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Merck
모든 사진(1)

주요 문서

D5567

Sigma-Aldrich

Anti-dimethyl-Histone H3 (diMe-Lys9) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

동의어(들):

Anti-H3K9me2

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About This Item

MDL number:
UNSPSC 코드:
12352203
NACRES:
NA.41

생물학적 소스

rabbit

Quality Level

결합

unconjugated

항체 형태

IgG fraction of antiserum

항체 생산 유형

primary antibodies

클론

polyclonal

양식

buffered aqueous solution

분자량

antigen 17 kDa

종 반응성

Drosophila, bovine, chicken, Arabidopsis thaliana, Caenorhabditis elegans, human, mouse, frog, rat

기술

ChIP: suitable
microarray: suitable
western blot: 1:1,000-1:2,000 using whole extract of human epitheloid carcinoma HeLa cell line

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

dimethylation (Lys9)

일반 설명

Histone methylation is a complex, dynamic process involved in a number of processes, including transcriptional regulation, chromatin condensation, mitosis and heterochromatin assembly. Conserved lysine residues in the N-terminal tail domains of histone H3, Lys4, Lys9 and Lys27 are the preferred sites of methylation. SET domain-, site-specific histone methyltransferases (HMTases) are involved in methylation of Lys9 in histone 3.

특이성

ChIP validated

면역원

synthetic methylated peptide corresponding to amino acids 5-13 (diMe-Lys9) of human histone H3, conjugated to KLH. This sequence is identical in many species including mouse, rat, bovine, chicken, frog, Drosophila, C. elegans, tetrahymena, and Arabidopsis thaliana histone H3.

애플리케이션

Anti-dimethyl-Histone H3 (diMe-Lys9) antibody produced in rabbit has been used in immunoblotting and chromatin immunoprecipitation assay.

생화학적/생리학적 작용

Mono- and dimethylation of H3 at Lys9 are intrinsically linked to epigenetic silencing and heterochromatin assembly. Methylation of H3 at Lys9 generates a binding site for HP1 proteins, a family of heterochromatic adaptor proteins implicated in both gene silencing and in the organization of higher order chromatin.

물리적 형태

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

면책조항

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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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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문서 라이브러리 방문

Noma K et al.
Science (New York, N.Y.), 293(5532), 1150-1155 (2001-08-11)
Eukaryotic genomes are organized into discrete structural and functional chromatin domains. Here, we show that distinct site-specific histone H3 methylation patterns define euchromatic and heterochromatic chromosomal domains within a 47-kilobase region of the mating-type locus in fission yeast. H3 methylated
Jikai Cui et al.
Cell death & disease, 12(6), 501-501 (2021-05-20)
Regulatory T cells play a crucial role in orchestrating immune response and maintaining immune tolerance, and the expression of the Foxp3 gene is indispensable to the differentiation of regulatory T cells. IL-4 shows strong inhibitory effects on Foxp3 expression and
T Jenuwein et al.
Science (New York, N.Y.), 293(5532), 1074-1080 (2001-08-11)
Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely impinge on histone amino termini, thereby regulating access to the underlying DNA. Distinct histone amino-terminal modifications can generate synergistic or
Molecular biology. Methylation talk between histones and DNA.
A Bird
Science (New York, N.Y.), 294(5549), 2113-2115 (2001-12-12)
Xiang Xiao et al.
Nature communications, 6, 8266-8266 (2015-09-15)
Glucocorticoid-induced TNFR-related protein (GITR) is a costimulatory molecule with diverse effects on effector T cells and regulatory T cells (Tregs), but the underlying mechanism remains poorly defined. Here we demonstrate that GITR ligation subverts the induction of Foxp3(+) Tregs and

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