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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 Proteine (18) und Sirtuin 5 Kits (16) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 177 products:
Human Polyclonal SIRT5 Primary Antibody für IHC (p), WB - ABIN390180
Wang, Yi, Li, Cai, He, Ni, Zhou, Cheng, Jin, Fan, Qiu: Down-regulation of sirtuin 3 is associated with poor prognosis in hepatocellular carcinoma after resection. in BMC cancer 2014
Human Polyclonal SIRT5 Primary Antibody für IHC, IHC (p) - ABIN4353920
Lv, Liu, Cheng, Yu, Xiong, Hu, Tang, Zeng, Sang: SUN2 exerts tumor suppressor functions by suppressing the Warburg effect in lung cancer. in Scientific reports 2015
Human Polyclonal SIRT5 Primary Antibody für IHC (fro), IF (p) - ABIN1387080
Takumida, Takumida, Anniko: Localization of sirtuins in the mouse inner ear. in Acta oto-laryngologica 2014
Human Polyclonal SIRT5 Primary Antibody für WB - ABIN252349
Alhazzazi, Kamarajan, Joo, Huang, Verdin, DSilva, Kapila: Sirtuin-3 (SIRT3), a novel potential therapeutic target for oral cancer. in Cancer 2011
Cow (Bovine) Polyclonal SIRT5 Primary Antibody für WB - ABIN2778619
Mahlknecht, Ho, Letzel, Voelter-Mahlknecht: Assignment of the NAD-dependent deacetylase sirtuin 5 gene (SIRT5) to human chromosome band 6p23 by in situ hybridization. in Cytogenetic and genome research 2006
Show all 2 Pubmed References
Our study uncovers a SIRT5-dependent mechanism that regulates cellular NADPH (zeige NQO1 Antikörper) homeostasis and redox potential by promoting IDH2 (zeige IDH2 Antikörper) desuccinylation and G6PD (zeige G6PD Antikörper) 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 Antikörper)/2/3/6) inhibitor against human SIRT5-catalyzed deacylation reaction.
Data indicate that compared to non-neoplastic endometria (NNE (zeige ENO1 Antikörper)), endometrial cancer (EC) showed SIRT7 (zeige SIRT7 Antikörper) mRNA overexpression, whereas SIRT1 (zeige SIRT1 Antikörper), SIRT2 (zeige SIRT2 Antikörper), SIRT4 (zeige SIRT4 Antikörper) and SIRT5 were underexpressed, and no significant differences were observed for SIRT3 (zeige SIRT3 Antikörper) and SIRT6 (zeige SIRT6 Antikörper).
Use of a pan (zeige SUPT6H Antikörper)-sirtuin (zeige SIRT1 Antikörper) 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 Antikörper) 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 Antikörper), SIRT4 (zeige SIRT4 Antikörper), 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 (zeige CRMP1 Antikörper) and to mitochondrial fragmentation.
Our study uncovers a SIRT5-dependent mechanism that regulates cellular NADPH (zeige FDXR Antikörper) homeostasis and redox potential by promoting IDH2 (zeige IDH2 Antikörper) desuccinylation and G6PD (zeige G6PD Antikörper) deglutarylation.
Data show that peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1alpha (zeige PPARGC1A Antikörper)) overexpression significantly increased the expression of sirtuin 3 (SIRT3 (zeige SIRT3 Antikörper)) and sirtuin 5 (SIRT5).
In the cochlea, the expression of SIRT1 (zeige SIRT1 Antikörper), 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 Antikörper)), implicating alteration in SDH (zeige SDS Antikörper) activity as causative of the injury.
SIRT5 has a role in cellular metabolism with a multiple enzymatic activities
SIRT3 (zeige SIRT3 Antikörper) and SIRT5 regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase (zeige ACADVL Antikörper)
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