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AB118334

Anti-SIRT3 antibody

3

(4 Reviews)

|

(12 Publications)

Goat Polyclonal SIRT3 antibody. Suitable for WB and reacts with Mouse, Caenorhabditis elegans samples. Cited in 12 publications. Immunogen corresponding to Synthetic Peptide within Mouse Sirt3 aa 50-150.

View Alternative Names

Sir2l3, Sirt3, NAD-dependent protein deacetylase sirtuin-3, NAD-dependent protein delactylase sirtuin-3, Regulatory protein SIR2 homolog 3, SIR2-like protein 3, mSIR2L3

1 Images
Western blot - Anti-SIRT3 antibody (AB118334)
  • WB

Unknown

Western blot - Anti-SIRT3 antibody (AB118334)

An additional band of unknown identity was also consistently observed at 15kDa. This band was successfully blocked by incubation with the immunizing peptide.

All lanes:

Western blot - Anti-SIRT3 antibody (ab118334) at 0.3 µg/mL

All lanes:

Mouse Heart lysate (in RIPA buffer) at 35 µg

Predicted band size: 43 kDa

true

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Caenorhabditis elegans

Applications

WB

applications

Immunogen

Synthetic Peptide within Mouse Sirt3 aa 50-150. The exact immunogen used to generate this antibody is proprietary information.

Q8R104

Specificity

ab118334 is expected to recognize both reported isoforms (NP_071878.2; NP_001171275.1). Reported variants represent identical proteins: NP_071878.2; NP_001120823.1.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
ab118334 is purified from Goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide.
Storage buffer
pH: 7.3 Preservative: 0.02% Sodium azide Constituents: 99% Tris buffered saline, 0.5% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

SIRT3 also known as Sirtuin 3 and mitochondrial sirtuin is a deacetylase with a mass of roughly 44 kDa. This protein is mostly found in the mitochondria where it regulates the acetylation state of various substrates. It plays an important role in maintaining mitochondrial homeostasis by modifying protein activity. SIRT3 is evolutionarily conserved and highly expressed in tissues with high energy demand like the heart liver and brown adipose tissue.
Biological function summary

SIRT3 modulates energy homeostasis by deacetylating and regulating enzymes involved in metabolism. It is a part of the mitochondrial sirtuin family contributing to fatty acid oxidation and the antioxidant defense system. By targeting key metabolic enzymes SIRT3 directly impacts the tricarboxylic acid (TCA) cycle and oxidative phosphorylation processes. These functions highlight its role in maintaining energy efficiency and reducing reactive oxidative species.

Pathways

SIRT3 participates in vital metabolic pathways such as the TCA cycle and the urea cycle. It interacts with other proteins like MnSOD and IDH2 to enhance mitochondrial function and overall cellular metabolism. This helps control the balance between energy production and consumption integrating signals from the AMPK and NAD+-dependent pathways to coordinate responses to changes in energy availability.

SIRT3 has implications in metabolic syndrome and cancer. Reduced SIRT3 activity is associated with increased susceptibility to metabolic disturbances like obesity and type 2 diabetes. Its deficiency affects the regulation of ROS and metabolic adaptation linking it to tumorigenesis and cancer progression. As it connects with proteins like HIF-1α in hypoxic conditions SIRT3 plays a role in cellular adaptation to stress influencing disease progression.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

NAD-dependent protein deacetylase (PubMed : 17923681, PubMed : 18794531, PubMed : 21172655, PubMed : 23835326, PubMed : 26620563). Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues (PubMed : 17923681, PubMed : 18794531, PubMed : 21172655, PubMed : 23835326). Known targets include ACSS1, IDH, GDH, PDHA1, SOD2, LCAD, SDHA, MRPL12 and the ATP synthase subunit ATP5PO (PubMed : 16790548, PubMed : 18794531, PubMed : 21172655). Contributes to the regulation of the cellular energy metabolism (PubMed : 23835326, PubMed : 36804859). Important for regulating tissue-specific ATP levels (PubMed : 18794531, PubMed : 24252090). In response to metabolic stress, deacetylates transcription factor FOXO3 and recruits FOXO3 and mitochondrial RNA polymerase POLRMT to mtDNA to promote mtDNA transcription (PubMed : 23283301). 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 (PubMed : 26620563). Regulates hepatic lipogenesis (PubMed : 36804859). Uses NAD(+) substrate imported by SLC25A47, triggering downstream activation of PRKAA1/AMPK-alpha signaling cascade that ultimately downregulates sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance (PubMed : 36804859). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by recognizing other acyl groups, such as benzoyl and lactoyl, leading to protein debenzoylation and delactylation, respectively (By similarity). Catalyzes debenzoylation of PPIF and ACLY (By similarity). Mediates delactylation of CCNE2 and 'Lys-16' of histone H4 (H4K16la) (By similarity).
See full target information Sirt3

Publications (12)

Recent publications for all applications. Explore the full list and refine your search

PloS one 18:e0291909 PubMed37816025

2023

Sirt3 deficiency promotes endothelial dysfunction and aggravates renal injury.

Applications

Unspecified application

Species

Unspecified reactive species

Anna Pezzotta,Luca Perico,Daniela Corna,Marina Morigi,Giuseppe Remuzzi,Ariela Benigni,Barbara Imberti

Cells 11: PubMed36291179

2022

Low Nephron Number Induced by Maternal Protein Restriction Is Prevented by Nicotinamide Riboside Supplementation Depending on Sirtuin 3 Activation.

Applications

Unspecified application

Species

Unspecified reactive species

Anna Pezzotta,Luca Perico,Marina Morigi,Daniela Corna,Monica Locatelli,Carlamaria Zoja,Ariela Benigni,Giuseppe Remuzzi,Barbara Imberti

Scientific reports 11:23580 PubMed34880332

2021

Post-translational modifications by SIRT3 de-2-hydroxyisobutyrylase activity regulate glycolysis and enable nephrogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Luca Perico,Marina Morigi,Anna Pezzotta,Daniela Corna,Valerio Brizi,Sara Conti,Cristina Zanchi,Fabio Sangalli,Piera Trionfini,Sara Buttò,Christodoulos Xinaris,Susanna Tomasoni,Carlamaria Zoja,Giuseppe Remuzzi,Ariela Benigni,Barbara Imberti

Oxidative medicine and cellular longevity 2021:5712280 PubMed34646424

2021

circFAM160A2 Promotes Mitochondrial Stabilization and Apoptosis Reduction in Osteoarthritis Chondrocytes by Targeting miR-505-3p and SIRT3.

Applications

Unspecified application

Species

Unspecified reactive species

Jiapeng Bao,Changjian Lin,Xing Zhou,Diana Ma,Lujie Ge,Kai Xu,Safwat Adel Abdo Moqbel,Yuzhe He,Chiyuan Ma,Jisheng Ran,Lidong Wu

Oxidative medicine and cellular longevity 2020:7517219 PubMed33062145

2020

Oleanolic Acid Decreases IL-1-Induced Activation of Fibroblast-Like Synoviocytes via the SIRT3-NF-B Axis in Osteoarthritis.

Applications

Unspecified application

Species

Unspecified reactive species

Jiapeng Bao,Weifeng Yan,Kai Xu,Mengyao Chen,Zhonggai Chen,Jisheng Ran,Yan Xiong,Lidong Wu

Frontiers in pharmacology 11:584 PubMed32508629

2020

Trilobatin Protects Against Aβ-Induced Hippocampal HT22 Cells Apoptosis Through Mediating ROS/p38/Caspase 3-Dependent Pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Nana Chen,Jiao Wang,Yuqi He,Yingshu Xu,Yuchuan Zhang,Qihai Gong,Changyin Yu,Jianmei Gao

International journal of molecular sciences 21: PubMed32210194

2020

Effect of a Resveratrol/Quercetin Mixture on the Reversion of Hypertension Induced by a Short-Term Exposure to High Sucrose Levels Near Weaning and a Long-Term Exposure That Leads to Metabolic Syndrome in Rats.

Applications

Unspecified application

Species

Unspecified reactive species

Vicente Castrejón-Téllez,Mariana Villegas-Romero,María Esther Rubio-Ruiz,Israel Pérez-Torres,Elizabeth Carreón-Torres,Eulises Díaz-Díaz,Verónica Guarner-Lans

Cell death & disease 11:83 PubMed32015327

2020

α-Linolenic acid but not linolenic acid protects against hypertension: critical role of SIRT3 and autophagic flux.

Applications

Unspecified application

Species

Unspecified reactive species

Guohua Li,Xinpei Wang,Hongyan Yang,Pengfei Zhang,Fangqin Wu,Yunchu Li,Yingjie Zhou,Xing Zhang,Heng Ma,Wei Zhang,Jia Li

Nutrients 11: PubMed30717220

2019

Effect of Sucrose Ingestion at the End of a Critical Window that Increases Hypertension Susceptibility on Peripheral Mechanisms Regulating Blood Pressure in Rats. Role of Sirtuins 1 and 3.

Applications

Unspecified application

Species

Unspecified reactive species

Vicente Castrejón-Téllez,Mariana Villegas-Romero,Israel Pérez-Torres,Gabriela Zarco,María Esther Rubio-Ruiz,Elizabeth Carreón-Torres,Eulises Díaz-Díaz,Oscar Emanuel Grimaldo,Verónica Guarner-Lans

Journal of neuropathology and experimental neurology 78:65-77 PubMed30481326

2018

Combined Adipose-Derived Mesenchymal Stem Cells and Low-Energy Extracorporeal Shock Wave Therapy Protect the Brain From Brain Death-Induced Injury in Rat.

Applications

Unspecified application

Species

Unspecified reactive species

Kuan-Hung Chen,Hao-Yi Hsiao,Christopher Glenn Wallace,Kun-Chen Lin,Yi-Chen Li,Tien-Hung Huang,Chi-Ruei Huang,Yi-Ling Chen,Chi-Wen Luo,Fan-Yen Lee,Hon-Kan Yip
View all publications

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