Analytical Data
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Gene name
EGFR
- Application
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Alternative Names
Proto-oncogene c-ErbB-1 Receptor tyrosine-protein kinase erbB-1 ERBB, ERBB1, HER1
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 85% as determined by SDS-PAGE.
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Uniprot
P00533
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Expression Region
669-684aa
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Protein Length
Partial
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Molecular Weight
22.2 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
Epidermal Growth Factor Receptor (EGFR) is a transmembrane protein that plays a critical role in cell signaling pathways regulating cell proliferation, differentiation, and survival. Abnormal activation of EGFR is closely associated with various human cancers, including non-small cell lung cancer (NSCLC) and colorectal cancer, making it a pivotal target for therapeutic intervention. The study of recombinant EGFR proteins has gained momentum due to their potential in understanding the molecular mechanisms of EGFR signaling and developing targeted therapies. Researchers aim to express and purify recombinant EGFR proteins to investigate their structure, function, and interactions with ligands and inhibitors. This research not only contributes to the fundamental understanding of EGFR biology but also facilitates the development of monoclonal antibodies and small molecule inhibitors that can selectively inhibit EGFR activity. Moreover, recombinant EGFR proteins have applications in drug discovery and the design of personalized medicine strategies, aiming to improve patient outcomes in EGFR-driven cancers. The insights gained from these studies are expected to lead to more effective treatment options and strategies for overcoming resistance mechanisms associated with EGFR-targeted therapies.
