RFWD2 Polyclonal Antibody

Cat.#: 160507

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Product Information

  • Product Name
    RFWD2 Polyclonal Antibody
  • Documents
  • Description
    Polyclonal antibody to RFWD2
  • Tested applications
    WB, IHC
  • Species reactivity
    Human, Mouse, Rat
  • Alternative names
    RFWD2 antibody; COP1 antibody; RNF200 antibody; E3 ubiquitin-protein ligase RFWD2 antibody
  • Isotype
    Rabbit IgG
  • Preparation
    Antigen: Recombinant fusion protein containing a sequence corresponding to amino acids 582-731 of human RFWD2 (NP_071902.2).
  • Clonality
    Polyclonal
  • Formulation
    PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
  • Storage instructions
    Store at -20℃. Avoid freeze / thaw cycles.
  • Applications
    WB 1:500 - 1:2000
    IHC 1:100 - 1:200
  • Validations

    Western blot - RFWD2 Polyclonal Antibody

    Western blot - RFWD2 Polyclonal Antibody

    Western blot analysis of extracts of various cell lines, using RFWD2 antibody at 1:1000 dilution.Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) at 1:10000 dilution.Lysates/proteins: 25ug per lane.Blocking buffer: 3% nonfat dry milk in TBST.Detection: ECL Basic Kit .Exposure time: 60s.

  • Background
    E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif (Probable).

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