Histone extracts of HeLa cells (15 µg) were analyzed by western blot using the anti-H3R17me2 crude serum (Cat. no. 49-1021), diluted 1:250 in TBS-Tween containing 5% skimmed milk. The location of the protein of interest is indicated with an arrow; the marker (in kDa) is shown on the right.
|Tested species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Raised against histone H3 containing the dimethylated arginine 17 (H3R17me2), using a KLH-conjugated synthetic peptide.|
|Storage buffer||whole serum|
|Contains||<0.1% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|ChIP assay (ChIP)||10-15 ug|
|ELISA (ELISA)||1:1,000 to 1:3,000|
|Western Blot (WB)||1:250|
* 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.
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