Recombinant Mouse Nad-Dependent Protein Deacetylase Sirtuin-3 (SIRT3) Protein (His&Myc)

Name: Recombinant Mouse Nad-Dependent Protein Deacetylase Sirtuin-3 (SIRT3) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00948P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Nad-Dependent Protein Deacetylase Sirtuin-3 (SIRT3) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q8R104
Target Symbol	SIRT3
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MVGAGISTPSGIPDFRSPGSGLYSNLQQYDIPYPEAIFELGFFFHNPKPFFMLAKELYPGHYRPNVTHYFLRLLHDKELLLRLYTQNIDGLERASGIPASKLVEAHGTFVTATCTVCRRSFPGEDIWADVMADRVPRCPVCTGVVKPDIVFFGEQLPARFLLHMADFALADLLLILGTSLEVEPFASLSEAVQKSVPRLLINRDLVGPFVLSPRRKDVVQLGDVVHGVERLVDLLGWTQELLDLMQRERGKLDGQDR
Expression Range	78-334aa
Protein Length	Partial
Mol. Weight	36.3 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	NAD-dependent protein deacetylase. Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues. Known targets include ACSS1, IDH, GDH, PDHA1, SOD2, LCAD, SDHA and the ATP synthase subunit ATP5PO. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels. In response to metabolic stress, deacetylates transcription factor FOXO3 and recruits FOXO3 and mitochondrial RNA polymerase POLRMT to mtDNA to promote mtDNA transcription. Acts as a regulator of ceramide metabolism by mediating deacetylation of ceramide synthases CERS1, CERS2 and CERS6, thereby increasing their activity and promoting mitochondrial ceramide accumulation.
Subcellular Location	[Isoform L]: Mitochondrion matrix.; [Isoform S]: Cytoplasm.
Protein Families	Sirtuin family, Class I subfamily
Database References	KEGG: mmu:64384 STRING: 10090.ENSMUSP00000026559 UniGene: PMID: 29574628 data indicate a specific action of the shorter SIRT3 isoform on lipid mitochondrial membrane biosynthesis and functioning. PMID: 29589261 Using the cre-loxP system, we overexpressed the mitochondrial NAD(+) dependent protein deacetylase SIRT3 in enterocytes of mice (iSIRT3 mice). We chronically fed iSIRT3 mice and floxed-SIRT3 control (S3fl) mice a low-fat, control diet (CD) or a high-fat diet (HFD) and then phenotyped the mice. There were no genotype differences in any of the parameters tested when the mice were fed CD. PMID: 29031725 the protective effects of Polydatin are associated with the up-regulation of autophagy and improvement of mitochondrial biogenesis through Sirt3 activity. PMID: 27613967 High-fat-mediated liver damage is associated with Sirt3 downregulation, which is followed by ERK-CREB pathway inactivation and Bnip3-mediated inhibition of mitophagy, causing hepatocytes to undergo mitochondria-dependent cell death. PMID: 30056271 Aerobic interval training (AIT) attenuates high-fat-diet (HFD) -associated cognitive dysfunction through SIRT3 upregulation and improvement of antioxidative MnSOD activity. PMID: 29765980 Low SIRT3 expression is associated with Acute respiratory distress syndrome. PMID: 30171880 SIRT3 inhibited hyperoxia-induced ALI. As a mitochondrial protein, SIRT3 enhanced the expression of MnSOD and reduced the oxidative injury caused by hyperoxic exposure. PMID: 29363727 Activating SIRT3-mediated deacetylation of cyclophilin D attenuated learning and memory dysfunction induced by Sepsis-Associated Encephalopathy. PMID: 28236057 SIRT3 activated mitophagy protecting AFSCs against high glucose-induced apoptosis via preserving mitochondrial function and improved the abnormalities in glucose metabolic parameters, including the levels of glucose, insulin, C-peptide, HbA1c and inflammatory markers. PMID: 29689547 SIRT3 drives Pink1/Parkin activity to increase rates of mitophagy in response to oxidative stress, and thereby limits the production of damaging ROS that would further promote angiogenesis and cardiac remodeling. PMID: 28862956 In this review, the expression of mitochondrial SIRT3 is altered in skeletal muscle of a mouse model of neurodegenerative disease. PMID: 28449871 These results implicate a role of SIRT3 in modulating endothelial function and cardiac function. PMID: 28935506 Results suggest that sirtuin 3 (SIRT3) plays a protective role against mitochondrial damage in the kidney by attenuating reactive oxygen species (ROS) production. PMID: 27620507 SIRT3-deficient macrophages displayed impaired autophagy and accelerated NLRP3 inflammasome activation and endothelial dysfunction. PMID: 29277324 CD38 plays an essential role in cardiac hypertrophy probably via inhibition of SIRT3 expression and activation of Ca(2+) -NFAT signaling pathway. PMID: 28296029 results demonstrate for the first time that melatonin treatment ameliorates myocardial ischemia reperfusion injury by reducing oxidative stress and apoptosis via activating the SIRT3 signaling pathway. PMID: 28500761 The results suggest that melatonin alleviates cardiac remodeling and dysfunction in diabetic cardiomyopathy by upregulating autophagy, limiting apoptosis, and modulating mitochondrial integrity and biogenesis. The mechanisms are associated with Mst1/Sirt3 signaling. PMID: 28480597 EphB2 signaling-mediated Sirt3 expression reduces mesenchymal stem cells senescence by maintaining mitochondrial reactive oxygen species homeostasis. PMID: 28687409 Sirt3 plays a protective role against oxidative stress in oocytes exposed to maternal diabetes through deacetylating SOD2K68. PMID: 28662362 our findings implicate that a novel SIRT3-KLF15 signaling may prevent kidney injury from hypertension and HKL can act as a SIRT3-KLF15 signaling activator to protect against hypertensive nephropathy. PMID: 28465484 Study provides evidence that present that Sirt3 expression protected pancreatic beta cells from lipotoxicity by antagonizing oxidative stress-induced cell damage. PMID: 28375738 The authors provide evidence that inactivation of PIKfyve by the selective inhibitor STA suppresses excessive mitochondrial reactive oxygen species production and apoptosis through a SIRT3-dependent pathway in cardiomyoblasts. PMID: 28396567 Since mitochondrial ATP regeneration is inevitably linked to the maintenance of cardiac pump function, it is not surprising that recent studies revealed a role for mitochondrial sirtuins in the regulation of myocardial energetics and function. In addition, mitochondrial sirtuins modulate the extent of myocardial ischemia reperfusion injury and the development of cardiac hypertrophy and failure. [review] PMID: 27295248 conclude that Sirt3 does not considerably impact NET formation, platelet function, or venous thrombosis in healthy young mice PMID: 29236713 vitamin C and edaravone effectively protected macrophages from stress-induced cytotoxicity, accompanied by downregulated SIRT3 expression and AMPK phosphorylation, and decreased level of autophagy response. Taken together, we conclude that a SIRT3/AMPK/autophagy network orchestrates in the protective effect of resveratrol in macrophages. PMID: 27021965 Sirtuin 3 is required for osteogenic differentiation through maintenance of PGC-1a-SOD2-mediated regulation of mitochondrial function PMID: 28255277 findings reveal an unexpected mechanism for SIRT3 regulation via SIRT1-mediated deacetylation. Improving mitochondrial SIRT3 functions by inhibiting SIRT3 acetylation may offer a new therapeutic approach for obesity- and aging-related diseases associated with mitochondrial dysfunction. PMID: 28808064 Sirt3 expression in bone marrow cells increases during aging, suggesting that Sirt3 promotes age-related adipogenesis and osteoclastogenesis associated with bone loss. These findings identify Sirt3 as an important regulator of adipogenesis and skeletal homeostasis in vivo and identify Sirt3 as a potential target for the treatment of osteoporosis. PMID: 28911171 These data suggest a novel role for SIRT3 deficiency in mediating alveolar epithelial cell mtDNA damage, apoptosis, and lung fibrosis.- PMID: 28258190 Diminished Sirt3 expression and redox inactivation of Sirt3 led to SOD2 inactivation and contributes to hypertension. PMID: 28684630 Results reveal a potential mechanism by which SIRT3 deletion exacerbates post-MI cardiac dysfunction and impairment of cardiac recovery involving microvascular rarefaction and pre-existing coronary microvascular dysfunction. PMID: 27128560 expression and activity of the NADase CD38 increase with aging and that CD38 is required for the age-related NAD decline and mitochondrial dysfunction via a pathway mediated at least in part by regulation of SIRT3 activity. PMID: 27304511 These data demonstrate a critical role of SIRT3 in the control of myofibroblast differentiation and lung fibrosis. PMID: 27815257 NMNAT3 regulates the activity of SIRT3 via synthesis of mitochondria NAD. PMID: 27423420 Data show that peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1alpha) overexpression significantly increased the expression of sirtuin 3 (SIRT3) and sirtuin 5 (SIRT5). PMID: 27052737 These results suggest that the antiinflammatory phenotype of FABP4/aP2 null mice is mediated by increased intracellular monounsaturated fatty acids leading to the increased expression of both uncoupling protein 2 and SirT3. PMID: 26789108 despite pre-existing defects in cardiac function and mitochondrial respiratory capacity in SIRT3(-/-) mice, SIRT3 deficiency does not additionally impair cardiac function following myocardial ischemia-reperfusion injury or following myocardial infarction PMID: 26524632 In the cochlea, the expression of SIRT1, 3, and 5 (both mRNA and protein) was decreased in the old mice PMID: 26472659 SIRT3 plays pivotal roles in adaptive responses of neurons to physiological challenges and resistance to degeneration. PMID: 26698917 Sirt3 activation protects the heart from doxorubicin-induced cardiotoxicity by maintaining OGG1 levels and protecting mitochondria from DNA damage. PMID: 26873966 CerS1, -2, and -6 are hyperacetylated in the mitochondria of SIRT3-null mice. PMID: 26620563 as compared to Sirt3 overexpressed and normal groups, the acetylation of IDH2 and accumulation of ox-LDL were significantly higher in the Sirt3 inhibited group PMID: 26464666 Sirt3-dependent deacetylation of SOD2 plays a protective role against oxidative stress and meiotic defects in oocytes under maternal obese conditions. PMID: 25790176 A mouse model of developmentally primed nonalcoholic steatohepatitis is c characterized by an altered cellular redox status, sirtuin abundance and clock gene expression. PMID: 27040510 Sir3 dysfunction in Cmah-null mice altered various signaling pathways, which are responsible for age-related hearing loss. PMID: 26319214 Ischemic postconditioning might prevent lethal reperfusion injury through an increased SIRT3 activity and subsequent attenuation of CyPD acetylation at reperfusion. PMID: 25871830 SIRT3 and SIRT5 regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase PMID: 25811481 This study demonstrates the importance of SIRT3 in preserving heart function and capillary density in the setting of obesity. PMID: 25782072 SIRT3 functions as a protein repair factor that removes acetylation lesions from lysine residues. PMID: 26358839

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