Analytical Data
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Gene name
EGFR
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简介
EGFR Protein is a receptor tyrosine kinase that binds to ligands of the EGF family. EGFR Protein is involved in the regulation of NF-kappa-B , RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs signaling pathways. EGFR Protein has calmodulin binding activity, epidermal growth factor binding activity and epidermal growth factor activating receptor activity. EGFR Protein, Cynomolgus (HEK293, His) is the recombinant human-derived EGFR protein, expressed by HEK293 , with C-10*His labeled tag.
- Application
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Biological Activity
1.Immobilized EGF Protein, Human, Recombinant (ECD, hFc Tag) at 2 μg/mL (100 μL/well) can bind EGFR Protein, Cynomolgus, Recombinant (ECD, His Tag), the EC50 is 150-500 ng/mL. 2.Immobilized Anti-EGFR(MK)-IgG1 Antibody (Cetuximab) at 2 μg/mL (100 μL/well) can bind EGFR Protein, Cynomolgus, Recombinant (ECD, His Tag),the EC50 is 2-8 ng/mL. 3.Immobilized Cynomolgus EGFR, at 2 μg/mL (100μL/well) can bind Human EGF. The ED50 for this effect is 4.983 ng/mL.
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Alternative Names
Epidermal growth factor receptor; EGFR; ERBB; ERBB1; HER1
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Species
Cynomolgus
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Source
HEK293
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Tag
C-10*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
XP_005549616
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Expression Region
L25-S645
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AA Sequence
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSEFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDTLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSSQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCQNVSRGRECVDKCNILEGEPREFVENSECIQCHPECLPQVMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCARNGPKIPS
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Protein Length
Extracellular Domain
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Molecular Weight
80-100 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
Epidermal Growth Factor Receptor (EGFR) is a transmembrane protein that plays a crucial role in cell growth, proliferation, and survival. Its dysregulation is commonly associated with various cancers, making it a pivotal target for therapeutic intervention. Research into recombinant EGFR proteins has gained momentum due to their potential applications in cancer biology and targeted therapies. The expression of EGFR is often upregulated in malignant tumors, where it mediates signaling pathways that promote tumorigenesis. As a result, scientists have focused on generating recombinant EGFR proteins to better understand its structure-function relationship and to develop novel inhibitors that can block its activity. Furthermore, recombinant EGFR proteins can serve as valuable tools for studying ligand-receptor interactions, developing diagnostic assays, and screening potential therapeutic compounds. The advent of advanced biotechnological techniques has made it easier to produce these proteins in sufficient quantities and with desired modifications, thus enabling detailed studies. As our understanding of EGFR continues to evolve, the ongoing research into its recombinant forms not only enhances our knowledge of cancer biology but also holds promise for improving treatment strategies and patient outcomes in EGFR-related malignancies.
