Antibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations [0]
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- Product number
- ABIN967033 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Sirtuin 6 (SIRT6) (C-Term), (pTyr526), (pTyr527) antibody
- Antibody type
- Polyclonal
- Antigen
- Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human SIRT6 (Mono-ADP-ribosyltransferase sirtuin-6)
- Reactivity
- Human
- Epitope
- C-Term,pTyr526,pTyr527
- Vial size
- 0.1 mg
Submitted references SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span.
Regulation of SIRT6 protein levels by nutrient availability.
SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin.
A quantitative atlas of mitotic phosphorylation.
Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins.
Kawahara TL, Michishita E, Adler AS, Damian M, Berber E, Lin M, McCord RA, Ongaigui KC, Boxer LD, Chang HY, Chua KF
Cell 2009 Jan 9;136(1):62-74
Cell 2009 Jan 9;136(1):62-74
Regulation of SIRT6 protein levels by nutrient availability.
Kanfi Y, Shalman R, Peshti V, Pilosof SN, Gozlan YM, Pearson KJ, Lerrer B, Moazed D, Marine JC, de Cabo R, Cohen HY
FEBS letters 2008 Mar 5;582(5):543-8
FEBS letters 2008 Mar 5;582(5):543-8
SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin.
Michishita E, McCord RA, Berber E, Kioi M, Padilla-Nash H, Damian M, Cheung P, Kusumoto R, Kawahara TL, Barrett JC, Chang HY, Bohr VA, Ried T, Gozani O, Chua KF
Nature 2008 Mar 27;452(7186):492-6
Nature 2008 Mar 27;452(7186):492-6
A quantitative atlas of mitotic phosphorylation.
Dephoure N, Zhou C, Villén J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP
Proceedings of the National Academy of Sciences of the United States of America 2008 Aug 5;105(31):10762-7
Proceedings of the National Academy of Sciences of the United States of America 2008 Aug 5;105(31):10762-7
Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins.
Frye RA
Biochemical and biophysical research communications 2000 Jul 5;273(2):793-8
Biochemical and biophysical research communications 2000 Jul 5;273(2):793-8
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