SIRT2 sirna

SIRT2 siRNA (Mouse)

Cat. Num. AAA8233539

• Gene Names: Sirt2; Sir2l; SIR2L2; 5730427M03Rik
• Reactivity: Mouse
• Applications: RNA Interference (RNAi)
• Purity: > 97%
• Synonyms: SIRT2; SIRT2 siRNA (Mouse); SIR2L2; NAD-dependent protein deacetylase sirtuin-2; Regulatory protein SIR2 homolog 2; SIR2-like protein 2; mSIR2L2; SIRT2 sirna

• Host: Synthetic
• Reactivity: Mouse
• Specificity: SIRT2 siRNA (Mouse) is a target-specific 19-23 nt siRNA oligo duplexes designed to knock down gene expression.
• Purity/Purification: > 97%
• Form/Format: Lyophilized powder
• Sequence Length: 352

• Applicable Applications for SIRT2 sirna: RNA Interference (RNAi)
• Quality Control: Oligonucleotide synthesis is monitored base by base through trityl analysis to ensure appropriate coupling efficiency. The oligo is subsequently purified by affinity-solid phase extraction. The annealed RNA duplex is further analyzed by mass spectrometry to verify the exact composition of the duplex. Each lot is compared to the previous lot by mass spectrometry to ensure maximum lot-to-lot consistency.
• Directions for Use: We recommends transfection with 100 nM siRNA 48 to 72 hours prior to cell lysis. Before resuspending, briefly centrifuge the tube to ensure the lyophilized siRNA is at the bottom of the tube. Resuspend the siRNA oligos to an appropriate concentration with DEPC water. For each vial, suitable for 250 transfections in 24 well plate (20 pmol for each well).
• Components: We offer pre-designed sets of 3 different target-specific siRNA oligo duplexes of mouse SIRT2 gene. Each vial contains 5 nmol of lyophilized siRNA. The duplexes can be transfected individually or pooled together to achieve knockdown of the target gene, which is most commonly assessed by qPCR or western blot. Our siRNA oligos are also chemically modified (2'-OMe) at no extra charge for increased stability and enhanced knockdown in vitro and in vivo.
• Preparation and Storage: Shipped at 4 degree C. Store at -20 degree C for one year.

Related Product Information for SIRT2 sirna

siRNA to inhibit SIRT2 expression using RNA interference

NCBI and Uniprot Product Information

• NCBI GI #: 170650632
• NCBI GeneID: 64383
• NCBI Accession #: NP_001116237.1
• NCBI GenBank Nucleotide #: NM_001122765.1
• UniProt Accession #: Q8VDQ8; Q9CXS5; Q9EQ18; Q9ERJ9; E9PXF5; U5TP50
• Molecular Weight: 35,678 Da
• NCBI Official Full Name: NAD-dependent protein deacetylase sirtuin-2 isoform 2
• NCBI Official Synonym Full Names: sirtuin 2
• NCBI Official Symbol: Sirt2
• NCBI Official Synonym Symbols: Sir2l; SIR2L2; 5730427M03Rik
• NCBI Protein Information: NAD-dependent protein deacetylase sirtuin-2
• UniProt Protein Name: NAD-dependent protein deacetylase sirtuin-2
• Protein Family: NAD-dependent protein deacetylase
• UniProt Gene Name: Sirt2
• UniProt Synonym Gene Names: Sir2l2; mSIR2L2
• UniProt Entry Name: SIR2_MOUSE

Uniprot Description

SIRT2: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA. Interacts with HDAC6, suggesting that these proteins belong to a large complex that deacetylate the cytoskeleton. 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. Inhibited by Sirtinol, A3 and M15 small molecules. Inhibited by nicotinamide. Belongs to the sirtuin family. Class I subfamily. 4 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.5.1.-; Deacetylase

Cellular Component: microtubule; centrosome; lateral loop; paranode region of axon; perikaryon; chromosome; nuclear heterochromatin; cytosol; centriole; cytoskeleton; cell projection; membrane; perinuclear region of cytoplasm; cytoplasm; plasma membrane; spindle; midbody; nucleus; myelin sheath

Molecular Function: (3,5-dichlorophenylurea)acetate amidohydrolase activity; ubiquitin binding; hydrolase activity; zinc ion binding; metal ion binding; histone deacetylase binding; protein deacetylase activity; beta-tubulin binding; UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity; transcription factor binding; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; N-acetylgalactosamine-6-phosphate deacetylase activity; histone acetyltransferase binding; N2-acetyl-L-lysine deacetylase activity; protein binding; iprodione amidohydrolase activity; tubulin deacetylase activity; indoleacetamide hydrolase activity; protein N-terminal asparagine amidohydrolase activity; NAD-dependent histone deacetylase activity (H4-K16 specific); chromatin binding; histone deacetylase activity; O-succinylbenzoate synthase activity; NAD binding

Biological Process: proteasomal ubiquitin-dependent protein catabolic process; negative regulation of autophagy; phosphoinositide 3-kinase cascade; regulation of myelination; regulation of fat cell differentiation; regulation of cell cycle; positive regulation of attachment of spindle microtubules to kinetochore; negative regulation of transcription from RNA polymerase II promoter; negative regulation of cell proliferation; protein amino acid deacetylation; regulation of transcription, DNA-dependent; meiotic cell cycle; cellular lipid catabolic process; protein kinase B signaling cascade; cell differentiation; positive regulation of DNA binding; nervous system development; mitosis; transcription, DNA-dependent; positive regulation of meiosis; hepatocyte growth factor receptor signaling pathway; histone deacetylation; negative regulation of fat cell differentiation; cell cycle; negative regulation of striated muscle development; myelination in the peripheral nervous system; negative regulation of oligodendrocyte differentiation; cell division; positive regulation of cell division; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; autophagy; positive regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; negative regulation of protein catabolic process; negative regulation of apoptosis