Human Histone H2A (asymmetric di methyl R3) peptide (ab22398)

Overview

Description

  • NatureSynthetic

Specifications

Our Abpromise guarantee covers the use of ab22398 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    Information available upon request.

General info

  • Alternative names
    • FO108
    • H2A
    • H2A1B_HUMAN
    • H4 histone family 2
    • H4 histone family member N
    • H4F2
    • H4FN
    • HIST1H2AE
    • HistH2A
    • Histone H2A type 1-B/E
    • Histone H2A.2
    • Histone H2A/a
    • Histone H2A/m
    see all
  • FunctionCore component of nucleosome. 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.
  • Sequence similaritiesBelongs to the histone H2A family.
  • Post-translational
    modifications
    The chromatin-associated form is phosphorylated on Thr-121 during mitosis.
    Deiminated on Arg-4 in granulocytes upon calcium entry.
    Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3. Monoubiquitination of Lys-120 by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Monoubiquitination and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events.
    Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1.
    Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.
  • Cellular localizationNucleus. Chromosome.
  • Target information above from: UniProt accession P04908 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

References for Human Histone H2A (asymmetric di methyl R3) peptide (ab22398)

ab22398 has not yet been referenced specifically in any publications.

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