KDM4C / GASC1 / JMJD2C peptide (ab155886)

Overview

Description

  • Nature
    Synthetic

Associated products

Specifications

Our Abpromise guarantee covers the use of ab155886 in the following tested applications.

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

  • Applications

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

  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

    Constituent: PBS

General Info

  • Alternative names
    • 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
  • Function
    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.
  • Tissue specificity
    Overexpressed in several esophageal squamous cell carcinomas (ESCs).
  • Sequence similarities
    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.
  • Domain
    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.
  • Cellular localization
    Nucleus.
  • Information by UniProt

References

ab155886 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

I have a follow up question based on multiple bands disappearing when the blocking peptide is added. What are the molecular weights of the other bands in your blot? If more than one band disappears in Western blot by peptide/antigen competition, those ...

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Thank you for your reply.

I have sent you the blocking peptide (https://www.abcam.com/kdm4c--gasc1--jmjd2c-peptide-ab155886.html) free of charge. Your order number is 1236828, and is expected to be delivered Friday, 1/18/2013.

Below i...

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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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