Analytical Data
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Gene name
EPS15
- Application
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Alternative Names
EPS15;AF1P;Epidermal growth factor receptor substrate 15
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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
P42566
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Expression Region
657-798aa
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AA Sequence
CFFRQSTDPFATSSTDPFSAANNSSITSVETLKHNDPFAPGGTVVAASDSATDPFASVFGNESFGGGFADFSTLSKVNNEDPFRSATSSSVSNVVITKNVFEETSVKSEDEPPALPPKIGTPTRPCPLPPGKRSINKLDSPD
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Molecular Weight
20.9 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
EPS15, or Epithelial Protein Lost in Neoplasm 15, is a vital protein involved in the regulation of cellular processes such as endocytosis and cellular signaling. Its role as an adaptor protein makes it critical in the formation of clathrin-coated pits, thus influencing the internalization of various membrane receptors, including growth factor receptors. The research surrounding EPS15 gained momentum due to its association with cancer; altered expression levels of this protein have been observed in various neoplastic conditions, suggesting that it may function as a tumor suppressor. The reconstitution of EPS15, particularly in the context of cell signaling and endocytosis, has become a focal point for scientists aiming to decipher the molecular underpinnings of tumorigenesis. Furthermore, understanding the structure-function relationship of EPS15 can help in developing therapeutic strategies targeting cancer by restoring or mimicking its normal function. Recent advancements in biophysical techniques, including crystallography and cryo-electron microscopy, have provided insights into its structure, which in turn can aid in the design of small molecules to modulate its activity. Ultimately, studying EPS15 through recombinant techniques not only enhances our comprehension of its biological roles but also holds promise for novel cancer treatment methodologies.











