Anti-SIRT4 Antibody Picoband® Fluoro647 Conjugated

Sirtuin 4, also known as SIRT4, is a protein which in humans is encoded by the SIRT4 gene. This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class IV of the sirtuin family.

NAD-dependent protein lipoamidase sirtuin-4, mitochondrial; NAD-dependent ADP-ribosyltransferase sirtuin-4; NAD-dependent protein deacetylase sirtuin-4; Regulatory protein SIR2 homolog 4; SIR2-like protein 4; SIRT4; SIR2L4

A synthetic peptide corresponding to a sequence at the C-terminus of human SIRT4, which shares 93.1% amino acid (aa) sequence identity with both mouse and rat SIRT4.

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.

Acetylation, Atherosclerosis, Cancer, Cardiovascular, Cell Biology, Chromatin Modifying Enzymes, Diabetes, Diabetes-associated, Energy Metabolism, Energy Transfer Pathways, Epigenetics and Nuclear Signaling, Heart Disease, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Signal Transduction

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. 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. In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation. Acts as a tumor suppressor. 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. Does not seem to deacetylate PC. Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1:PPARA interaction probably through the regulation of NAD+ levels. Down-regulates insulin secretion.

1. Frye RA (June 1999) . Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res. Commun. 260 (1) : 273–79. 2. Haigis MC, Mostoslavsky R, Haigis KM, Fahie K, Christodoulou DC, Murphy AJ, Valenzuela DM, Yancopoulos GD, Karow M, Blander G, Wolberger C, Prolla TA, Weindruch R, Alt FW, Guarente L (September 2006) . SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell. 126 (5) : 941–54.