Analytical Data
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Gene name
EREG
- Application
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Alternative Names
EREG;Proepiregulin
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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
O14944
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Expression Region
60-108aa
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AA Sequence
MVAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL
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Molecular Weight
19 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
EREG (Epiregulin) is a member of the epidermal growth factor (EGF) family and plays a crucial role in various biological processes, including cell proliferation, differentiation, and tissue repair. Initially identified for its involvement in skin and epithelial tissues, EREG has gained attention for its implications in cancer biology, particularly in promoting tumor growth and metastasis. Research indicates that EREG is often overexpressed in several types of cancer, such as colorectal, breast, and lung cancers, making it a potential biomarker for cancer diagnosis and prognosis. Additionally, EREG functions by binding to the epidermal growth factor receptor (EGFR), triggering signaling pathways that contribute to cellular growth and survival. Given its dual role in physiological processes and pathological conditions, EREG is a target of interest for therapeutic interventions. Studies focusing on the recombinant expression of EREG are critical for elucidating its functional mechanisms and interactions, enabling the development of EREG-targeted therapies. Current research aims to provide insights into the structural and functional attributes of EREG, exploring its potential in personalized medicine and novel cancer treatments. Understanding the biochemistry of EREG at the molecular level will facilitate the discovery of inhibitors that could mitigate its oncogenic effects, thereby contributing to more effective cancer therapies.
