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AB125810

Recombinant human SIRT3 protein

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(1 Publication)

Recombinant human SIRT3 protein is a Human Fragment protein, in the 47 to 399 aa range, expressed in Baculovirus infected Sf9 cells, with >70%, suitable for SDS-PAGE, FuncS.

View Alternative Names

SIR2L3, SIRT3, hSIRT3, NAD-dependent protein delactylase sirtuin-3, Regulatory protein SIR2 homolog 3, SIR2-like protein 3

4 Images
Functional Studies - Recombinant human SIRT3 protein (AB125810)
  • FuncS

Unknown

Functional Studies - Recombinant human SIRT3 protein (AB125810)

The specific activity of ab125810 was determined to be 150 RLU/min/mg.

Functional Studies - Recombinant human SIRT3 protein (AB125810)
  • FuncS

Unknown

Functional Studies - Recombinant human SIRT3 protein (AB125810)

The specific activity of SIRT3 (ab125810) was determined to be 145 RLU/min/mg as per activity assay protocol

SDS-PAGE - Recombinant human SIRT3 protein (AB125810)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human SIRT3 protein (AB125810)

SDS-PAGE analysis of ab125810.

SDS-PAGE - Recombinant human SIRT3 protein (AB125810)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human SIRT3 protein (AB125810)

SDS PAGE analysis of ab125810

Key facts

Purity

>70% Densitometry

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag C-Terminus

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

The specific activity of ab125810 was determined to be 150 RLU/min/mg.

Accession

Q9NTG7

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":"66 kDa","actualMolecularWeight":null,"aminoAcidEnd":399,"aminoAcidStart":47,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q9NTG7","tags":[{"tag":"GST","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True
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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.
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Specifications

Form

Liquid

Additional notes

Purity was determined to be >70% by densitometry. Affinity purified.

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General info

Function

NAD-dependent protein deacetylase (PubMed : 12186850, PubMed : 12374852, PubMed : 16788062, PubMed : 18680753, PubMed : 18794531, PubMed : 19535340, PubMed : 23283301, PubMed : 24121500, PubMed : 24252090). Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues (PubMed : 12186850, PubMed : 12374852, PubMed : 16788062, PubMed : 18680753, PubMed : 18794531, PubMed : 23283301, PubMed : 24121500, PubMed : 24252090). Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA and the ATP synthase subunit ATP5PO (PubMed : 16788062, PubMed : 18680753, PubMed : 19535340, PubMed : 24121500, PubMed : 24252090). Contributes to the regulation of the cellular energy metabolism (PubMed : 24252090). Important for regulating tissue-specific ATP levels (PubMed : 18794531). 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 (By similarity). Regulates hepatic lipogenesis (By similarity). 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 (By similarity). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by mediating delactylation of proteins, such as CCNE2 and 'Lys-16' of histone H4 (H4K16la) (PubMed : 36896611, PubMed : 37720100).

Sequence similarities

Belongs to the sirtuin family. Class I subfamily.

Post-translational modifications

Processed by mitochondrial processing peptidase (MPP) to give a 28 kDa product. Such processing is probably essential for its enzymatic activity.

Subcellular localisation

Mitochondrion matrix

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Product protocols

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Target data

NAD-dependent protein deacetylase (PubMed : 12186850, PubMed : 12374852, PubMed : 16788062, PubMed : 18680753, PubMed : 18794531, PubMed : 19535340, PubMed : 23283301, PubMed : 24121500, PubMed : 24252090). Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues (PubMed : 12186850, PubMed : 12374852, PubMed : 16788062, PubMed : 18680753, PubMed : 18794531, PubMed : 23283301, PubMed : 24121500, PubMed : 24252090). Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA and the ATP synthase subunit ATP5PO (PubMed : 16788062, PubMed : 18680753, PubMed : 19535340, PubMed : 24121500, PubMed : 24252090). Contributes to the regulation of the cellular energy metabolism (PubMed : 24252090). Important for regulating tissue-specific ATP levels (PubMed : 18794531). 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 (By similarity). Regulates hepatic lipogenesis (By similarity). 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 (By similarity). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by mediating delactylation of proteins, such as CCNE2 and 'Lys-16' of histone H4 (H4K16la) (PubMed : 36896611, PubMed : 37720100).
See full target information SIRT3
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Publications (1)

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

The Biochemical journal 474:2829-2839 PubMed28673962

2017

Potential mechanisms linking SIRT activity and hypoxic 2-hydroxyglutarate generation: no role for direct enzyme (de)acetylation.

Applications

Unspecified application

Species

Unspecified reactive species

Sergiy M Nadtochiy,Yves T Wang,Jimmy Zhang,Keith Nehrke,Xenia Schafer,Kevin Welle,Sina Ghaemmaghami,Josh Munger,Paul S Brookes
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