Phospho-H1.3+H1.4 Recombinant Rabbit monoclonal Ab IgG

SKU: BA111317-100µl
$279.00Price

Fig1: Western blot analysis of Phospho-Histone H1.3(T17)+Histone H1.4(T17) on CRC cell lysates using anti-Phospho-Histone H1.3(T17)+Histone H1.4(T17) antibody at 1/500 dilution.

Positive control: 

  Lane 1: Untreated CRC whole cell lysates  Lane 2: CRC cells treated with 1.5ug/ml Colcemid for 12 hours whole cell lysates

Fig2: ICC staining Phospho-Histone H1.3(T17)+Histone H1.4(T17) in NIH/3T3 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.

Fig3: ICC staining Phospho-Histone H1.3(T17)+Histone H1.4(T17) in CRC cells (green). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.

Bon Opus Cat. #BA111317
Size
  • Host Species; Species Reactivity

    Rabbit; Human, Mouse, Rat
  • Immunogen

    Synthetic phospho-Peptide corresponding to residues surrounding Thr17 of human H1.4.
  • Application Summary

    WB, ICC/IF, IHC
  • Purification; Formulation

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

    Histone H1.3, Histone H1c, Histone H1s-2, Histone H1.4, Histone H1b, Histone H1s-4
  • Background

    Eukaryotic histones are basic and water soluble nuclear proteins that form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fiber. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form the octamer; formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Over 80% of nucleosomes contain the linker Histone H1, derived from an intronless gene, that interacts with linker DNA between nucleosomes and mediates compaction into higher order chromatin. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Such modifications include methylation, citrullination, acetylation, phosphorylation, sumoylation, ubiquitination and ADP-ribosylation.(ET1602-11)

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