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重要文件

05-1354

Sigma-Aldrich

Anti-Histone H3 Antibody (Dimethyl K9, Phospho S10), clone 6HH3-2C5

ascites fluid, clone 6HH3-2C5, from mouse

同義詞:

H3K9me2S10P, Histone H3 (di methyl K9, phospho S10), H3 histone, family 3B (H3.3B)

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About This Item

分類程式碼代碼:
12352203
eCl@ss:
32160702
NACRES:
NA.41

生物源

mouse

品質等級

抗體表格

ascites fluid

抗體產品種類

primary antibodies

無性繁殖

6HH3-2C5, monoclonal

物種活性

human

物種活性(以同源性預測)

Drosophila (based on 100% sequence homology)

技術

immunocytochemistry: suitable
western blot: suitable

同型

IgG1κ

GenBank登錄號

UniProt登錄號

運輸包裝

wet ice

目標翻譯後修改

dimethylation (Lys9), phosphorylation (pSer10)

基因資訊

human ... H3F3B(3021)

一般說明

Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the ′beads on a string′ structure. Histone proteins are highly post-translationally modified, and Histone H3 is the most extensively modified of the five histones. The term "Histone H3" alone is purposely ambiguous in that it does not distinguish between sequence variants or modification state. Histone H3 is an important protein in the emerging field of epigenetics, where its sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes.

特異性

Antibody recognizes dimethyl (Lys9) phospho(Ser10) on Histone H3.

免疫原

Epitope: Dimethyl (Lys9) & Phospho (Ser10)
Synthetic linear peptide corresponding to dimethyl (Lys9) and Phospho (Ser10) of Histone H3.

應用

Immunocytochemistry:
A 1:500 dilution of a representative lot of this antibody detected Dimethyl (Lys9)-Phospho (Ser10) Histone H3 in A431 and HeLa cells.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Histones
Use Anti-Histone H3 Antibody (Dimethyl K9, Phospho S10), clone 6HH3-2C5 (mouse monoclonal antibody) validated in WB, ICC to detect Histone H3 (Dimethyl K9 also known as H3K9me2S10P, Histone H3 (di methyl K9 phospho S10).

品質

Evaluated by western blot in untreated and Etoposide-treated HeLa acid extracts.

Western Blot Analysis:
A 1:1,000 dilution of this antibody detected Dimethyl (Lys9)-Phospho (Ser10) Histone H3 in 10 µg of untreated and Etoposide-treated HeLa acid extracts.

標靶描述

~17 kDa

外觀

Unpurified
Mouse monoclonal IgG1κ ascites with 0.05% sodium azide.

儲存和穩定性

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

分析報告

Control
Untreated and Etoposide-treated HeLa acid extracts.

法律資訊

GenBank is a registered trademark of United States Department of Health and Human Services

免責聲明

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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儲存類別代碼

12 - Non Combustible Liquids

水污染物質分類(WGK)

nwg

閃點(°F)

Not applicable

閃點(°C)

Not applicable


分析證明 (COA)

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存取文件庫

Histone H3S10 phosphorylation by the JIL-1 kinase in pericentric heterochromatin and on the fourth chromosome creates a composite H3S10phK9me2 epigenetic mark.
Wang, Chao, et al.
Chromosoma (2014)
Jing Sun et al.
Frontiers in plant science, 12, 814465-814465 (2022-02-05)
Lesion mimic mutants have become an effective material for understanding plant-microbe interactions and the immune mechanism in plants. Although many mechanisms responsible for the lesion mimic phenotype have been clarified in plants, the mechanism by which lesion mimic is regulated
Yeran Li et al.
Development (Cambridge, England), 144(18), 3232-3240 (2017-08-16)
A model has been proposed in which JIL-1 kinase-mediated H3S10 and H2Av phosphorylation is required for transcriptional elongation and heat shock-induced chromatin decondensation. However, here we show that although H3S10 phosphorylation is indeed compromised in the H2Av null mutant, chromatin
Scott B Rothbart et al.
Nature structural & molecular biology, 19(11), 1155-1160 (2012-10-02)
A fundamental challenge in mammalian biology has been the elucidation of mechanisms linking DNA methylation and histone post-translational modifications. Human UHRF1 (ubiquitin-like PHD and RING finger domain-containing 1) has multiple domains that bind chromatin, and it is implicated genetically in

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