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Cat. Number
070530371933317
Chemical Name
HDAC11 Polyclonal Antibody
References
Synonyms
  • Histone Deacetylase 11
Formulation 100 μg of protein G-purified IgG in 200 μl PBS containing 0.02% gelatin and 0.05 sodium azide
Stability 1 year
Storage -20°C
Shipping Wet ice in continental US; may vary elsewhere
Specificity
Human HDAC +
Murine HDAC11 +
Rat HDAC11 +

Background Reading

Nakayama, T., and Takami, Y. Participation of histones and histone-modifying enzymes in cell functions through alterations in chromatin structure. J Biochem 129 491-499 (2001).

Meinke, P.T., and Liberator, P. Histone deacetylase: A target for antiproliferative and antiprotozoal agents. Curr Med Chem 8(2) 211-235 (2001).

Gao, L., Cueto, M.A., Asselbergs, F., et al. Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J Biol Chem 277(28) 25748-25755 (2002).

Cress, W.D., and Seto, E.J. Histone deacetylases, transcriptional control, and cancer. J Cell Physiol 184 1-16 (2000).

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Size Global Purchasing
1 ea  

Description

Antigen: synthetic peptide from human HDAC11 amino acids (AHQGNGHERDFMDDKRVY) · Host: rabbit · Application(s): WB · Histone deacetylase (HDAC) and histone acetyltransferase (HAT) are enzymes that regulate transcription by selectively deacetylating or acetylating the ε-amino groups of lysines located near the amino termini of core histone proteins.1 Eleven members of HDAC family have been identified in the past several years.2,3 These HDAC family members are divided into two classes, I and II.The newest memeber of this family, HDAC11, has been cloned by Gao et al.4 HDAC11 transcripts were limited to kidney, heart, brain, skeletal muscle, and testis. These results suggested that each member of the HDAC family exhibits a different, individual substrate specificity and function in vivo.

1 Gao, L., Cueto, M.A., Asselbergs, F., et al. Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J Biol Chem 277(28) 25748-25755 (2002).

2 Meinke, P.T., and Liberator, P. Histone deacetylase: A target for antiproliferative and antiprotozoal agents. Curr Med Chem 8(2) 211-235 (2001).

3 Nakayama, T., and Takami, Y. Participation of histones and histone-modifying enzymes in cell functions through alterations in chromatin structure. J Biochem 129 491-499 (2001).

4 Cress, W.D., and Seto, E.J. Histone deacetylases, transcriptional control, and cancer. J Cell Physiol 184 1-16 (2000).

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