EED Protein, Human (sf9, His-GST)

EED protein is a core member of the Polycomb group (PcG) and is critical in the PRC2/EED-EZH2 complex, driving "Lys-9" and "Lys-27" methylation on histone H3 to achieve transcriptional repression . It recognizes trimethylated "Lys-26" on histone H1 and inhibits the methyltransferase activity of the PRC2 complex on nucleosomal histone H3 "Lys-27". EED Protein, Human (sf9, His-GST) is the recombinant human-derived EED protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag.

EED, a Polycomb group (PcG) protein, serves as a key component of the PRC2/EED-EZH2 complex, contributing to the methylation of 'Lys-9' and 'Lys-27' residues on histone H3, resulting in the transcriptional repression of target genes. It plays a crucial role in recognizing trimethylated 'Lys-26' of histone H1, inhibiting the methyltransferase activity of the PRC2 complex on nucleosomal histone H3 'Lys-27'. Conversely, recognition of 'Lys-27' trimethylation enables the propagation of this repressive mark. Beyond its role in histone modification, the PRC2/EED-EZH2 complex may act as a platform recruiting DNA methyltransferases, bridging two distinct epigenetic repression systems. Genes subject to repression by this complex include HOXC8, HOXA9, MYT1, and CDKN2A. Comprising EED, EZH2, SUZ12, RBBP4, and RBBP7, and possibly AEBP2, the PRC2/EED-EZH2 complex requires EED, EZH2, and SUZ12 as minimum components for its methyltransferase activity. Furthermore, EED participates in the PRC2/EED-EZH1 complex, which involves EED, EZH1, SUZ12, RBBP4, and AEBP2. The intricate network of interactions, including those with histones, DNMTs, and other proteins, highlights EED's pivotal role in epigenetic regulation.

Human

Sf9 insect cells

N-His;N-GST

O75530 (M1-R441)

8726  [NCBI]

Full Length

MSEREVSTAPAGTDMPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR

Approximately 75-85 kDa,based on SDS-PAGE under reducing conditions.

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.