Human SIRT3 peptide

Name: Human SIRT3 peptide
SKU: DAG-P1120
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Nature

Synthetic

Tag/Conjugate

Unconjugated

SequenceSimilarities

SIRT3 peptide corresponds to 12 amino acids of SIRT3.

Purity

> 95 % by SDS-PAGE.

Format

Lyophilized

Preservative

None

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.

Reconstitution

SIRT3 peptide is supplied as 1mg of dried peptide. When the peptide is reconstituted in 1 mL strile water, the concentration will be 1 mg/mL.

Introduction

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 I of the sirtuin family. Two alternatively spliced transcript variants that encode different proteins have been described for this gene. [provided by RefSeq, Jul 2008]

Entrez Gene ID

23410

Synonyms

SIRT3; sirtuin 3; SIR2L3; NAD-dependent protein deacetylase sirtuin-3, mitochondrial; sir2-like 3; sirtuin type 3; SIR2-like protein 3; regulatory protein SIR2 homolog 3; NAD-dependent deacetylase sirtuin-3, mitochondrial; silent mating type information regulation 2, S.cerevisiae, homolog 3; mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase;

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Mitochondria as Target for Tumor Management of Hemangioendothelioma

ANTIOXIDANTS & REDOX SIGNALING

Authors: Gordillo, Gayle M.; Biswas, Ayan; Singh, Kanhaiya; Sen, Abhishek; Guda, Poornachander R.; Miller, Caroline; Pan, Xueliang; Khanna, Savita; Cadenas, Enrique; Sen, Chandan K.

Abstract

Aims:Hemangioendothelioma (HE) may be benign or malignant. Mouse hemangioendothelioma endothelial (EOMA) cells are validated to study mechanisms in HE. This work demonstrates that EOMA cells heavily rely on mitochondria to thrive. Thus, a combination therapy, including weak X-ray therapy (XRT, 0.5 Gy) and a standardized natural berry extract (NBE) was tested. This NBE is known to be effective in managing experimental HE and has been awarded with the Food and Drug Administration Investigational New Drug (FDA-IND) number 140318 for clinical studies on infantile hemangioma. Results:NBE treatment alone selectively attenuated basal oxygen consumption rate of EOMA cells. NBE specifically sensitized EOMA, but not murine aortic endothelial cells to XRT-dependent attenuation of mitochondrial respiration and adenosine triphosphate (ATP) production. Combination treatment, selectively and potently, influenced mitochondrial dynamics in EOMA cells such that fission was augmented. This was achieved by lowering of mitochondrial sirtuin 3 (SIRT3) causing increased phosphorylation of AMP-activated protein kinase (AMPK). A key role of SIRT3 in loss of EOMA cell viability caused by the combination therapy was evident when pyrroloquinoline quinone, an inducer of SIRT3, pretreatment rescued these cells. Innovation and Conclusion:Mitochondria-targeting NBE significantly extended survival of HE-affected mice. The beneficial effect of NBE in combination with weak X-ray therapy was, however, far more potent with threefold increase in murine survival. The observation that safe natural products may target tumor cell mitochondria and sharply lower radiation dosage required for tumor management warrants clinical testing.

Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse

BIOSCIENCE REPORTS

Authors: Weiss, Alexander K. H.; Naschberger, Andreas; Cappuccio, Elia; Metzger, Christina; Mottes, Lorenza; Holzknecht, Max; von Velsen, Jill; Bowler, Matthew W.; Rupp, Bernhard; Jansen-Duerr, Pidder

Abstract

FAH domain containing protein 1 (FAHD1) is a mammalian mitochondrial protein, displaying bifunctionality as acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. We report the crystal structure of mouse FAHD1 and structural mapping of the active site of mouse FAHD1. Despite high structural similarity with human FAHD1, a rabbit monoclonal antibody (RabMab) could be produced that is able to recognize mouse FAHD1, but not the human form, whereas a polyclonal antibody recognized both proteins. Epitope mapping in combination with our deposited crystal structures revealed that the epitope overlaps with a reported SIRT3 deacetylation site in mouse FAHD1.