SIRT5 (human, recombinant)

Sirtuin 5 (SIRT5) is an enzyme that catalyzes the NAD-dependent removal of malonyl, succinyl, and glutaryl groups from target proteins. Although it was originally characterized as a class III histone deacetylase (HDAC), SIRT5 exhibits weak NAD-dependent deacetylase activity in vitro and in vivo. SIRT5 is localized to mitochondria and is composed of a zinc binding domain and a Rossmann fold domain with the NAD and substrate binding sites located at the domain interface. Knockdown of Sirt5 induces hepatic and muscle protein hypersuccinylation, as well as fatty acid oxidation defects and hypertrophic cardiomyopathy in mice. SIRT5 protein and mRNA expression is elevated in human non-small cell lung cancer (NSCLC) tumors and is predictive of tumor recurrence and poor survival. SIRT5 also interacts with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) non-structural protein 14 (Nsp14), an exoribonuclease component of the viral replicase-transcriptase complex. Cayman's SIRT5 (human, recombinant) protein can be used for ELISA and western blot applications.Synonyms: Mitochondrial Regulatory Protein SIR2 Homolog 5, NAD-dependent Deacetylase 5, NAD-dependent Protein Deacylase Sirtuin-5, Silent Information Regulator 5, SIR2L5, SIR2-like Protein 5, Sirtuin 5. Purity: >85% estimated by SDS-PAGE. Source: Recombinant human N-terminal GST-tagged enzyme purified from E. coli. MW: 60.6 kDa. Formulation: (Request formulation change), 50 mM NaPO4, pH 7.2, 100 mM sodium chloride, 5mM DTT, 20% glycerol. UniProt Accession #: Q9NXA8.