SRP0119
Sirtuin 5 human
recombinant, expressed in E. coli, ≥50% (SDS-PAGE)
Sinónimos:
NAD-dependent ADP-ribosyltransferase sirtuin-5, SIR2L5, SIRT5, sir2-like 5
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About This Item
Código UNSPSC:
12352200
NACRES:
NA.32
Productos recomendados
origen biológico
human
recombinante
expressed in E. coli
Análisis
≥50% (SDS-PAGE)
formulario
aqueous solution
mol peso
59.8 kDa
envase
pkg of 100 μg
condiciones de almacenamiento
avoid repeated freeze/thaw cycles
concentración
>0.02 mg/mL
Nº de acceso NCBI
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−70°C
Información sobre el gen
human ... SIRT5(23408)
Descripción general
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.
Aplicación
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Acciones bioquímicas o fisiológicas
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.
Forma física
Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20 and 20% glycerol.
Nota de preparación
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.
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «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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