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Immunofluorescence study using the anti-H3K9me3 polyclonal antibody. NIH3T3 cells (mouse fibroblasts) were formaldehyde fixed, permeabilized with Triton® X-100 (Dow Chemical Co) and blocked with PBS containing 2.5% BSA. (A) Cells were labeled with the anti-H3K9me3 antibody (diluted 1:200 and incubated for 1 hour at room temperature) followed by FITC-labeled goat anti-rabbit secondary antibody. (B) Nuclei were stained using the DNA-specific stain DAPI. Both the anti-H3K9me3 antibody and DAPI produced clear nuclear staining. The dense signals obtained with both probes characterize the distribution pattern of H3K9me3, which is linked to the transcriptionally inactive, condensed pericentric heterochromatin.
|Tested species reactivity||Human, Mouse|
|Published species reactivity||Mouse, Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||rabbits against histone H3, trimethylated at lysine 9 [K9me3], 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 ug|
|ELISA (ELISA)||1:100 to 1:500|
|Western Blot (WB)||1:1,000|
* 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 2 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.
FBXO22 protein is required for optimal synthesis of the N-methyl-D-aspartate (NMDA) receptor coagonist D-serine.
49-1008 was used in western blot to investigate the regulation of d-serine synthesis
|Dikopoltsev E,Foltyn VN,Zehl M,Jensen ON,Mori H,Radzishevsky I,Wolosker H||The Journal of biological chemistry (289:33904)||2014|
Induction of 11β-HSD 1 and activation of distinct mineralocorticoid receptor- and glucocorticoid receptor-dependent gene networks in decidualizing human endometrial stromal cells.
49-1008 was used in western blot to study the effects of glucocorticoids at the feto-maternal interface.
|Kuroda K,Venkatakrishnan R,Salker MS,Lucas ES,Shaheen F,Kuroda M,Blanks A,Christian M,Quenby S,Brosens JJ||Molecular endocrinology (Baltimore, Md.) (27:192)||2013|
H3 histone family, member A; H3a; H3K9me3; HIST1H3A; Histone 1; histone 1, H3a; Histone H3.1; Histone H3/a; Histone H3/b; Histone H3/c; Histone H3/d; Histone H3/f; Histone H3/h; Histone H3/i; Histone H3/j; Histone H3/k; Histone H3/l
H3/A; H3FA; H3FB; H3FC; H3FD; H3FF; H3FH; H3FI; H3FJ; H3FK; H3FL; HIST1H3A; HIST1H3B; HIST1H3C; HIST1H3D; HIST1H3E; HIST1H3F; HIST1H3G; HIST1H3H; HIST1H3I; HIST1H3J