|Calculated MW||44898 Da|
|Other Names||SIR2; Sirtuin 7; Silent Information Regulator 7|
|Format||50 µg of antibody in 100 µl PBS containing 0.2% gelatin and 0.05% sodium azide|
|Handling||The antibody solution should be gently mixed before use.|
|Precautions||SIRT7 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||NAD-dependent protein deacetylase that specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays selectivity for a single histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors. SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. These data suggest that SIRT7 may play a key role in oncogenic transformation by suppresses expression of tumor suppressor genes by locus-specific deacetylation of H3K18Ac at promoter regions. Also required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis: promotes the association of RNA polymerase I with the rDNA promoter region and coding region. Stimulates transcription activity of the RNA polymerase I complex. May also deacetylate p53/TP53 and promotes cell survival, however such data need additional confirmation.|
|Cellular Location||Cytoplasm. Nucleus, nucleolus. Note=Located close to the nuclear membrane when in the cytoplasm. Associated with chromatin. Associated with rDNA promoter and transcribed region. Associated with nucleolar organizer regions during mitosis|
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Provided below are standard protocols that you may find useful for product applications.
The sirtuins represent a distinct class of trichostatin A-insensitive lysyl-deacetylases (class III HDACs) and have been shown to catalyze a reaction that couples lysine deacetylation to the formation of nicotinamide and O-acetyl-ADP-ribose from NAD+ and the abstracted acetyl group. SIRT7 is a member of this family of proteins and is present in prokaryotes and eukaryotes. All SIR2-like proteins have a sirtuin core domain, which contains a series of sequence motifs conserved in organisms ranging from bacteria to humans. Bacterial, yeast, and mammalian sirtuins are able to metabolize NAD+ and several act as mono-ADP-ribosyltransferases. The enzymatic function of sirtuins is not yet completely understood but as mentioned above, recent reports of histone-activated SIR2-mediated NAD+ metabolism and NAD+-activated SIR2-mediated histone deacetylation s µggest a possible coupled reciprocal activation mechanism involving interactions of SIR2 with NAD+ and the N-ε-acetyl-lysine groups of acetylated histone.
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