Recombinant Human EED Protein (His & GST Tag)

Name: Recombinant Human EED Protein (His & GST Tag)
Brand: Beta LifeScience
SKU: BLPSN-1704
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His&GST
Host Species	Human
Accession	O75530
Synonym	HEED, WAIT1
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.
Description	A DNA sequence encoding the human EED (O75530-1) (Met 1-Arg 441) was fused with the N-terminal His-tagged GST tag at the N-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Met
AA Sequence	Met 1-Arg 441
Molecular Weight	The recombinant human EED/GST chimera consists of 678 a.a. and has a calculated molecular mass of 78 kDa. It migrates as an approximately 75-85 kDa band in SDS-PAGE under reducing conditions.
Purity	>93% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 8.0, 2mM GSH, 10% gly.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.