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MABE645

Anti-acetyl-Histone H3 (Lys9) Antibody, clone RM161

clone RM161, from rabbit

Sinónimos:

Histone H3.3, Histone H3

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Tamaño de envaseSKUDisponibilidadPrecio
100 μg
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426,00 €

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UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Clone:
RM161, monoclonal
Species reactivity:
human
Application:
WB, multiplexing
Citations:
1

426,00 €


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biological source

rabbit

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

RM161, monoclonal

species reactivity

human

technique(s)

multiplexing: suitable, western blot: suitable

isotype

IgG

UniProt accession no.

shipped in

wet ice

target post-translational modification

acetylation (Lys9)

Gene Information

human ... H3F3B(3021)

General description

Histone H3, also known as Histone H3.1t (H3/t), H3t, H3/g, and encoded by the gene name HIST3H3/ H3FT, is a core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Therefore, histones play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. 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. 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. High levels of phosphorylation of Histone H3 are associated with mitosis.
~17 kDa observed. Uncharacterized bands may be observed in some lysate(s).

Immunogen

A linear peptide corresponding to human Histone H3 acetylated at Lys9.

Application

This Anti-acetyl-Histone H3 (Lys9) Antibody, clone RM161 is validated for use in Western Blotting, Multiplexing for the detection of acetyl-Histone H3.

Biochem/physiol Actions

This antibody reacts to Histone H3 acetylated at Lysine 9 (K9ac). No cross reactivity with other acetylated Lysines in Histone H3.

Physical form

Format: Purified

Analysis Note

Evaluated by Western Blotting in untreated and sodium butyrate treated HeLa acid extract.

Western Blotting Analysis (WB): 0.25 μg/mL of this antibody detected acetyl-Histone H3 (Lys9) in sodium butyrate treated HeLa acid extract.

Other Notes

Concentration: Please refer to lot specific datasheet.

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Este artículo
MABE647MABE636MABE643
Gene Information

human ... H3F3B(3021)

Gene Information

human ... H3F3B(3021)

Gene Information

human ... H3F3B(3021)

Gene Information

human ... H3F3B(3021)

clone

RM161, monoclonal

clone

RM172, monoclonal

clone

RM140, monoclonal

clone

RM147, monoclonal

antibody form

purified antibody

antibody form

purified antibody

antibody form

-

antibody form

purified antibody

species reactivity

human

species reactivity

human

species reactivity

human

species reactivity

human

biological source

rabbit

biological source

rabbit

biological source

rabbit

biological source

rabbit

Quality Level

100

Quality Level

100

Quality Level

100

Quality Level

100


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Clase de almacenamiento

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

does not flash

flash_point_c

does not flash



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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.


William J Lu-Culligan et al.
Nature, 622(7981), 173-179 (2023-09-21)
Lysine residues in histones and other proteins can be modified by post-translational modifications that encode regulatory information1. Lysine acetylation and methylation are especially important for regulating chromatin and gene expression2-4. Pathways involving these post-translational modifications are targets for clinically approved



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SKUGTIN
MABE64504055977181463

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