SRP0119
Sirtuin 5 human
recombinant, expressed in E. coli, ≥50% (SDS-PAGE)
Synonyme(s) :
NAD-dependent ADP-ribosyltransferase sirtuin-5, SIR2L5, SIRT5, sir2-like 5
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About This Item
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32
Produits recommandés
Source biologique
human
Produit recombinant
expressed in E. coli
Pureté
≥50% (SDS-PAGE)
Forme
aqueous solution
Poids mol.
59.8 kDa
Conditionnement
pkg of 100 μg
Conditions de stockage
avoid repeated freeze/thaw cycles
Concentration
>0.02 mg/mL
Numéro d'accès NCBI
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−70°C
Informations sur le gène
human ... SIRT5(23408)
Description générale
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.
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.
Actions biochimiques/physiologiques
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.
Forme physique
Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20 and 20% glycerol.
Notes préparatoires
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.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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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)
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)
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)
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)
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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