Lane 1: mouse pancreas
Lane 2: SiHa
Lane 3: PC-3M
Rabbit polyclonal primary
macroH2A.1 Rabbit Polyclonal Antibody (ER1803-04)
Recombinant protein within human macroh2a.1 aa 190-372.
Mouse pancreas tissue, SiHa, PC-3M, human colon tissue, human placenta tissue, mouse brain tissue.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Protein affinity purified.
Core histone macro h2a.1 antibody; Core histone macro-H2A.1 antibody; H2A histone family member Y antibody; H2A.y antibody; H2A/y antibody; H2AF12M antibody; H2AFJ antibody; H2afy antibody; H2AY_HUMAN antibody; Histone H2A.Y antibody; Histone macroH2A1 antibody; Histone macroH2A1.1 antibody; Histone macroH2A1.2 antibody; Macroh2a1 antibody; MACROH2A1.1 antibody; MacroH2A1.2 antibody; Medulloblastoma antigen MU MB 50.205 antibody; Medulloblastoma antigen MU-MB-50.205 antibody; mH2a antibody; mH2A1 antibody
Monoubiquitinated at either Lys-116 or Lys-117. May also be polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 complex and does not promote proteasomal degradation. Instead, it is required for enrichment in inactive X chromosome chromatin.
Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin.