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Histone extracts (10 µg) from NB4 cells were analyzed by western blot using anti-H3K27me2 antibody (Cat. no. 49-1013), diluted 1:500 in TBS-Tween. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.
|Tested species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Raised against the region of the histone H3 containing the dimethylated lysine 27 (H3K27me2), using a KLH-conjugated synthetic peptide.|
|Contains||<0.1% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|ChIP assay (ChIP)||5-10 ug|
|Western Blot (WB)||1:750|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Histone H3 is one of the DNA-binding proteins found in the chromatin of all eukaryotic cells. H3 along with four core histone proteins binds to DNA forming the structure of the nucleosome. Histones play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Post tranlationally, histones are modified in a variety of ways to either directly change the chromatin structure or allow for the binding of specific transcription factors. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of post-translational modification that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.