Human SIRT5 blocking peptide (CDBP2685)

Synthetic Human SIRT5 blocking peptide for BL

Product Overview
Blocking peptide for anti-SIRT5 antibody
Target
SIRT5
Nature
Synthetic
Species Reactivity
Human
Tag/Conjugate
Unconjugated
Application Notes
For in vitro research use only. Not intended for any diagnostic or therapeutic purpose. Not suitable for human or animal consumption.
Procedure
None
Format
Liquid
Concentration
200 μg/ml
Size
50 μg
Buffer
PBS containing 0.02% sodium azide
Preservative
0.02% Sodium Azide
Storage
Store at -20℃, stable for one year.
UniProt ID
Antigen Description
This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class III of the sirtuin family. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Jul 2010]
Function
NOT NAD+ ADP-ribosyltransferase activity; NAD+ binding; hydrolase activity; metal ion binding; protein-malonyllysine demalonylase activity; protein-succinyllysine desuccinylase activity; zinc ion binding;
Synonyms
SIRT5; sirtuin 5; sirtuin (silent mating type information regulation 2 homolog) 5 (S. cerevisiae) , sirtuin (silent mating type information regulation 2, S.cerevisiae, homolog) 5; NAD-dependent lysine demalonylase and desuccinylase sirtuin-5, mitochondrial; sir2-like 5; sirtuin type 5; SIR2-like protein 5; NAD-dependent deacetylase sirtuin-5; silent mating type information regulation 2, S.cerevisiae, homolog 5; SIR2L5; FLJ36950;

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References


Histone Deacetylase 11 Is an epsilon-N-Myristoyllysine Hydrolase

CELL CHEMICAL BIOLOGY

Authors: Moreno-Yruela, Carlos; Galleano, Iacopo; Madsen, Andreas S.; Olsen, Christian A.

Histone deacetylase (HDAC) enzymes regulate diverse biological function, including gene expression, rendering them potential targets for intervention in a number of diseases, with a handful of compounds approved for treatment of certain hematologic cancers. Among the human zinc-dependent HDACs, the most recently discovered member, HDAC11, is the only member assigned to subclass IV. It is the smallest protein and has the least well understood biological function. Here, we show that HDAC11 cleaves long-chain acyl modifications on lysine side chains with remarkable efficiency. We further show that several common types of HDAC inhibitors, including the approved drugs romidepsin and vorinostat, do not inhibit this enzymatic activity. Macrocyclic hydroxamic acid-containing peptides, on the other hand, potently inhibit HDAC11 demyris-toylation activity. These findings should be taken carefully into consideration in future investigations of the biological function of HDAC11 and will serve as a foundation for the development of selective chemical probes targeting HDAC11.

Functional genetic variants in the SIRT5 gene promoter in acute myocardial infarction

GENE

Authors: Chen, Lu; Wang, Haiyan; Gao, Feng; Zhang, Jie; Zhang, Yexin; Ma, Ruchao; Pang, Shuchao; Cui, Yinghua; Yang, Jian; Yan, Bo

Coronary artery disease (CAD) including acute myocardial infarction (AMI) is a common complex disease. To date, genetic causes for atherosclerosis remain largely unknown. It has recently been proposed that low frequency and rare genetic variants may be the main causes. Mitochondria] sirtuins, SIRT3, SIRT4 and SIRT5, function as critical regulators of mitochondrial metabolism, oxidative stress and cell survival. We speculated that altered SIRT5 level resulting from DNA sequence variants (DSVs) within SIRT5 gene regulatory regions may contribute to the CAD and AMI development. In this study, the SIRT5 gene promoter was genetically and functionally analyzed in large cohorts of AMI patients (n = 381) and healthy controls (n = 391). A total of eleven DSVs and SNPs were found. Two novel heterozygous DSVs (g.13574131C > A and g.13574287G > C) and three heterozygous SNPs [g.13573450A > G (rs573515169), g.13574110G > A (rs2804924) and g.13574259G > C (rs112443954)] were identified only in AMI patients. The DSVs and SNPs significantly decreased the transcriptional activity of the SIRT5 gene promoter in both HEK-293 and H9c2 cells (P < 0.05). Further electrophoretic mobility shift assay indicated that the SNPs significantly affected the binding of transcription factors. In contrast, the DSVs and SNPs found only in controls or in both AMI patients and controls did not significantly change the SIRT5 gene promoter activity (P > 0.05). Therefore, our data suggested that the DSVs and SNPs identified in AMI patients may change SIRT5 level by affecting activity of SIRT5 gene promoter, contributing to the AMI development as a risk factor.

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