Mouse NIH3T3 cells were stained with antibody against H3K27me3 (Cat. No. A15024) and with DAPI. Cells were fixed with 4% formaldehyde for 10 and quote; and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H3K27me3 antibody (left) diluted 1:200 in blocking solution followed by an antirabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.
|Tested species reactivity||Human|
|Published species reactivity||Not Applicable|
|Host / Isotype||Rabbit / IgG|
|Immunogen||rabbit immunized with the region of the histone H3 containing the trimethylated lysine 27 (H3K27me3)|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|ChIP assay (ChIP)||Assay Dependent|
|ELISA (ELISA)||Assay Dependent|
|Immunocytochemistry (ICC)||Assay Dependent|
|Immunofluorescence (IF)||Assay Dependent|
|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.
|Not Applicable||Not Cited||
Interference with endogenous EZH2 reverses the chemotherapy drug resistance in cervical cancer cells partly by up-regulating Dicer expression.
A15024 was used in western blot to study reversal of chemotherapy drug resistance in cervical cancer cells by interference with endogenous EZH2 and up-regulation of Dicer expression
|Cai L,Wang Z,Liu D||Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine (37:6359)||2016|