Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|H, M, R||FC, ICC, IHC, IH(P), IP, WB||Rb||Culture Supernatant||Monoclonal Antibody|
|Presentation||Unpurified rabbit monoclonal IgG in buffer containing 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Safety Information according to GHS|
|Material Size||100 µL|
|Anti-HDAC2, clone Y461 - 2378176||2378176|
|Anti-HDAC2, clone Y461 - 2446688||2446688|
|Anti-HDAC2, clone Y461 - 2453127||2453127|
|Anti-HDAC2, clone Y461 - 2068519||2068519|
|Anti-HDAC2, clone Y461 - 2161088||2161088|
|Anti-HDAC2, clone Y461 - 2275531||2275531|
|Anti-HDAC2, clone Y461 - DAM1621688||DAM1621688|
|Anti-HDAC2, clone Y461 - NG1572368||NG1572368|
|Anti-HDAC2, clone Y461 - NG1853926||NG1853926|
|Reference overview||Pub Med ID|
|HDAC2 blockade by nitric oxide and histone deacetylase inhibitors reveals a common target in Duchenne muscular dystrophy treatment.|
Colussi, Claudia, et al.
Proc. Natl. Acad. Sci. U.S.A., 105: 19183-7 (2008) 2008
The overlapping histological and biochemical features underlying the beneficial effect of deacetylase inhibitors and NO donors in dystrophic muscles suggest an unanticipated molecular link among dystrophin, NO signaling, and the histone deacetylases (HDACs). Higher global deacetylase activity and selective increased expression of the class I histone deacetylase HDAC2 were detected in muscles of dystrophin-deficient MDX mice. In vitro and in vivo siRNA-mediated down-regulation of HDAC2 in dystrophic muscles was sufficient to replicate the morphological and functional benefits observed with deacetylase inhibitors and NO donors. We found that restoration of NO signaling in vivo, by adenoviral-mediated expression of a constitutively active endothelial NOS mutant in MDX muscles, and in vitro, by exposing MDX-derived satellite cells to NO donors, resulted in HDAC2 blockade by cysteine S-nitrosylation. These data reveal a special contribution of HDAC2 in the pathogenesis of Duchenne muscular dystrophy and indicate that HDAC2 inhibition by NO-dependent S-nitrosylation is important for the therapeutic response to NO donors in MDX mice. They also define a common target for independent pharmacological interventions in the treatment of Duchenne muscular dystrophy.
|HDAC2 deficiency and histone acetylation.|
Ree, Anne Hansen, et al.
Nat. Genet., 40: 812-3; author reply 813 (2008) 2008
|S-Nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons.|
Nott, Alexi, et al.
Nature, 455: 411-5 (2008) 2008