Human KDM4C / GASC1 / JMJD2C peptide (ab111662)

製品の概要

製品の詳細

  • 由来
    Synthetic
  • アミノ酸配列
    • 生物種
      Human
    • 配列
      CLCNLRGGALKQTKNNKWAHVMCAVAVPEVRFTNVPERTQIDVGRIPLQR

関連製品

特性

Our Abpromise guarantee covers the use of ab111662 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

    Blocking - Blocking peptide for Anti-KDM4C / GASC1 / JMJD2C antibody (ab85454)

  • 製品の状態
    Liquid
  • Concentration information loading...

前処理および保存

  • 保存方法および安定性

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid repeated freeze / thaw cycles.

関連情報

  • 別名
    • bA146B14.1
    • GASC 1 protein
    • GASC-1 protein
    • GASC1
    • Gene amplified in squamous cell carcinoma 1 protein
    • JHDM3C
    • JmjC domain containing histone demethylation protein 3C
    • JmjC domain-containing histone demethylation protein 3C
    • JMJD2C
    • Jumonji domain containing 2C
    • Jumonji domain containing protein 2C
    • Jumonji domain-containing protein 2C
    • Kdm4c
    • KDM4C_HUMAN
    • Lysine (K) specific demethylase 4C
    • Lysine demethylase 4C
    • Lysine-specific demethylase 4C
    • TDRD14C
    • Tudor domain containing 14C
    see all
  • 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.
  • 組織特異性
    Overexpressed in several esophageal squamous cell carcinomas (ESCs).
  • 配列類似性
    Belongs to the JHDM3 histone demethylase family.
    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 histones. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails.
  • 細胞内局在
    Nucleus.
  • Information by UniProt

参考文献

ab111662 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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