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Merck
CN

06-599-AF647

Anti-acetyl-Histone H3 Antibody, Alexa Fluor™ 647 Conjugate

from rabbit, ALEXA FLUOR™ 647

别名:

H3 histone family, member T, Histone 3, H3, Histone cluster 3, H3

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UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702

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产品名称

Anti-acetyl-Histone H3 Antibody, Alexa Fluor™ 647 Conjugate, from rabbit, ALEXA FLUOR™ 647

Quality Level

100

biological source

rabbit

conjugate

ALEXA FLUOR™ 647

antibody form

purified antibody

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human, mouse

species reactivity (predicted by homology)

rat (based on 100% sequence homology)

technique(s)

immunocytochemistry: suitable

NCBI accession no.

NP_003484.1

UniProt accession no.

Q16695

shipped in

wet ice

target post-translational modification

acetylation (not specified)

Gene Information

human ... H3C1(8350)
mouse ... H3C1(360198)
rat ... H3C1(679994)

Analysis Note

Evaluated by Immunocytochemistry in A431 cells.

Immunocytochemistry Analysis: A 1:100 dilution of this antibody detected acetyl-Histone H3 in A431 cells.

Application

Immunocytochemistry Analysis: A 1:100 dilution from a representative lot detected acetyl-Histone H3 in NIH/3T3 cells.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Nuclear Receptors
This Anti-acetyl-Histone H3 Antibody, Alexa Fluor™ 647 Conjugate is validated for use in Immunocytochemistry for the detection of acetyl-Histone H3.

Biochem/physiol Actions

Antibody recognizes histone H3 with acetylated Lys9 and/or Lys14.
Other homologies: Broad species cross-reactivity expected based on sequence similarity.

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

17 kDa observed
Histone H3 is one of the five main histone proteins that are involved in the structure of chromatin in eukaryotic cells. The chromatin fiber is composed on repetitive units, known as nucleosomes, which are comprised of an octamer of core histones (two each of H2A, H2B, H3, and H4), around which DNA are wrapped. Histone H3 features a main globular domain and a long N-terminal tail. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Histone H3 is specifically phosphorylated during both mitosis and meiosis in patterns that are specifically coordinated in space and time. These phosphorylations are initiated at different phases of the cell division. Histone H3 variants (H3.1, H3.2 and H3.3) have been implicated in the epigenetic memory of cellular state. Genome-wide patterns of H3 are dependent on amino acid sequence and change with cellular differentiation at developmentally regulated loci.

Immunogen

Epitope: N-terminus
Synthetic peptide corresponding to human histone H3 N-terminal sequence with acetylated Lys9 and Lys14

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Protein A purified
Purified rabbit antibody conjugate in buffer containing PBS, 15 mg/mL BSA and 0.1% Sodium Azide.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.

Legal Information

ALEXA FLUOR is a trademark of Life Technologies

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存储类别

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

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A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.

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