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anti-Human SIRT4 Antibodies:
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Human Polyclonal SIRT4 Primary Antibody for IHC (p), IHC - ABIN250192
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
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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
Show all 2 Pubmed References
Human Polyclonal SIRT4 Primary Antibody for IHC, ELISA - ABIN185191
do Amaral, Ueno, Oliveira, Borsonello, Vanzela, Ribeiro, Alves, Barbosa, Carneiro, Boschero: Reduced expression of SIRT1 is associated with diminished glucose-induced insulin secretion in islets from calorie-restricted rats. in The Journal of nutritional biochemistry 2011
Show all 2 Pubmed References
This makes SIRT4 become the last puzzle of mitochondrial sirtuins, and thus brings some obstacles for studying SIRT4 biological functions or developing SIRT4 modulators.
structural model of a complex of human Sirt4 and GDH in order to elucidate the molecular mechanism underlying the ADP-ribosylation of GDH by Sirt4
we propose that the SIRT4-OPA1 axis is causally linked to mitochondrial dysfunction and altered mitochondrial dynamics that translates into aging-associated decreased mitophagy based on an unbalanced mitochondrial fusion/fission cycle.
SIRT4 protein levels in endometrioid adenocarcinoma were markedly lower than its non-neoplastic tissue counterpart (P< 0.001).
The function of the three mitochondrial sirtuins (SIRT3, SIRT4, SIRT5) and their role in disease are reviewed.
Protein levels of SIRT 4 were significantly higher in HUVECs from HELLP pregnancies compared to control after 60 and 120 minutes of hypoxia.
we found that knock-out of mitochondrial sirtuin sir-2.3, homologous to mammalian SIRT4, is protective in both chemical ischemia and hyperactive channel induced necrosis. This work suggests a deleterious role of SIRT4 during ischemic processes in mammals that must be further investigated
This is the first study to identify an association between SIRT4 expression and decreased mitochondrial fission, which was driven by Drp1. SIRT4 inhibited Drp1 phosphorylation and weakened Drp1 recruitment to the mitochondrial membrane via an interaction with Fis-1.
miR-15b is a negative regulator of stress-induced SIRT4 expression, thereby counteracting senescence associated mitochondrial dysfunction and regulating the SASP and possibly organ aging, such as photoaging of human skin.
SIRT4 overexpression inhibits the proliferation of colorectal cancer cells in vitro and in vivo.
Data indicate that compared to non-neoplastic endometria (NNE), endometrial cancer (EC) showed SIRT7 mRNA overexpression, whereas SIRT1, SIRT2, SIRT4 and SIRT5 were underexpressed, and no significant differences were observed for SIRT3 and SIRT6.
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, SIRT4, and SIRT5 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.
C-terminal-binding protein (CtBP) 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 is a biological substrate; compared to its catalytic efficiency for deacetylation, SIRT4 exhibits far superior enzymatic activity for lipoyl- and biotinyl-lysine modifications.
Loss of sirtuin 4 leads to elevated glucose- and leucine-stimulated insulin levels and accelerated age-induced insulin resistance in mice from multiple genetic backgrounds.
SIRT4 is downregulated in cardiomyocytes after myocardial ischemia-reperfusion (MI-R), ameliorates MI-R injury, preserves mitochondrial function and reduces cardiomyocyte apoptosis after MI-R.
Data suggest that high-fat diet (HFD) alters regulation of expression of sirtuins (Sirt4 and Sirt7) and enzymes in NAD biosynthetic pathway (Tdo2 and Nnmt); these alterations are more prominent in liver as compared to white adipose tissue or skeletal muscle; Tdo2 and Nnmt may serve as markers of HFD consumption. (Tdo2 = tryptophan 2,3-dioxygenase; Nnmt = nicotinamide N-methyltransferase)
These findings identify a robust enzymatic activity for SIRT4, uncover a mechanism controlling branched-chain amino acid flux, and position SIRT4 as a crucial player maintaining insulin secretion and glucose homeostasis during aging.
miR-497 modulates cardiac hypertrophy by targeting Sirt4 and may serve as a potential therapeutic substance in the course.
The results of this study indicated a critical and novel stress response role for SIRT4 in promoting proper glutamate transport capacity and protecting against excitotoxicity
regulates ATP levels via ANT2 and a feedback loop involving AMPK
these results highlight the tumor-suppressive role of SIRT4 in Myc-induced B cell lymphoma and suggest that SIRT4 may be a potential target against Myc-induced and/or glutamine-dependent cancers.
The enhanced fatty acid oxidation observed in SIRT4 knockout hepatocytes requires functional SIRT1, 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 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, human SirT1, mouse SirT4, and mouse SirT6.
Fluorescence in situ hybridization analysis identified a single genomic locus for murine Sirt4 gene on chromosome 5F and is neighbored by the PLA2G1B and PXN genes.
NRF1-mediated transcriptional inhibition and CMYB-mediated transcriptional activation of SIRT4 expression were strengthened by demethylation during bovine adipocyte differentiation
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