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CHD4 Recombinant Rabbit monoclonal Antibody IgG

SKU: BA112252-100µl

Fig1: ICC staining of CHD4 in 293T cells (green). Formalin fixed cells were permeabilized with 0.1% Triton X-100 in TBS for 10 minutes at room temperature and blocked with 1% Blocker BSA for 15 minutes at room temperature. Cells were probed with the primary antibody (ET1704-53, 1/200) for 1 hour at room temperature, washed with PBS. Alexa Fluor®488 Goat anti-Rabbit IgG was used as the secondary antibody at 1/100 dilution. The nuclear counter stain is DAPI (blue).

Fig2: Immunohistochemical analysis of paraffin-embedded human breast cancer tissue using anti-CHD4 antibody. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH 6.0) for 20 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody (ET1704-53, 1/100) for 30 minutes at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.

Fig3: Flow cytometric analysis of CHD4 was done on 293T cells. The cells were fixed, permeabilized and stained with the primary antibody (ET1704-53, 1/100) (red). After incubation of the primary antibody at room temperature for an hour, the cells were stained with a Alexa Fluor 488-conjugated goat anti-rabbit IgG Secondary antibody at 1/500 dilution for 30 minutes.Unlabelled sample was used as a control (cells without incubation with primary antibody; black).

Bon Opus Cat. #BA112252
  • Host Species; Species Reactivity

    Rabbit; Human
  • Immunogen

    Recombinant protein.
  • Application Summary

    WB, ICC, IHC, FC
  • Purification; Formulation

    ProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
  • ALTnames

    Chromodomain-helicase-DNA-binding protein 4, ATP-dependent helicase CHD4, Mi-2 autoantigen 218 kDa protein, Mi2-beta
  • Background

    In the intact cell, DNA closely associates with histones and other nuclear proteins to form chromatin. The remodeling of chromatin is believed to be a critical component of transcriptional regulation and a major source of this remodeling is brought about by the acetylation of nucleosomal histones. Acetylation of lysine residues in the amino terminal tail domain of histone results in an allosteric change in the nucleosomal conformation and an increased accessibility to transcription factors by DNA. Conversely, the deacetylation of histones is associated with transcriptional silencing. Chromatin structure alteration may be brought about by the action of ATP-dependent multiprotein complexes. One such complex is the mSin3 corepressor complex, which contains mSin3, the histone deacetylases HDAC1 and HDAC2, the associated proteins SAP 30 and SAP 18, and the autoantigens Mi2-α and Mi2-β.(ET1704-53)