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Western blot analysis of lysates prepared from thymidine–treated NIH3T3 cells using rabbit anti-histone H3 [pS10] antibody (Cat. no. 44-1190G). The membrane was treated with either no peptide (lane 1), the non-phosphopeptide corresponding to the phosphopeptide immunogen (lane 2), a generic phosphoserine containing peptide (lane 3), or the phosphopeptide immunogen (lane 4). Prior to incubation with the primary antibody, lane 5 was treated with Lambda phosphatase.
|Tested species reactivity||Human|
|Published species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Phosphopeptide derived from the region of human Histone H3 that contains serine 10.|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.3, with 1mg/ml BSA, 50% glycerol|
|Contains||0.05% sodium azide|
|Tested Applications||Dilution *|
|Western Blot (WB)||Assay Dependent|
* 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.
|Western Blot (WB)||See 1 publications below|
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.
The SKP1-Cul1-F-box and leucine-rich repeat protein 4 (SCF-FbxL4) ubiquitin ligase regulates lysine demethylase 4A (KDM4A)/Jumonji domain-containing 2A (JMJD2A) protein.
44-1190G was used in western blot to report that degradation of JMJD2A is regulated by the proteasome.
|Van Rechem C,Black JC,Abbas T,Allen A,Rinehart CA,Yuan GC,Dutta A,Whetstine JR||The Journal of biological chemistry (286:30462)||2011|