Recombinant production enables lot-to-lot consistency and is animal-cruelty-free
Western blot analysis of SIRT2 on human brain tissue lysates. Proteins were transferred to a PVDF membrane and blocked with 5% BSA in PBS for 1 hour at room temperature. The primary antibody (ET1701-43, 1/500) was used in 5% BSA at room temperature for 2 hours. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1:200,000 dilution was used for 1 hour at room temperature.
FLJ35621 antibody;FLJ37491 antibody;NAD dependent deacetylase sirtuin 2 antibody;NAD-dependent deacetylase sirtuin-2 antibody;NAD-dependent protein deacetylase sirtuin-2 antibody;Regulatory protein SIR2 homolog 2 antibody;Silencing information regulator 2 like antibody;Silent information regulator 2 antibody;SIR2 antibody;SIR2 like protein 2 antibody;Sir2 related protein type 2 antibody;SIR2, S. cerevisiae, homolog-loke 2 antibody;SIR2-like protein 2 antibody;SIR2L antibody;SIR2L2 antibody;SIRT2 antibody;SIRT2_HUMAN antibody;Sirtuin (silent mating type information regulation 2 homolog) 2 (S.cerevisiae) antibody;Sirtuin 2 antibody;Sirtuin type 2 antibody
Belongs to the sirtuin family. Class I subfamily.
Isoform 1 is expressed in heart, liver and skeletal muscle, weakly expressed in the cortex. Isoform 2 is strongly expressed in the cortex, weakly expressed in heart and liver. Weakly expressed in several malignancies including breast, liver, brain, kidney and prostate cancers compared to normal tissues. Weakly expressed in glioma cell lines compared to normal brain tissues (at protein level). Widely expressed. Highly expressed in heart, brain and skeletal muscle, while it is weakly expressed in placenta and lung. Down-regulated in many gliomas suggesting that it may act as a tumor suppressor gene in human gliomas possibly through the regulation of microtubule network.
Peaks during mitosis. After mitosis, it is probably degraded by the 26S proteasome.
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.
The silent information regulator (SIR2) family of genes are highly conserved from prokaryotes to eukaryotes and are involved in diverse processes, including transcriptional regulation, cell cycle progression, DNA-damage repair and aging. In S. cerevisiae, Sir2p deacetylates histones in a NAD-dependent manner, which regulates silencing at the telomeric, rDNA and silent mating-type loci. Sir2p is the founding member of a large family, designated sirtuins, which contain a conserved catalytic domain. The human homologs, which include SIRT1-7, are divided into four main branches: SIRT1-3 are class I, SIRT4 is class II, SIRT5 is class III and SIRT6-7 are class IV. SIRT proteins may function via mono-ADP-ribosylation of proteins. SIRT2 contains a 323 amino acid catalytic core domain with a NAD-binding domain and a large groove which is the likely site of catalysis.
Just like the interactions between antigens and antibodies, the higher the affinity between you and us the better.