Recombinant Human SIRT3 protein (Tagged)
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Recombinant Human SIRT3 protein (Tagged) is a Human Full Length protein, in the 1 to 399 aa range, expressed in Escherichia coli, with >75%, suitable for SDS-PAGE.
View Alternative Names
SIR2L3, SIRT3, hSIRT3, NAD-dependent protein delactylase sirtuin-3, Regulatory protein SIR2 homolog 3, SIR2-like protein 3
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human SIRT3 protein (Tagged) (AB125586)
SDS Page analysis of ab125586 running at approximately 66 kDa.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
Specifications
Form
Liquid
Additional notes
Purity was determined to be >75% by densitometry.
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, PubMed : 38146092). Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA, MRPL12 and the ATP synthase subunit ATP5PO (PubMed : 16788062, PubMed : 18680753, PubMed : 19535340, PubMed : 24121500, PubMed : 24252090, PubMed : 38146092). 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 recognizing other acyl groups, such as benzoyl and lactoyl, leading to protein debenzoylation and delactylation, respectively (PubMed : 39524354, PubMed : 36896611, PubMed : 37720100). Catalyzes debenzoylation of PPIF and ACLY (PubMed : 37720100). Mediates delactylation of 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.
Target data
Product promise
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