• Product name

    Recombinant Human SIRT4 protein
    See all SIRT4 proteins and peptides
  • Purity

    > 90 % SDS-PAGE.

  • Expression system

    Escherichia coli
  • Accession

  • Protein length

    Protein fragment
  • Animal free

  • Nature

    • Species

    • Amino acids

      25 to 314
    • Tags

      GST tag N-Terminus

Associated products


Our Abpromise guarantee covers the use of ab79949 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications


  • Form

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.

    pH: 8.00
    Constituents: 0.395% Tris HCl, 0.05% Tween, 20% Glycerol, 0.58% Sodium chloride

General Info

  • Alternative names

    • MGC130046
    • MGC130047
    • MGC57437
    • NAD dependent deacetylase sirtuin 4
    • NAD dependent protein deacetylase sirtuin 4
    • NAD-dependent ADP-ribosyltransferase sirtuin-4
    • NAD-dependent protein deacetylase sirtuin-4
    • NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
    • Regulatory protein SIR2 homolog 4
    • Silent mating type information regulation 2 homolog
    • Sir 2 like 4
    • SIR 2 like protein 4
    • Sir2 like 4
    • SIR2 like protein 4
    • SIR2-like protein 4
    • SIR2L 4
    • SIR2L4
    • SIR4_HUMAN
    • SIRT 4
    • Sirt4
    • Sirtuin (silent mating type information regulation 2 homolog) 4
    • Sirtuin (silent mating type information regulation 2 homolog) 4 (S. cerevisiae)
    • Sirtuin 4
    • Sirtuin type 4
    • Sirtuin-4
    • Sirtuin4
    see all
  • Function

    Acts as NAD-dependent protein lipoamidase, ADP-ribosyl transferase and deacetylase. Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner (PubMed:25525879). Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest (PubMed:16959573, PubMed:17715127). In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation. Acts as a tumor suppressor (PubMed:23562301, PubMed:23663782). Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis (By similarity). Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1:PPARA interaction probably through the regulation of NAD(+) levels (PubMed:24043310). Down-regulates insulin secretion.
  • Tissue specificity

    Detected in vascular smooth muscle and striated muscle. Detected in insulin-producing beta-cells in pancreas islets of Langerhans (at protein level). Widely expressed. Weakly expressed in leukocytes and fetal thymus.
  • Sequence similarities

    Belongs to the sirtuin family. Class II subfamily.
    Contains 1 deacetylase sirtuin-type domain.
  • Cellular localization

    Mitochondrion matrix.
  • Information by UniProt


  • 10% SDS-PAGE, Coomassie staining.
    Lane 1: ab79949 8µg.
    Lane 2: Protein marker.


ab79949 has not yet been referenced specifically in any publications.

Customer reviews and Q&As


I can confirm that ab79949 has not been tested for biological activity in our labs however, other customers who have bought this protein have found it is active. Unfortunately since we do not test this, we cannot guarantee that this protein is active.

Read More

For licensing inquiries, please contact

Sign up