SirT2 Antibody (YA5213)
(Synonyms: FLJ35621; FLJ37491; NAD dependent deacetylase sirtuin 2; NAD-dependent deacetylase sirtuin-2; NAD-dependent protein deacetylase sirtuin-2; Regulatory protein SIR2 homolog 2; Silencing information regulator 2 like; Silent information regulator 2; Silent mating type information regulation 2; Silent mating type information regulation 2 homolog; SIR 2; SIR2; SIR2 like; SIR2 like protein 2; Sir2 related protein type 2; SIR2, S. cerevisiae, homolog-loke 2; SIR2-like protein 2; SIR2L; SIR2L2; SIRT 2; SIRT2; SIRT2_HUMAN; Sirtuin; silent mating type information regulation 2 homolog; 2; S.cerevisiae; Sirtuin 2; Sirtuin type 2; Sirtuin2.)Based on 1 Customer Validation
SirT2 Antibody (YA5213) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to SirT2.
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Host:
Mouse
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Application:
WB, ICC/IF
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide, pH 7.3.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
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| Dilution Ratio | 1:500-1:1000 | 1:50-1:200 |
Product Details
SirT2 Antibody (YA5213) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to SirT2.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 43 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
Purified recombinant human SirT2 protein expressed in E.coli.
affinity chromatography.
Non-conjugated
Unmodified
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide, pH 7.3.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Verification Images
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Western blot analysis was performed on protein extracts (25 μg) from Mouse brain (lane 2) and Rat brain (lane 3) using SirT2 antibody. Proteins were transferred onto a 0.45 μm PVDF membrane using the Trans-Blot® Turbo™ system for 13 min. The membrane was then blocked with 5% nonfat milk in TBST (HY-K1025) for 1 h at room temperature. The primary antibody (1:1000) and loading control antibody GAPDH Antibody (HRP) (HY-P80954A) (1:5000) were diluted in 5% nonfat milk in TBST and incubated with the membrane overnight at 4°C. After washing, the membrane of primary antibody was incubated with HRP-conjugated goat anti-rabbit/mouse IgG secondary antibody (HY-P8001/HY-P8004) (1:5000) diluted in 5% nonfat milk in TBST for 1 h at room temperature. Protein bands were visualized using an Ultra High Sensitivity ECL detection kit (HY-K1005).
Background
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Function
SIRT2 is an NAD+-dependent sirtuin deacetylase with a catalytic core containing a Rossmann-fold NAD-binding domain and a zinc-binding module[1]. It functions as a cytoplasmic microtubule regulator by deacetylating α-tubulin Lys40 in vitro and in vivo, while SIRT2 knockdown causes tubulin hyperacetylation[2]. Mechanistically, SIRT2 also enters chromatin-linked cell-cycle control, because it deacetylates histone H4K16 during G2/M and supports mitotic chromatin regulation[3]. In cancer-relevant models, SIRT2 maintains genome integrity by deacetylating APC/C coactivators CDH1 and CDC20, and Sirt2 deficiency causes centrosome amplification, aneuploidy, and tumorigenesis in mice[4]. In neurodegeneration models, SIRT2 inhibition rescues α-synuclein toxicity and modifies inclusion morphology in cellular Parkinson’s disease models[5]. Compared with related sirtuin isoforms, SIRT2 shows distinctive cytoplasmic localization but undergoes active nuclear import controlled by its C-terminus and importins[6]. Isoform-level analysis is important because catalytically inactive nuclear SIRT2.5 antagonizes SIRT2.1 and SIRT2.2 effects on HBV replication from cccDNA[7]. For experimental applications, SIRT2 inhibitors support studies of microtubule acetylation, mitotic regulation, α-synuclein toxicity, viral chromatin control, and Myc-driven cancer signaling[2][4][5][7][8].
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Subcellular Localization
Nucleus; Cytoplasm, perinuclear region; Cytoplasm; Cytoplasm, cytoskeleton; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole; Cytoplasm, cytoskeleton, spindle; Midbody; Chromosome; Perikaryon; Cell projection; Cell projection, growth cone; Myelin membrane; Cytoplasm; Nucleus; Cytoplasm; Nucleus; Cytoplasm; Nucleus
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Expression
Tissue_specificity:Isomer 1 is expressed in the heart, liver, and skeletal muscle, and weakly in the cerebral cortex. Isomer 2 is expressed strongly in the cerebral cortex, and weakly in the heart and liver. Compared to normal tissues, it is expressed weakly in various malignancies, including breast cancer, liver cancer, brain cancer, kidney cancer, and prostate cancer. Compared to normal brain tissue, it is expressed weakly in glioma cell lines (protein level) . It is widely expressed. It is highly expressed in the heart, brain, and skeletal muscle, but weakly expressed in the placenta and lungs. Its expression is downregulated in many gliomas, suggesting that it may act as a tumor suppressor gene in human gliomas by regulating microtubule networks.
Induction:Up-regulated in response to low levels of glucose and anoxia-reoxygenation stress. Up-regulated by trichostatin A. Down-regulated in response to high levels of glucose. Down-regulated by histone deacetylation in several tumors -
Isoforms & Post-Translational Modification
Q8IXJ6 has 5 isomers: Q8IXJ6-1: 43182 Da (predicted); Q8IXJ6-2: 39515 Da (predicted); Q8IXJ6-3: 41353 Da (predicted); Q8IXJ6-4: 30379 Da (predicted); Q8IXJ6-5: 35654 Da (predicted).
Phosphorylated at phosphoserine and phosphothreonine. Phosphorylated at Ser-368 by a mitotic kinase CDK1/cyclin B at the G2/M transition; phosphorylation regulates the delay in cell-cycle progression. Phosphorylated at Ser-368 by a mitotic kinase G1/S-specific cyclin E/Cdk2 complex; phosphorylation inactivates SIRT2-mediated alpha-tubulin deacetylation and thereby negatively regulates cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Phosphorylated by cyclin A/Cdk2 and p35-Cdk5 complexes and to a lesser extent by the cyclin D3/Cdk4 and cyclin B/Cdk1, in vitro. Dephosphorylated at Ser-368 by CDC14A and CDC14B around early anaphase;Acetylated by EP300; acetylation leads both to the decreased of SIRT2-mediated alpha-tubulin deacetylase activity and SIRT2-mediated down-regulation of TP53 transcriptional activity;Ubiquitinated -
Subunit
Interacts with CDC20, FOXO3 and FZR1.
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SwissProt ID
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Synonyms
FLJ35621; FLJ37491; NAD dependent deacetylase sirtuin 2; NAD-dependent deacetylase sirtuin-2; NAD-dependent protein deacetylase sirtuin-2; Regulatory protein SIR2 homolog 2; Silencing information regulator 2 like; Silent information regulator 2; Silent mating type information regulation 2; Silent mating type information regulation 2 homolog; SIR 2; SIR2; SIR2 like; SIR2 like protein 2; Sir2 related protein type 2; SIR2, S. cerevisiae, homolog-loke 2; SIR2-like protein 2; SIR2L; SIR2L2; SIRT 2; SIRT2; SIRT2_HUMAN; Sirtuin; silent mating type information regulation 2 homolog; 2; S.cerevisiae; Sirtuin 2; Sirtuin type 2; Sirtuin2.
Documentation
References
[1]. Finnin MS, et al. Structure of the histone deacetylase SIRT2. Nat Struct Biol. 2001 Jul;8(7):621-5. [Content Brief]
[2]. North BJ, et al. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell. 2003 Feb;11(2):437-44. [Content Brief]
[3]. Vaquero A, et al. SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev. 2006 May 15;20(10):1256-61. [Content Brief]
[4]. Kim HS, et al. SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity. Cancer Cell. 2011 Oct 18;20(4):487-99. [Content Brief]
[5]. Outeiro TF, et al. Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease. Science. 2007 Jul 27;317(5837):516-9. [Content Brief]
[6]. Eldridge MJG, et al. Active nuclear import of the deacetylase Sirtuin-2 is controlled by its C-terminus and importins. Sci Rep. 2020 Feb 10;10(1):2034. [Content Brief]
[7]. Piracha ZZ, et al. An Alternatively Spliced Sirtuin 2 Isoform 5 Inhibits Hepatitis B Virus Replication from cccDNA by Repressing Epigenetic Modifications Made by Histone Lysine Methyltransferases. J Virol. 2020 Jul 30;94(16):e00926-20. [Content Brief]
[8]. Brady JJ, et al. An Arntl2-Driven Secretome Enables Lung Adenocarcinoma Metastatic Self-Sufficiency. Cancer Cell. 2016 May 9;29(5):697-710. [Content Brief]