Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
Purification
This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogène
This SIRT3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 250-279 amino acids from the C-terminal region of human SIRT3.
Takumida, Takumida, Katagiri, Anniko: "Localization of sirtuins (SIRT1-7) in the aged mouse inner ear." dans: Acta oto-laryngologica, pp. 1-12, (2015) (PubMed).
He, Hu, Shi, Weidert, Lu, Xu, Huang, Kelley, Xie: "Activation of the aryl hydrocarbon receptor sensitizes mice to nonalcoholic steatohepatitis by deactivating mitochondrial sirtuin deacetylase Sirt3." dans: Molecular and cellular biology, Vol. 33, Issue 10, pp. 2047-55, (2013) (PubMed).
Kamarajan, Alhazzazi, Danciu, Dsilva, Verdin, Kapila: "Receptor-interacting protein (RIP) and Sirtuin-3 (SIRT3) are on opposite sides of anoikis and tumorigenesis." dans: Cancer, Vol. 118, Issue 23, pp. 5800-10, (2012) (PubMed).
Parker, Vazquez-Manrique, Tourette, Farina, Offner, Mukhopadhyay, Orfila, Darbois, Menet, Tissenbaum, Neri: "Integration of ?-catenin, sirtuin, and FOXO signaling protects from mutant huntingtin toxicity." dans: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 32, Issue 36, pp. 12630-40, (2012) (PubMed).
Caton, Holness, Bishop-Bailey, Sugden: "PPAR?-LXR as a novel metabolostatic signalling axis in skeletal muscle that acts to optimize substrate selection in response to nutrient status." dans: The Biochemical journal, Vol. 437, Issue 3, pp. 521-30, (2011) (PubMed).
Xiong, Salazar, Patrushev, Alexander: "FoxO1 mediates an autofeedback loop regulating SIRT1 expression." dans: The Journal of biological chemistry, Vol. 286, Issue 7, pp. 5289-99, (2011) (PubMed).
Alhazzazi, Kamarajan, Joo, Huang, Verdin, DSilva, Kapila: "Sirtuin-3 (SIRT3), a novel potential therapeutic target for oral cancer." dans: Cancer, Vol. 117, Issue 8, pp. 1670-8, (2011) (PubMed).
Pillai, Sundaresan, Kim, Gupta, Rajamohan, Pillai, Samant, Ravindra, Isbatan, Gupta: "Exogenous NAD blocks cardiac hypertrophic response via activation of the SIRT3-LKB1-AMP-activated kinase pathway." dans: The Journal of biological chemistry, Vol. 285, Issue 5, pp. 3133-44, (2010) (PubMed).
Sundaresan, Gupta, Kim, Rajamohan, Isbatan, Gupta: "Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice." dans: The Journal of clinical investigation, Vol. 119, Issue 9, pp. 2758-71, (2009) (PubMed).
Sundaresan, Samant, Pillai, Rajamohan, Gupta: "SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70." dans: Molecular and cellular biology, Vol. 28, Issue 20, pp. 6384-401, (2008) (PubMed).
SIRT3 is 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 SIRT3 is included in class I of the sirtuin family.