Analytical Data
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Gene name
COPE
- Application
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Alternative Names
COPE;Coatomer subunit epsilon
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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
O14579
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Expression Region
1-308aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMAPPAPGPASGGSGEVDELFDVKNAFY IGSYQQCINEAQRVKLSSPERDVERDVFLYRAYLAQRKFGVVLDEIKPSS APELQAVRMFADYLAHESRRDSIVAELDREMSRSVDVTNTTFLLMAASIY LHDQNPDAALRALHQGDSLECTAMTVQILLKLDRLDLARKELKRMQDLDE DATLTQLATAWVSLATGGEKLQDAYYIFQEMADKCSPTLLLLNGQAACHM AQGRWEAAEGLLQEALDKDSGYPETLVNLIVLSQHLGKPPEVTNRYLSQL KDAHRSHPFIKEYQAKENDFDRLVLQYAPSA
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Molecular Weight
37 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
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Protein Description
COPE (Cytosolic Oligomeric Protein Exosome) is a crucial protein involved in various cellular processes, including membrane trafficking, secretion, and cytoskeletal organization. It plays a significant role in maintaining cellular homeostasis by regulating the transport of proteins and lipids within the cell. Recent studies have highlighted its involvement in pathophysiological conditions, such as neurodegenerative diseases and cancer, where its dysregulation can lead to altered cellular functions and contribute to disease progression. The structural characterization of COPE, particularly its oligomeric states, provides insights into its functional mechanisms and interactions with other cellular components. By employing advanced techniques like cryo-electron microscopy and nuclear magnetic resonance spectroscopy, researchers aim to elucidate the dynamics of COPE assembly and its functional implications in the cell. Understanding the biochemical pathways involving COPE could pave the way for novel therapeutic strategies to target diseases associated with its dysfunction. Therefore, the study of COPE not only enhances our fundamental knowledge of cellular biology but also opens avenues for developing interventions in various human diseases.
