Analytical Data
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Gene name
EED
- Application
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Alternative Names
EED;Polycomb Protein EED
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75530
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Expression Region
1-441aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMSEREVSTAPAGTDMPAAKKQKLSSDE NSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKK CKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECH SQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINP ITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVA IFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKES YDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENA IVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKML ALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIA VCDDASIWRWDRLR
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Molecular Weight
53 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
EED (Embryonic Ectoderm Development) is a critical component of the PRC2 (Polycomb Repressive Complex 2), which plays a significant role in epigenetic regulation during development and cell differentiation. Research on EED has gained momentum due to its involvement in various biological processes, including stem cell maintenance, X-chromosome inactivation, and tumorigenesis. The understanding of EED’s function has been propelled by advancements in proteomics and structural biology, which have unveiled its interactions with histone modifications and other regulatory proteins. These insights have significant implications for cancer research, as aberrations in the PRC2 complex, where EED is a pivotal player, are often linked to malignancies. By investigating the structure and function of EED, scientists aim to unravel its mechanistic role in gene silencing and cellular identity. Moreover, reconstituted EED proteins serve as valuable tools for drug discovery, specifically targeting its pathways in cancer therapy. The study of EED not only enhances our understanding of fundamental biological processes but also opens avenues for developing novel therapeutic strategies against diseases associated with Polycomb misregulation.
