Nad dependent deacetylase sirtuin 3 sirt3

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NAD-dependent deacetylase sirtuin-3 (Sirt3) is a member of the sirtuin family of enzymes. Sirt3 is a mitochondrial protein that functions as an NAD-dependent deacetylase, catalyzing the removal of acetyl groups from target proteins.

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Lab products found in correlation

Amido black, by Merck Group (2 mentions) Mitoprofile total oxphos rodent wb antibody cocktail, by Abcam (2 mentions) Nad dependent deacetylase sirtuin 1 sirt1, by Santa Cruz Biotechnology (2 mentions) Protein kinase b akt, by Cell Signaling Technology (1 mentions) Srebp 1c, by Santa Cruz Biotechnology (1 mentions) Acetyl coa carboxylase, by Cell Signaling Technology (1 mentions) Phospho akt ser473, by Cell Signaling Technology (1 mentions) Fatty acid synthase fas, by Cell Signaling Technology (1 mentions) Pgc 1α, by Merck Group (1 mentions) Cytochrome c, by Cell Signaling Technology (1 mentions)

Close spelling variants of this product

SIRT3 (143 citations)

2 protocols using nad dependent deacetylase sirtuin 3 sirt3

Comprehensive Protein Expression Analysis

Cited 1 time

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Western blots were performed as described earlier for oxidative phosphorylation (OXPHOS) electron transport chain complexes I through V (MitoProfile Total OXPHOS Rodent WB Antibody Cocktail; Abcam, Cambridge, MA), NAD-dependent deacetylase sirtuin-1 (Sirt1; Santa Cruz Biotechnology, Santa Cruz, CA), NAD-dependent deacetylase sirtuin-3 (Sirt3; Cell Signaling, Beverly, MA), microsomal triglyceride transfer protein (MTTP; Santa Cruz Biotechnology), apolipoprotein B100 (apoB100; Abcam), fatty acid synthase (FAS, Cell Signaling), acetyl-CoA carboxylase (ACC; Cell Signaling), sterol regulatory element binding protein (SREBP-1c; Santa Cruz Biotechnology), protein kinase B (Akt; Cell Signaling), and phospho-Akt Ser473 (Cell Signaling) (19 (link),27 (link)). Membranes stained with 0.1% amido-black (Sigma-Aldrich) were quantified to control for differences in protein loading or transfer of band densities, as previously described (19 (link)).

Aroor A.R., Habibi J., Ford D.A., Nistala R., Lastra G., Manrique C., Dunham M.M., Ford K.D., Thyfault J.P., Parks E.J., Sowers J.R, & Rector R.S. (2015). Dipeptidyl Peptidase-4 Inhibition Ameliorates Western Diet–Induced Hepatic Steatosis and Insulin Resistance Through Hepatic Lipid Remodeling and Modulation of Hepatic Mitochondrial Function. Diabetes, 64(6), 1988-2001.

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Western Blot Analysis of Metabolic Regulators

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Western blot analyses were performed to determine protein content of the following: oxidative phosphorylation (OXPHOS) electron transport chain complexes I through V (MitoProfile Total OXPHOS Rodent WB Antibody Cocktail; Abcam, Cambridge, MA.), peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α; EMD Millipore Corp., Billerica, MA), NAD-dependent deacetylase sirtuin-1 (SIRT1; Santa Cruz Biotechnology, Santa Cruz, CA), NAD-dependent deacetylase sirtuin-3 (SIRT3; Cell Signaling, Beverly, MA), cAMP-responsive Element-binding Protein (CREB and phospho-CREB(Ser133); Cell Signaling), AMP-activated protein kinase(AMPK and phospho-AMPK (Thr 172); Cell Signaling), and cytochrome c (Cell Signaling). Phosphorylation status (using phosphospecific antibodies) was calculated from the density of the phosphoprotein band divided by density of the total protein using the appropriate antibody (30 (link), 31 (link)). Membranes stained with 0.1% amido-black (Sigma) were quantified to control for differences in protein loading or transfer of band densities as previously described (31 (link)).

Fletcher J.A., Meers G.M., Linden M.A., Kearney M.L., Morris E.M., Thyfault J.P, & Rector R.S. (2014). Impact of Various Exercise Modalities on Hepatic Mitochondrial Function. Medicine and science in sports and exercise, 46(6), 1089-1097.

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