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Merck
모든 사진(1)

주요 문서

H0913

Sigma-Aldrich

Anti-acetyl-Histone H3 (Ac-Lys9) antibody, Mouse monoclonal

clone AH3-120, purified from hybridoma cell culture

동의어(들):

Anti-H3K9ac

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About This Item

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

생물학적 소스

mouse

Quality Level

결합

unconjugated

항체 형태

purified immunoglobulin

항체 생산 유형

primary antibodies

클론

AH3-120, monoclonal

양식

buffered aqueous solution

분자량

antigen ~17 kDa

종 반응성

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

포장

antibody small pack of 25 μL

농도

~2 mg/mL

기술

immunocytochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 1-2 μg/mL using whole cell extract of mouse fibroblasts 3T3 cell line treated with sodium butyrate

동형

IgG1

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

acetylation (Lys9)

일반 설명

Monoclonal Anti-Acetyl-Histone H3 (Ac-Lys9) recognizes human histone H3 when acetylated on Lys9. Staining of the histone H3-Ac-Lys9 band in immunoblotting is specifically inhibited with the acetylated histone H3 immunizing peptide but not with the nonacetylated one.

면역원

synthetic, acetylated histone H3 peptide (amino acids 7-20, Ac-Lys9) corresponding to the N-terminus of human histone H3. The sequence is identical in many species including mouse, rat, bovine, chicken, frog, Drosophila, and C. elegans, and is highly conserved (single amino acid substitution) in Tetrahymena histone H3.

애플리케이션

Monoclonal Anti-acetyl-Histone H3 (Ac-Lys9) antibody may be used in various applications including ELISA, immunoblotting (approx. 17 kDa), and immunocytochemistry.

생화학적/생리학적 작용

Acetyl-Histone H3 hav Acetylation of lysine residues within these N-terminal domains of histones by histone acetyl-transferase (HATs), including Gcn5p, PCAF, p300/CBP and TAFII250 is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylase (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms. Acetylation of specific lysines in histone H3 is also associated with processes apart from transcription. During DNA replication, new histones are rapidly synthesized and assembled into replicated DNA. Histones H3 and H4 are brought to replicating chromatin in a pre-acetylated state that turns into a de-acetylated state after replication is completed and the newly assembled chromatin matures.

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

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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문서 라이브러리 방문

A novel Arabidopsis acetyltransferase interacts with the geminivirus movement protein NSP
McGarry RC, et al.
Plant Cell, 15, 1605-1618 (2003)
Priyanka Jain et al.
Scientific reports, 9(1), 8508-8508 (2019-06-13)
Glycosylphosphatidylinositol (GPI)-anchored proteins are important for virulence of many pathogenic organisms including the human fungal pathogen, Candida albicans. GPI biosynthesis is initiated by a multi-subunit enzyme, GPI-N-acetylglucosaminyltransferase (GPI-GnT). We showed previously that two GPI-GnT subunits, encoded by CaGPI2 and CaGPI19
Regulation of immune responses by histone deacetylase inhibitor
Licciardi PV and Karagiannis TC
ISRN hematology, 2012 (2012)
Histone H3 variants and modifications on transcribed genes
Workman JL and Abmayr SM
Proceedings of the National Academy of Sciences of the USA, 101, 1429-1430 (2004)
Parisa Nadri et al.
PloS one, 17(7), e0267598-e0267598 (2022-07-22)
SCNT embryos suffer from poor developmental competence (both in vitro and in vivo) due to various defects such as oxidative stress, incomplete epigenetic reprogramming, and flaws in telomere rejuvenation. It is very promising to ameliorate all these defects in SCNT

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