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Merck

07-595

Anti-acetyl-Histone H4 (Lys12) Antibody

serum, Upstate®

동의어(들):

H4K12Ac, Histone H4 (acetyl K12)

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제품정보 (DICE 배송 시 비용 별도)

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Clone:
polyclonal
Species reactivity:
Saccharomyces cerevisiae, human
Application:
ChIP
dot blot
western blot
Technique(s):
ChIP: suitable (ChIP-seq)
dot blot: suitable
western blot: suitable
Citations:
106
Uniprot accession no.:
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제품 이름

Anti-acetyl-Histone H4 (Lys12) Antibody, serum, Upstate®

biological source

rabbit

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

Saccharomyces cerevisiae, human

manufacturer/tradename

Upstate®

technique(s)

ChIP: suitable (ChIP-seq)
dot blot: suitable
western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

acetylation (Lys12)

Quality Level

Gene Information

human ... HIST2H4B(554313)

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Analysis Note

Control
Acid extracted proteins from HeLa cells treated with sodium butyrate
routinely evaluated by immunoblot on acid extracted proteins from HeLa cells

Application

Research Category
Epigenetics & Nuclear Function
Research Sub Category
Histones
Use Anti-acetyl-Histone H4 (Lys12) Antibody (Rabbit Polyclonal Antibody) validated in ChIP, DB, WB, ChIP-seq to detect acetyl-Histone H4 (Lys12) also known as H4K12Ac, Histone H4 (acetyl K12).

Biochem/physiol Actions

Broad species cross-reactivity expected
Recognizes Histone H4 acetylated on lysine 12.

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.

General description

10 kDa
Histone H4 is one of the 5 main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N terminal tail H4 is involved with the structure of the nucleosomes of the ′beads on a string′ structure.

Acetylation of histone H4 occurs at several different lysine positions in the histone tail and is performed by a family of enzymes known as Histone Acetyl Transferases (HATs).

Immunogen

peptide containing the sequence (LGAcKGG) corresponding to lysine 12 acetylation of yeast Histone H4.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Physical form

Depleted rabbit antiserum in 30% glycerol, 0.07M Tris-glycine, pH 7.4, 0.105 M NaCl, 0.035% sodium azide as a preservative.
Immunodepleted Serum

Preparation Note

Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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저장 등급

10 - Combustible liquids

wgk

WGK 1


시험 성적서(COA)

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이 제품을 이미 가지고 계십니까?

문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

The complex pattern of epigenomic variation between natural yeast strains at single-nucleosome resolution.
Filleton, F; Chuffart, F; Nagarajan, M; Bottin-Duplus, H; Yvert, G
Epigenetics & Chromatin null
Histone deacetylase inhibitors modify pancreatic cell fate determination and amplify endocrine progenitors.
Haumaitre, Cecile, et al.
Molecular and cellular biology, 28, 6373-6383 (2008)
The molecular topography of silenced chromatin in Saccharomyces cerevisiae.
Thurtle, DM; Rine, J
Genes & Development null
Paola Y Bertucci et al.
Nucleic acids research, 41(12), 6072-6086 (2013-05-04)
Steroid receptors were classically described for regulating transcription by binding to target gene promoters. However, genome-wide studies reveal that steroid receptors-binding sites are mainly located at intragenic regions. To determine the role of these sites, we examined the effect of
Panagis Filippakopoulos et al.
Cell, 149(1), 214-231 (2012-04-03)
Bromodomains (BRDs) are protein interaction modules that specifically recognize ε-N-lysine acetylation motifs, a key event in the reading process of epigenetic marks. The 61 BRDs in the human genome cluster into eight families based on structure/sequence similarity. Here, we present

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07-59504053252733284

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