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SIRT5 encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Zusätzlich bieten wir Ihnen Sirtuin 5 Antikörper (177) und Sirtuin 5 Kits (17) und viele weitere Produktgruppen zu diesem Protein an.
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Our study uncovers a SIRT5-dependent mechanism that regulates cellular NADPH (zeige NQO1 Proteine) homeostasis and redox potential by promoting IDH2 (zeige IDH2 Proteine) desuccinylation and G6PD (zeige G6PD Proteine) deglutarylation.
Results demonstrated presence of endogenous SIRT5 in mitochondria of cultured SH-EP cells, identified down-regulation of cellular oxidative stress by SIRT5 as one of the possible mechanisms mediating the anti-apoptotic effect of SIRT5 in SH-EP cells.
Data (including data from studies using knockout mice) suggest that SIRT5 is targeted to protein complexes on the inner mitochondrial membrane via affinity for cardiolipin to promote respiratory chain function, particularly Complex I and Complex II; SIRT5 expression is observed in inner mitochondrial membrane of periportal hepatocytes.
a side chain-to-side chain cyclic pentapeptide harboring a central N(epsilon)-carboxyethyl-thiocarbamoyl-lysine residue behaved as a strong and selective (versus human SIRT1 (zeige SIRT1 Proteine)/2/3/6) inhibitor against human SIRT5-catalyzed deacylation reaction.
Data indicate that compared to non-neoplastic endometria (NNE (zeige ENO1 Proteine)), endometrial cancer (EC) showed SIRT7 (zeige SIRT7 Proteine) mRNA overexpression, whereas SIRT1 (zeige SIRT1 Proteine), SIRT2 (zeige SIRT2 Proteine), SIRT4 (zeige SIRT4 Proteine) and SIRT5 were underexpressed, and no significant differences were observed for SIRT3 (zeige SIRT3 Proteine) and SIRT6 (zeige SIRT6 Proteine).
Use of a pan-sirtuin (zeige SIRT1 Proteine) inhibitor and shRNA-mediated protein knockdown led us to uncover a role for the NAD(+)-dependent family of sirtuins, and in particular for SIRT2 (zeige SIRT2 Proteine) and SIRT5, in the regulation of the necroptotic cell death program
mutual cooperation between Y102 and R105 residues in promoting the desuccinylation versus deacetylation reaction in SIRT5.
Data showed that SIRT5 was involved in protein post-translational modifications through its potent demalonylase, desuccinylase, and deglutarylase activities. Also, the protein was found in the mitochondrial, cytoplasmic, and nuclear compartments. [review]
Results show that mitochondrial sirtuins SIRT3 (zeige SIRT3 Proteine), SIRT4 (zeige SIRT4 Proteine), and SIRT5 can promote increased mitochondrial respiration and cellular metabolism and respond to excess glucose by inducing a coordinated increase of glycolysis and respiration.
Results suggest a role for SIRT5 in influencing oocyte quality and in vitro fertilization outcomes.
Association analysis of individual SIRT5 SNPs and haplotype combinations reveal that the 4 loci are significantly associated with some body measurement and ultrasound traits in Qinchuan cattle.
Deletion of Sirt5 in starved mouse embryonic fibroblasts increased levels of mitochondrial dynamics leading to mitochondrial accumulation of the pro-fission Drp1 and to mitochondrial fragmentation.
Our study uncovers a SIRT5-dependent mechanism that regulates cellular NADPH (zeige FDXR Proteine) homeostasis and redox potential by promoting IDH2 (zeige IDH2 Proteine) desuccinylation and G6PD (zeige G6PD Proteine) deglutarylation.
Data show that peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1alpha) overexpression significantly increased the expression of sirtuin 3 (SIRT3 (zeige SIRT3 Proteine)) and sirtuin 5 (SIRT5).
In the cochlea, the expression of SIRT1 (zeige SIRT1 Proteine), 3, and 5 (both mRNA and protein) was decreased in the old mice
These findings establish that regulating heart metabolism and function is a major physiological function of lysine succinylation and SIRT5.
Myocardial ischemic reperfusion injury in Sirt5-/- heart is restored to wild-type levels by pretreatment with dimethyl malonate, a competitive inhibitor of succinate dehydrogenase (SDH (zeige SDHA Proteine)), implicating alteration in SDH (zeige SDS Proteine) activity as causative of the injury.
SIRT5 has a role in cellular metabolism with a multiple enzymatic activities
SIRT3 (zeige SIRT3 Proteine) and SIRT5 regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase (zeige ACADVL Proteine)
Pathway analysis identified glycolysis as the top SIRT5-regulated pathway. Importantly, glycolytic flux was diminished in primary hepatocytes from Sirt5(-/-) compared to WT mice.
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 III of the sirtuin family. Alternative splicing of this gene results in multiple transcript variants.
sirtuin (silent mating type information regulation 2 homolog) 5 (S. cerevisiae)
, sirtuin 5
, NAD-dependent lysine demalonylase and desuccinylase sirtuin-5, mitochondrial
, NAD-dependent protein deacylase sirtuin-5, mitochondrial
, regulatory protein SIR2 homolog 5
, sirtuin (silent mating type information regulation 2 homolog) 5
, NAD-dependent deacetylase sirtuin-5
, SIR2-like protein 5
, nad-dependent deacetylase sirtuin-5
, silent mating type information regulation 2, S.cerevisiae, homolog 5
, sir2-like 5
, sirtuin type 5
, NAD-dependent lysine demalonylase and desuccinylase sirtuin-5A, mitochondrial
, NAD-dependent protein deacylase sirtuin-5A, mitochondrial
, regulatory protein SIR2 homolog 5-a
, Regulatory protein SIR2 homolog 5