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SIRT4 encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Additionally we are shipping SIRT4 Proteins (10) and SIRT4 Kits (8) and many more products for this protein.
Showing 10 out of 103 products:
Human Polyclonal SIRT4 Primary Antibody for IHC, ELISA - ABIN185191
Frye: 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. in Biochemical and biophysical research communications 1999
Show all 2 references for ABIN185191
Cow (Bovine) Polyclonal SIRT4 Primary Antibody for EIA, IHC (p) - ABIN374409
Ahuja, Schwer, Carobbio, Waltregny, North, Castronovo, Maechler, Verdin: Regulation of insulin secretion by SIRT4, a mitochondrial ADP-ribosyltransferase. in The Journal of biological chemistry 2007
Show all 2 references for ABIN374409
Human Polyclonal SIRT4 Primary Antibody for EIA, WB - ABIN783612
Salminen, Kaarniranta: SIRT1: regulation of longevity via autophagy. in Cellular signalling 2009
Show all 2 references for ABIN783612
Human Polyclonal SIRT4 Primary Antibody for IHC (fro), IF (p) - ABIN872709
Takumida, Takumida, Anniko: Localization of sirtuins in the mouse inner ear. in Acta oto-laryngologica 2014
Thus, these results suggest that SIRT4 has essential roles in stress resistance and may be an important therapeutic target for cancer treatment.
SIRT4 behaves as a tumor suppressor at the human tissue protein level.
Overexpression of SIRT4 attenuated inflammation mediators in umbilical vein endothelial cells.
Results show that mitochondrial sirtuins SIRT3 (show SIRT3 Antibodies), SIRT4, and SIRT5 (show SIRT5 Antibodies) can promote increased mitochondrial respiration and cellular metabolism and respond to excess glucose by inducing a coordinated increase of glycolysis and respiration.
SIRT4 has a tumour-suppressive function and may serve as a novel therapeutic target in colorectal cancer.
Serum Sirt4 was inversely related to anthropometric and metabolic parameters and positively related to peak GH and IGF-1 (show IGF1 Antibodies).
C-terminal-binding protein (CtBP (show CTBP2 Antibodies)) was found to have an essential role in promoting glutaminolysis by directly repressing the expression of SIRT4.
This study demonstrated that SIRT4 upregulation in the liver of non-alcoholic fatty liver disease patients.
Until now, a mammalian cellular lipoamidase has not been characterized; this study discovered that SIRT4 can function with this enzymatic capacity in the mitochondria, and that PDH (show PDP Antibodies) is a biological substrate; compared to its catalytic efficiency for deacetylation, SIRT4 exhibits far superior enzymatic activity for lipoyl- and biotinyl-lysine modifications.
The present study shows low circulating levels of SIRT4 in obese patients with nonalcoholic fatty liver disease.
The results of this study indicated a critical and novel stress response role for SIRT4 in promoting proper glutamate (show GRIN1 Antibodies) transport capacity and protecting against excitotoxicity
regulates ATP levels via ANT2 (show SLC25A5 Antibodies) and a feedback loop involving AMPK (show PRKAA1 Antibodies)
these results highlight the tumor-suppressive role of SIRT4 in Myc (show MYC Antibodies)-induced B cell lymphoma and suggest that SIRT4 may be a potential target against Myc (show MYC Antibodies)-induced and/or glutamine (show GFPT1 Antibodies)-dependent cancers.
The enhanced fatty acid oxidation observed in SIRT4 knockout hepatocytes requires functional SIRT1 (show SIRT1 Antibodies), demonstrating a clear cross talk between mitochondrial and nuclear sirtuins.
Data uncover SIRT4 as an important component of the DNA damage response pathway that orchestrates a metabolic block in glutamine (show GFPT1 Antibodies) metabolism, cell cycle arrest, and tumor suppression.
SIRT4 represses fatty acid oxidation and stimulates lipogenesis. SIRT4 deacetylates and represses malonyl CoA decarboxylase, regulating malonyl coA levels.
Data demonstrate that SIRT4 inhibition increases fat oxidative capacity in liver and mitochondrial function in muscle.
controls insulin secretion in pancreatic beta cells; also transfers an ADP-ribosyl group from NAD to histones
NAD analogues and 32P-NAD were used to study the ADP-ribosyltransferase activity of several different sirtuins, including yeast Sir2 (show SIRT1 Antibodies), human SirT1 (show SIRT1 Antibodies), mouse SirT4, and mouse SirT6 (show SIRT6 Antibodies).
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.
sirtuin (silent mating type information regulation 2 homolog) 4 (S. cerevisiae)
, sirtuin 4
, NAD-dependent ADP-ribosyltransferase sirtuin-4
, NAD-dependent protein deacetylase sirtuin-4
, SIR2-like protein 4
, regulatory protein SIR2 homolog 4
, sir2-like 4
, sirtuin type 4
, NAD-dependent deacetylase sirtuin-4