Host: E. coli • AA: 30-310 • Tag: N-terminal GST • MW: 60.6 kDa
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SIRT5 (human, recombinant)

Item No. 10318

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
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
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $528

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    Product Description

    Sirtuin 5 (SIRT5) is an enzyme that catalyzes the NAD-dependent removal of malonyl, succinyl, and glutaryl groups from target proteins.1,2 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.1 Knockdown of Sirt5 induces hepatic and muscle protein hypersuccinylation, as well as fatty acid oxidation defects and hypertrophic cardiomyopathy in mice.3 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.4 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.5 Cayman’s SIRT5 (human, recombinant) protein can be used for ELISA and western blot applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Yang, L., Ma, X., He, Y., et al. Sirtuin 5: A review of structure, known inhibitors and clues for developing new inhibitors. Sci. China Life Sci. 60, 249-256 (2017).

    2. Roessler, C., Tüting, C., Meleshin, M., et al. A novel continuous assay for the deacylase sirtuin 5 and other deacetylases. J. Med. Chem. 58(18), 7217-7223 (2015).

    3. Sadhukhan, S., Liu, X., Ryu, D., et al. Metabolomics-assisted proteomics identifies succinylation and SIRT5 as important regulators of cardiac function. PNAS 113(16), 4320-4325 (2016).

    4. Bringman-Rodenbarger, L.R., Guo, A.H., Lyssiotis, C.A., et al. Emerging roles for SIRT5 in metabolism and cancer. Antioxid. Redox Signal. 28(8), 677-690 (2018).

    5. Gordon, D.E., Jang, G.M., Bouhaddou, M., et al. A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature 583(7816), 459-468 (2020).