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EED Protein, Human, Recombinant (His & GST)

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EED Protein, Human, Recombinant (His & GST)

Catalog No. TMPY-02379

EED is essential for regulating the repressive histone modification, histone 3 lysine 27 tri-methylation (H3K27me3) at many developmental genes. EED depletion significantly impeded erythroid maturation. EED depletion impaired the generation of hematopoietic stem cells. The function of EED within polycomb repressive complex 2 (PRC2) is mediated by a complex network of protein-protein interactions. The targeted disruption of EED's reader function can lead to allosteric inhibition of PRC2 catalytic activity. Eed(Delta/Delta) HSPCs exhibited increased attachment to a major extracellular matrix component, fibronectin. Thus, EED deficiency increases proliferation on one side but promotes quiescence possibly by enhanced adhesion to the hematopoietic niche on the other, and these conflicting events would lead to abnormal differentiation and functional defect of Eed(Delta/Delta) HSPCs.

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Pack Size	Price	Availability	Quantity
100 μg	$600	7-10 days

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Biological Description

Biological Information	Testing in progress
Description	EED is essential for regulating the repressive histone modification, histone 3 lysine 27 tri-methylation (H3K27me3) at many developmental genes. EED depletion significantly impeded erythroid maturation. EED depletion impaired the generation of hematopoietic stem cells. The function of EED within polycomb repressive complex 2 (PRC2) is mediated by a complex network of protein-protein interactions. The targeted disruption of EED's reader function can lead to allosteric inhibition of PRC2 catalytic activity. Eed(Delta/Delta) HSPCs exhibited increased attachment to a major extracellular matrix component, fibronectin. Thus, EED deficiency increases proliferation on one side but promotes quiescence possibly by enhanced adhesion to the hematopoietic niche on the other, and these conflicting events would lead to abnormal differentiation and functional defect of Eed(Delta/Delta) HSPCs.
Species	Human
Expression System	Baculovirus Insect Cells
Tag	His, GST
Accession Number	O75530-1
Synonyms	HEED,WAIT1,embryonic ectoderm development
Construction	The Human EED (O75530-1) (Met 1-Arg 441) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
Protein Purity	> 93 % as determined by SDS-PAGE
Molecular Weight	78 kDa (predicted)
Endotoxin	< 1.0 EU/μg of the protein as determined by the LAL method.
Formulation	Lyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM Tris, 500 mM NaCl, pH 8.0, 2 mM GSH, 10% gly. Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization.
Reconstitution	A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage	It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	In general, Lyophilized powders are shipping with blue ice.
Research Background	EED is essential for regulating the repressive histone modification, histone 3 lysine 27 tri-methylation (H3K27me3) at many developmental genes. EED depletion significantly impeded erythroid maturation. EED depletion impaired the generation of hematopoietic stem cells. The function of EED within polycomb repressive complex 2 (PRC2) is mediated by a complex network of protein-protein interactions. The targeted disruption of EED's reader function can lead to allosteric inhibition of PRC2 catalytic activity. Eed(Delta/Delta) HSPCs exhibited increased attachment to a major extracellular matrix component, fibronectin. Thus, EED deficiency increases proliferation on one side but promotes quiescence possibly by enhanced adhesion to the hematopoietic niche on the other, and these conflicting events would lead to abnormal differentiation and functional defect of Eed(Delta/Delta) HSPCs.