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AB97951

Recombinant Human SIRT3 protein (His tag N-Terminus)

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(1 Publication)

Recombinant Human SIRT3 protein (His tag N-Terminus) is a Human Fragment protein, in the 118 to 399 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

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

1 Images
SDS-PAGE - Recombinant Human SIRT3 protein (His tag N-Terminus) (AB97951)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human SIRT3 protein (His tag N-Terminus) (AB97951)

15% SDS-PAGE showing ab97951 at approximately 33.5kDa (3μg).

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

Q9NTG7

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

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

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMSDKGKLSLQDVAELIRARACQRVVVMVGAGISTPSGIPDFRSPGSGLYSNLQQYDLPYPEAIFELPFFFHNPKPFFTLAKELYPGNYKPNVTHYFLRLLHDKGLLLRLYTQNIDGLERVSGIPASKLVEAHGTFASATCTVCQRPFPGEDIRADVMADRVPRCPVCTGVVKPDIVFFGEPLPQRFLLHVVDFPMADLLLILGTSLEVEPFASLTEAVRSSVPRLLINRDLVGPLAWHPRSRDVAQLGDVVHGVESLVELLGWTEEMRDLVQRETGKLDGPDK","proteinLength":"Fragment","predictedMolecularWeight":"33.5 kDa","actualMolecularWeight":null,"aminoAcidEnd":399,"aminoAcidStart":118,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9NTG7","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

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.

Specifications

Form

Liquid

Additional notes

ab97951 is purified using conventional chromatography techniques.

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

Product protocols

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

Publications (1)

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

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
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