Anti-KDM4A / JHDM3A / JMJD2A 抗体 (ab84518)

製品の概要

  • 製品名Anti-KDM4A / JHDM3A / JMJD2A antibody
    KDM4A / JHDM3A / JMJD2A 一次抗体 製品一覧
  • 製品の詳細
    Rabbit polyclonal to KDM4A / JHDM3A / JMJD2A
  • アプリケーション適用あり: IHC-Pmore details
  • 種交差性
    交差種: Human
    交差が予測される動物種: Chimpanzee, Gorilla, Orangutan
  • 免疫原

    Synthetic peptide corresponding to a region between residues 350 and 400 of Human KDM4A/ JHDM3A/ JMJD2A (NP_055478.1).

  • ポジティブ・コントロール
    • Human ovarian tumor tissue.

製品の特性

アプリケーション

Our Abpromise guarantee covers the use of ab84518 in the following tested applications.

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

アプリケーション Abreviews 特記事項
IHC-P
  • 追加情報IHC-P: 1/100 - 1/500.
    Epitope exposure is recommended.
    Epitope exposure with citrate buffer will enhance staining.


    Not yet tested in other applications.
    Optimal dilutions/concentrations should be determined by the end user.
  • ターゲット情報

    • 機能Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.
      Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.
    • 組織特異性Ubiquitous.
    • 配列類似性Belongs to the JHDM3 histone demethylase family.
      Contains 1 C2HC pre-PHD-type zinc finger.
      Contains 1 JmjC domain.
      Contains 1 JmjN domain.
      Contains 2 PHD-type zinc fingers.
      Contains 2 Tudor domains.
    • ドメインThe 2 Tudor domains recognize and bind methylated histone H3 'Lys-4' residue (H3K4me). Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails. Trimethylated H3 'Lys-4' (H3K4me3) is bound in a cage of 3 aromatic residues, 2 of which are from the Tudor domain 2, while the binding specificity is determined by side-chain interactions involving residues from the Tudor domain 1. The Tudor domains are also able to bind trimethylated histone H3 'Lys-9' (H3K9me3), di- and trimethylated H4 'Lys-20' (H4K20me2 and H4K20me3). Has high affinity for H4K20me2, blocking recruitment of proteins such as TP53BP1.
    • 翻訳後修飾Ubiquitinated by RNF8 and RNF168 following DNA damage, leading to its degradation. Degradation promotes accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited.
    • 細胞内局在Nucleus.
    • Information by UniProt
    • 参照データベース
    • 別名
      • JHDM3A antibody
      • JmjC domain containing histone demethylation protein 3A antibody
      • JmjC domain-containing histone demethylation protein 3A antibody
      • JMJD2 antibody
      • JMJD2A antibody
      • jumonji C domain containing histone demethylase 3A antibody
      • Jumonji domain containing 2 antibody
      • Jumonji domain containing 2A antibody
      • Jumonji domain containing protein 2A antibody
      • Jumonji domain-containing protein 2A antibody
      • KDM4A antibody
      • KDM4A_HUMAN antibody
      • KIAA0677 antibody
      • Lysine (K) specific demethylase 4A antibody
      • Lysine-specific demethylase 4A antibody
      • TDRD14A antibody
      • Tudor domain containing 14A antibody
      see all

    Anti-KDM4A / JHDM3A / JMJD2A antibody 画像

    • ab84518, at 1/250 dilution, staining KDM4A / JHDM3A / JMJD2A in formalin-fixed, paraffin-embedded human ovarian tumor by Immunohistochemistry using DAB staining.

    Anti-KDM4A / JHDM3A / JMJD2A antibody (ab84518) 使用論文

    ab84518 has not yet been referenced specifically in any publications.

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