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Sirtuin 2 (SIRT2) (C-Term) antibody

Details for Product No. ABIN500724, Supplier: Log in to see
Antigen
  • CG5085
  • D.mel2
  • Dmel\\CG5085
  • SIRT2
  • dSIRT2
  • sir2
  • Sirt2
  • BmSirt2
  • AtSRT2
  • SIRTUIN 2
  • T2K12.8
  • sirtuin 2
  • SIR2
  • SIR2L
  • SIR2L2
  • 5730427M03Rik
  • Sir2l
  • wu:fb57d05
  • zgc:55966
  • zgc:77003
Epitope
C-Term
33
16
6
5
5
3
3
3
3
3
2
2
1
1
1
1
1
1
Reactivity
Human, Mouse (Murine), Rat (Rattus)
110
50
49
4
3
3
2
2
1
1
1
1
1
Host
Rabbit
110
11
4
Clonality
Polyclonal
Conjugate
Un-conjugated
2
2
1
Application
Enzyme Immunoassay (EIA), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Western Blotting (WB)
110
56
35
18
10
8
6
4
4
1
1
1
Supplier
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Immunogen SIRT2 antibody was raised against a 19 amino acid peptide near the carboxy terminus of the Human SIRT2.
Isotype IgG
Specificity This antibody detects SIRT2 / SIR2 at C-term.
Cross-Reactivity (Details) Species reactivity (tested):Human, Mouse, Rat
Purification Peptide Affinity Chromatography
Alternative Name SIRT2 / SIR2 (SIRT2 Antibody Abstract)
Background The founding member of the sirtuin protein family was the silent information regulator 2 protein (Sir2p) of Saccharomyces cervisiae, an NAD+-dependent histone deacetylase (HDAC) that regulates chromatin silencing. The SIR2 family of genes are highly conserved from prokaryotes to eukaryotes. Mammals have seven homologs of Sir2p, SIRT1-7, which are involved in diverse processes ranging from transcriptional regulation, cell cycle progression and DNA-damage repair to aging. SIRT2 is a predominantly cytoplasmic protein that colocalizes with microtubules and can deacetylate ?-tubulin and regulate progression through the cell cycle. Most Sirtuins are highly expressed in brain and testis, while Sirt2 expression is higher in fetal relative to adult brain. Recent studies on SIRT2 support the therapeutic utility of inhibitors for the treatment of neurodegenerative diseases such as Parkinson's disease.Synonyms: NAD-dependent deacetylase sirtuin-2, SIR2-like protein 2, SIR2L, SIR2L2, SIRT-2, sirtuin (silent mating type information regulation 2 homolog) 2 (S. cerevisiae), sirtuin 2, sirtuin type 2, sirtuin-2
Gene ID 22933
NCBI Accession NP_036369
UniProt Q8IXJ6
Application Notes ELISA. Western blot: 1-2 μg/mL. Immunohistochemistry on Paraffin Sections. Positive Control: Mouse Brain Tissue Lysate.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Buffer PBS containing 0.02 % Sodium Azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C
Storage Comment Store the antibody undiluted at 2-8 °C.
Supplier Images
Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)) image for anti-Sirtuin 2 (SIRT2) (C-Term) antibody (ABIN500724) Immunohistochemical staining of human brain tissue using AP30785PU-N SIRT2 antibody a...
Western Blotting (WB) image for anti-Sirtuin 2 (SIRT2) (C-Term) antibody (ABIN500724) Western blot analysis of SIRT2 in Mouse brain lysate with AP30785PU-N SIRT2 antibody ...
Background publications Outeiro, Kontopoulos, Altmann et al.: "Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease." in: Science (New York, N.Y.), Vol. 317, Issue 5837, pp. 516-9, 2007 (PubMed).

Inoue, Hiratsuka, Osaki et al.: "The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation." in: Cell cycle (Georgetown, Tex.), Vol. 6, Issue 9, pp. 1011-8, 2007 (PubMed).

Yamamoto, Schoonjans, Auwerx: "Sirtuin functions in health and disease." in: Molecular endocrinology (Baltimore, Md.), Vol. 21, Issue 8, pp. 1745-55, 2007 (PubMed).

North, Marshall, Borra et al.: "The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase." in: Molecular cell, Vol. 11, Issue 2, pp. 437-44, 2003 (PubMed).

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).