Sirtuin 4 (SIRT4) Peptide

Details for Product No. ABIN495214
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Protein Name
Application
Control Peptide (CP)
Pubmed 2 references available
Quantity 0.1 mg
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Catalog No. ABIN495214
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Specificity SIRT4 Antibody (C-term) Blocking Peptide
Alternative Name SIRT4
Background SIRT4 is 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.
Alternate names: NAD-Dependent ADP-Ribosyltransferase Sirtuin-4, SIR2-like 4, SIR2L4, SIRT-4, sirtuin (silent mating type information regulation 2 homolog) 4 (S. cerevisiae), sirtuin 4, sirtuin type 4, sirtuin-4
Molecular Weight 1875.52 Da.
Gene ID 23409
NCBI Accession NP_036372
UniProt Q9Y6E7
Research Area Chromatin and Nuclear Signaling, Metabolism, Proteases
Comment

This peptide is for ABIN358733

Restrictions For Research Use only
Format Lyophilized
Reconstitution Restore with 0.1 mL deionized water
Concentration 1,0 mg/mL
Buffer Lyophilized with 100% acetonitrile
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Prior to reconstitution store at 2-8°C. Following reconstitution store undiluted at 2-8°C for one month or (in aliquots) at-20°C for longer.
Expiry Date 12 months
Background publications Frye: "Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity." in: Biochemical and biophysical research communications, Vol. 260, Issue 1, pp. 273-9, 1999 (PubMed).

Frye: "Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins." in: Biochemical and biophysical research communications, Vol. 273, Issue 2, pp. 793-8, 2000 (PubMed).

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