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H7162
Anti-methyl-Histone H3 (Me-Lys9) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-H3K9me1
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100 G
CN¥1,535.72
250 G
CN¥1,999.56
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100 G
CN¥1,535.72
250 G
CN¥1,999.56
About This Item
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
Drosophila, Caenorhabditis elegans, rat, bovine, human, mouse, frog, chicken
technique(s)
microarray: suitable
western blot: 1:1,000 using whole cell extract of the human epitheloid carcinoma HeLa cell line
UniProt accession no.
shipped in
dry ice
1 of 4
This Item | 11358 | 242772 | SAAR5882500 |
|---|---|---|---|
| assay ≥99% (acidimetric) | assay 99.0-101.0% (T) | assay ≥99% | assay - |
| Quality Level 300 | Quality Level 100 | Quality Level 100 | Quality Level - |
| form solid | form - | form powder or crystals | form - |
| solubility 213 g/L | solubility - | solubility water: 50 mg/mL, clear, colorless | solubility - |
| pH 1.2 (10 g/L in H2O) | pH - | pH - | pH - |
| storage temp. 2-30°C | storage temp. - | storage temp. - | storage temp. 2-30°C |
General description
Histones are proteins that form the nucleosome along with DNA. A nucleosome consists of core histone octamers made of two heterodimers of H2A and H2B along with two heterodimers of H3 and H4. This octamer is bound by the DNA and H1 protein. The HIST3H3 gene is mapped on the human chromosome at 1q42.13.
Specificity
Anti-Methyl-Histone H3 [Me-Lys9] recognizes histone H3 methylated on Lys9.
Immunogen
synthetic methylated peptide corresponding to amino acids 7-20 [Me-Lys9] of human histone H3. The sequence is identical in many species.
Application
Anti-methyl-Histone H3 (Me-Lys9) antibody produced in rabbit may be used in immunoblotting.
Biochem/physiol Actions
Histones H3 and H4 are the predominant histones modified by methylation and are highly methylated in mammalian cells. Lysine residues can be mono-, di-, and tri-methylated, adding further complexity to the regulation of chromatin structure. Conserved lysine residues in the N-terminal tail domains of histone H3, Lys-4, Lys-9 and Lys-27 are the preferred sites of methylation. Methylation of H3 at Lys-9 is a modification intrinsically linked to epigenetic silencing and heterochromatin assembly. Histone H3 is methylated at Lys-9 by site-specific H3 methyltransferases (HMTases) and generates a binding site for heterochromatin protein 1 (HP1).
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.
Storage and Stability
For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots at −20 °C. Repeated freezing and thawing is not recom-mended. Storage in frost-free freezers is also not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Emanuely Silva Chrun et al.
Pathology, research and practice, 213(11), 1329-1339 (2017-09-09)
Among the epigenetic changes, histone acetylation has been recognized as a fundamental process that strongly affects gene expression regulation. Disrupt of this phenomenon has been linked to carcinogenesis. In this review, we analysed studies reporting the process of histone modification
B D Strahl et al.
Nature, 403(6765), 41-45 (2000-01-19)
Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of
Thomas H A Ederveen et al.
Biochimica et biophysica acta, 1809(10), 577-586 (2011-07-26)
Histones are highly basic, relatively small proteins that complex with DNA to form higher order structures that underlie chromosome topology. Of the four core histones H2A, H2B, H3 and H4, it is H3 that is most heavily modified at the
J C Rice et al.
Current opinion in cell biology, 13(3), 263-273 (2001-05-10)
Post-translational addition of methyl groups to the amino-terminal tails of histone proteins was discovered more than three decades ago. Only now, however, is the biological significance of lysine and arginine methylation of histone tails being elucidated. Recent findings indicate that
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