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Merck
CN

09-774

Anti-EED Antibody

from rabbit

别名:

embryonic ectoderm development

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
polyclonal
Application:
western blot
Species reactivity:
human, mouse
Citations:
42
Technique(s):
western blot: suitable
Uniprot accession no.:
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产品名称

Anti-EED Antibody, from rabbit

biological source

rabbit

conjugate

unconjugated

antibody form

purified antibody

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human, mouse

species reactivity (predicted by homology)

dog, chicken, bovine, opossum, rat

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Quality Level

Gene Information

dog ... Eed(476779)
human ... EED(8726)
mouse ... Eed(13626)
rat ... Eed(293104)

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Replaces: 09-727

Physical form

Format: Purified

Analysis Note

Control
Jurkat Cell Lysate

3T3/A31 cell lysate
Western Blot Analysis: 1 μg/mL of this lot detected EED on 10 μg of Jurkat cell lysate.

Application

Use Anti-EED Antibody (Rabbit Polyclonal Antibody) validated in WB to detect EED also known as embryonic ectoderm development.

Biochem/physiol Actions

This antibody recognizes EED, Mr ~ 62-70 kDa.

General description

Polycomb group proteins are important for maintaining transcriptional silencing. One conserved PcG complex, PRC2, is composed of several proteins including the histone methyltransferase EZH2, the WD-repeat protein EED (Embryonic ectoderm development), and the Zn-finger protein Suz12. Transcriptional repression mediated by EED involves histone deacetylation, while the EZH2 methylates histone H3 on lysine 27. EED protein is present in four isoforms. These EED isoforms selectively associate with distinct EZH2-containing complexes, resulting in differential targeting of their associated methyltransferase activity. These complexes play a role in Hox gene silencing, X-inactivation, germline development, stem cell pluripotency and cancer metastasis.
~53 kDa observed. Uniprot describes three isoforms at 51 kDa (isoform 1), 53 kDa (isoform 2), and 46 kDa (isoform 3).

Immunogen

A synthetic peptide corresponding to a.a. 429-441 of human EED, conjugated to KLH.
Epitope: a.a. 429-441

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存储类别

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Falak Sher et al.
Cellular reprogramming, 13(1), 1-6 (2010-10-29)
Recently, we have demonstrated the expression of the polycomb group protein Ezh2 in embryonic and adult neural stem cells. Although Ezh2 remained highly expressed when neural stem cells differentiate into oligodendrocyte precursor cells, it is downregulated during the differentiation into
Sylvia Mahara et al.
Proceedings of the National Academy of Sciences of the United States of America, 113(26), E3735-E3744 (2016-06-16)
Despite the established oncogenic function of Polycomb repressive complex 2 (PRC2) in human cancers, its role as a tumor suppressor is also evident; however, the mechanism underlying the regulation of the paradoxical functions of PRC2 in tumorigenesis is poorly understood.
Bin Shi et al.
Cancer medicine, 8(14), 6383-6392 (2019-08-29)
The aims of this study were to investigate the link between enhancer of zeste homolog 2 (EZH2) and histone deacetylase (HDAC) in preclinical studies and in human lung cancer tissue microarrays. Enhancer of zeste homolog 2 and HDAC1 mRNA expression
Taichi Takashina et al.
Cancer science, 107(7), 955-962 (2016-04-27)
Recent discoveries have revealed that human cancer involves aberrant epigenetic alterations. We and others have previously shown that the histone methyltransferase EZH2, the catalytic subunit of polycomb repressive complex 2 (PRC2), is frequently overexpressed in non-small-cell lung cancer (NSCLC) and
Stefanie Göllner et al.
Nature medicine, 23(1), 69-78 (2016-12-13)
In acute myeloid leukemia (AML), therapy resistance frequently occurs, leading to high mortality among patients. However, the mechanisms that render leukemic cells drug resistant remain largely undefined. Here, we identified loss of the histone methyltransferase EZH2 and subsequent reduction of

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