EPI010
Sirtuin 2 (SIRT2) Inhibitor Screening Assay Kit
100 assays in 96 well plates
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About This Item
Código UNSPSC:
12352200
NACRES:
NA.41
Productos recomendados
uso
100 assays in 96 well plates
condiciones de almacenamiento
protect from light
Nº de acceso NCBI
Condiciones de envío
wet ice
temp. de almacenamiento
−20°C
Información sobre el gen
human ... SIRT2(22933)
mouse ... SIRT2(64383)
Descripción general
Sirtuin 2 (SIRT2) is a cytoplasmic protein and is part of the sirtuin family of proteins. Sirtuin family contains a sirtuin core domain and isgrouped into four classes with SIRT2 being a member of class I. SIRT2 colocalizes with microtubules. The gene encoding this protein is localized on human chromosome 19q13.2.
With Sigma′s Sirtuin Inhibitor Screening Kit, Sirtuin deacetylates the Substrate, and then a Developer cleaves the deacetylated substrate to release a fluorescent group, the latter of which can be detected at Ex/Em = 395/541 nm. In the presence of a SIRT inhibitor, the deacetylation will be impeded, preventing substrate cleavage and release of the fluorescent group. The kit provides a rapid, simple, sensitive, and reliable test, which is suitable for both low and high-throughput screening of SIRT2 inhibitors. A positive control inhibitor, Nicotinamide, is included to compare with the efficacy of the test inhibitors.
With Sigma′s Sirtuin Inhibitor Screening Kit, Sirtuin deacetylates the Substrate, and then a Developer cleaves the deacetylated substrate to release a fluorescent group, the latter of which can be detected at Ex/Em = 395/541 nm. In the presence of a SIRT inhibitor, the deacetylation will be impeded, preventing substrate cleavage and release of the fluorescent group. The kit provides a rapid, simple, sensitive, and reliable test, which is suitable for both low and high-throughput screening of SIRT2 inhibitors. A positive control inhibitor, Nicotinamide, is included to compare with the efficacy of the test inhibitors.
Aplicación
Sirtuin 2 (SIRT2) inhibitor screening assay kit has been used for acetyl peptide deacetylase assay.
Acciones bioquímicas o fisiológicas
Sirtuin 2 (SIRT2) maintains the integrity of the genome. Inhibition of SIRT2 can lead to neuroprotection in cellular and invertebrate models of Huntington′s disease. Huntington′s disease is characterized by increased sterol synthesis in neuronal cells and this process is reversed by SIRT2 inhibition. SIRT2 can deacetylate lys40 of α-tubulin both in vitro and in vivo. Knockdown of SIRT2 by small interfering RNA (siRNA) leads to tubulin hyperacetylation.
Características y beneficios
- Simple, sensitive, and reliable assay
- Species reactivity: mammalian
- Utilizes fluorometric methods
- Suitable for individual tests or high throughput assays
- Convenient 96-well microplate format
- Screening and characterization of Sirtuin inhibitors
Producto relacionado
Referencia del producto
Descripción
Precios
Palabra de señalización
Warning
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Eye Irrit. 2 - STOT SE 3
Órganos de actuación
Respiratory system
Código de clase de almacenamiento
10 - Combustible liquids
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene
Masaharu Hiratsuka
Biochemical and Biophysical Research Communications (2003)
Damir Janigro
The Cell Cycle in the Central Nervous System (2008)
The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase.
North BJ
Molecular and Cellular Biochemistry, 11(2) (2003)
Brian P Weiser et al.
The Journal of biological chemistry, 290(13), 8559-8568 (2015-02-11)
meta-Azi-propofol (AziPm) is a photoactive analog of the general anesthetic propofol. We photolabeled a myelin-enriched fraction from rat brain with [(3)H]AziPm and identified the sirtuin deacetylase SIRT2 as a target of the anesthetic. AziPm photolabeled three SIRT2 residues (Tyr(139), Phe(190)
Propofol Inhibits SIRT2 Deacetylase through a Conformation-specific, Allosteric Site*
Brian P
The Journal of Biological Chemistry (2015)
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