| References |
| Synonyms |
|
| Formulation |
100 μg of protein G-purified IgG in 200 μl PBS containing 0.05% BSA and 0.05% sodium azide |
| Stability |
1 year |
| Storage |
-20°C |
| Shipping |
Wet ice
in continental US; may vary elsewhere
|
| Specificity |
| Human HDAC4 |
+ |
| Murine HDAC4 |
+ |
|
Background Reading
Meinke, P.T., and Liberator, P. Histone deacetylase: A target for antiproliferative and antiprotozoal agents. Curr Med Chem 8(2) 211-235 (2001).
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).
Rioli, V., Gozzo, F.C., Heimann, A.S., et al. Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotension-converting enzyme. J Biol Chem 278(10) 8547-8555 (2003).
| Size |
Global Purchasing |
| 1 ea |
|
Description
Antigen:
synthetic peptide corresponding to amino acids 194-209 of human HDAC4
·
Host:
rabbit
·
Application(s):
WB, IP, and ChIP
·
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. HDAC4 is a member of the class II family which also includes HDACs 5, 6, and 7, the molecular weights of which are all about two-fold larger than those of the class I members.
1
Meinke, P.T., and Liberator, P. Histone deacetylase: A target for antiproliferative and antiprotozoal agents. Curr Med Chem 8(2) 211-235 (2001).
2
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).
3
Rioli, V., Gozzo, F.C., Heimann, A.S., et al. Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotension-converting enzyme. J Biol Chem 278(10) 8547-8555 (2003).
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