SIRT5 is a human member of a family of proteins called Sirtuins (Sir2-like proteins) and are 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 possibly at as mono-ADP-ribosyltransferases. The enzymatic function of sirtuins is not yet completely understood but recent reports of histone-activated Sir2-mediated NAD metabolism and NAD-activated Sir2-mediated histone deacetylation suggest a possible coupled reciprocal activation mechanism involving interactions of Sir2 with NAD and the N epsilon-acetyl-lysine groups of acetylated histones.
Background References
1. Teng P et al. SIRT5-mediated ME2 desuccinylation promotes cancer growth by enhancing mitochondrial respiration. Cell Death Differ. 2024 Jan
2. Wu M et al. Sirt5 improves cardiomyocytes fatty acid metabolism and ameliorates cardiac lipotoxicity in diabetic cardiomyopathy via CPT2 de-succinylation. Redox Biol. 2024 Jul
Proteins were transferred to a PVDF membrane and blocked with 5% NFDM/TBST for 1 hour at room temperature. The primary antibody (HA723774) at 1/2,000 dilution was used in primary antibody dilution (K1803) at 4℃ overnight. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1/50,000 dilution was used for 1 hour at room temperature.
Immunohistochemical analysis of paraffin-embedded human liver tissue with Rabbit anti-SIRT5 antibody (HA723774) at 1/1,000 dilution.
The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 20 minutes. The tissues were blocked in 1% BSA for 20 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody (HA723774) at 1/1,000 dilution for 1 hour at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
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