, an essential enzyme of urea cycle, via maintaining lysine glutarylation levels. Sirtuin 5 as a mitochondrial protein plays a major role in controlling ATP production, apoptosis, and cell signaling.

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 Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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SIRT5 facilitates cancer cell growth and drug resistance in non-small cell lung cancer.
Lu W
Tumour Biology : the Journal of the International Society For Oncodevelopmental Biology and Medicine, 35(11), 10699-10705 (2014)
Chemical probing of the human sirtuin 5 active site reveals its substrate acyl specificity and peptide-based inhibitors.
Roessler C
Angewandte Chemie (International Edition in English), 53(40), 10728-10732 (2014)
Assignment of the NAD-dependent deacetylase sirtuin 5 gene (SIRT5) to human chromosome band 6p23 by in situ hybridization.
Mahlknecht U
Cytogenetic and genome research, 112(3-4), 208-212 (2006)
Role of the Substrate Specificity-Defining Residues of Human SIRT5 in Modulating the Structural Stability and Inhibitory Features of the Enzyme.
Yu J
PLoS ONE, 11(3), e0152467-e0152467 (2016)
Rommel A Mathias et al.
Cell, 159(7), 1615-1625 (2014-12-20)
Sirtuins (SIRTs) are critical enzymes that govern genome regulation, metabolism, and aging. Despite conserved deacetylase domains, mitochondrial SIRT4 and SIRT5 have little to no deacetylase activity, and a robust catalytic activity for SIRT4 has been elusive. Here, we establish SIRT4

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