Technical Data
SIRT1 (SIRT1 Sir2-like Proteins (Sirtuins) Type 1, Sirtuin, Sirtuin (Silent Mating Type Information Regulation 2 Homolog) 1 (S. cerevisiae), Sirtuin Type 1, BA57G10.4, hSIRT1, NAD-dependent Deacetylase SIRT1, NAD-dependent Deacetylase Sirtuin-1, SIR2-like
The S. cerevisiae silent information regulator 2 (Sir2) protein is an NAD+-dependent histone deacetylase (HDACs) that plays a critical role in transcriptional silencing, genome stability, and longevity (1-2). Part of the Sirtuin family (Sir2, Sir3, Sir3), yeast Sir2 is the founding member of Class III HDACs. A human homologue of Sir2 , SIRT1, regulates the activity of the p53 tumor suppressor and inhibits apoptosis (3-4).

Suitable for use in Flow Cytometry, Western Blot, Immunoprecipitation, Immunohistochemistry and Immunocytochemistry. Other applications not tested.

Recommended Dilution:
Flow Cytometry: 1:30
Western Blot: 1:1000 MW: 110kD
Immunohistochemistry: 1:50
Immunocytochemistry: 1:100
Immunoprecipitation: 1:40
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, aliquot and store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Manufactured incorporating RabMAb technology under Epitomics US patents, No 5,675,063 and 7,429,487, owned by Abcam.
100ul 4C (-20C Glycerol)Blue IceHumanRabbit
Not Determined
A synthetic peptide corresponding to residues near N-terminus and before Ala-rich domain of human Sir2.
Supplied as a liquid in 50mM Tris-Glycine, pH 7.4, 0.15M sodium chloride, 0.05% BSA, 0.01% sodium azide and 40% glycerol.
Recognizes human Sir2/SIRT1. Does not cross-react with other Sirtuin family members.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. David A. Sinclair et al; Inhibition of Silencing and Accelerated Aging by Nicotinamide, a Putative Negative Regulator of Yeast Sir2 and Human SIRT1*; J. Biol. Chem., Vol. 277, Issue 47, 45099-45107, November 22, 2002 Tony 2. Smith, J. S., Brachmann, C. B., Celic, I., Kenna, M. A., Muhammad, S., Starai, V. J., Avalos, J. L., Escalante-Semerena, J. C., Grubmeyer, C., Wolberger, C., and Boeke, J. D. (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 6658-6663 3. Kouzarides et al, Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence; The EMBO Journal, Vol. 21, No. 10 pp. 2383-2396, 2002 4. Tanner, K. G., Landry, J., Sternglanz, R., and Denu, J. M. (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 14178-14182