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SIRT3 (human, recombinant)

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    SIRT3 (human, recombinant)
  • SIRT3 (human, recombinant)
Cat No: 10011194
Proteins - Enzymes
Cayman

The sirtuins (SIRTs) represent a distinct class of trichostatin A-insensitive lysyl-deacetylases (class III HDACs) and have been shown to catalyze a reaction that couples lysine deacetylation to the formation of nicotinamide and O-acetyl-ADP-ribose fr...

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: 100 µg

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Territorial Availability: Available through Bertin Technologies only in France
Correlated keywords:
  • SIRT 3 SIRTs sirtuins HDACs DNA p53 proteins anti-cancers GST-tags GST-tagged sirtuin silent mating type information regulation 2 homolog 3 sirtuin type 3 sir2-like 3 active genes regulations
Product Overview:
The sirtuins (SIRTs) represent a distinct class of trichostatin A-insensitive lysyl-deacetylases (class III HDACs) and have been shown to catalyze a reaction that couples lysine deacetylation to the formation of nicotinamide and O-acetyl-ADP-ribose from NAD+ and the abstracted acetyl group.{15271,15275,15273} There are seven human SIRTs, which have been designated SIRT 1-7.{15274} SIRT3, is a mitochondrial protein, with its N-terminal 25 amino acid residues responsible for its localization.{15787,15788} Synthesized as an enzymatically inactive protein, human SIRT3 is activated by a matrix-processing peptidase.{15788} Recently, it was demonstrated that SIRT3 is translocated to the mitochondria from the nucleus during cellular stress or by the overexpression of SIRT3 itself.{15789} In mice, caloric restriction up-regulates SIRT3 expression levels in white and brown adipose tissue (WAT & BAT). Cold exposure also induces SIRT3 in brown adipose tissue (BAT).{15790} The constitutive expression of SIRT3 promotes the expression of PGC-1a, UCP1, and other genes involved in mitochondrial functions, indicating that SIRT3 modulates adaptive thermogenesis in BAT.{15790}
Size 100 µg
Shipping dry ice
Formulation 50 mM sodium phosphate, pH 7.2, with 100 mM sodium chloride and 20% glycerol
Purity ≥60% estimated by SDS-PAGE
Custom Code 3507.90
UNSPSC code 12352204

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Cayman Chemical's mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.

Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009

Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.

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