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Recombinant Human EGFR His-tag Protein, CF

Catalog #: 11302-ER Datasheet
HEK293 Expressed
Catalog # Availability Size / Price Qty
11302-ER-050
Recombinant Human EGFR His-tag Protein Binding Activity.
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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human EGFR His-tag Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. When Human EGFR (Research Grade Cetuximab Biosimilar) Antibody  (Catalog # MAB9577) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human EGFR His-tag (Catalog # 11302-ER) binds with an ED50 of 1.25-15.0 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human EGFR protein
Leu25-Ser645, with a C-terminal 6-His tag
Accession #
CAA25240.1
N-terminal Sequence
Analysis
Leu25
Predicted Molecular Mass
69 kDa
SDS-PAGE
94-104 kDa, under reducing conditions.

Product Datasheets

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11302-ER

Product Datasheet

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

11302-ER

Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution Reconstitute at 500 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Scientific Data

Binding Activity View Larger

When Human EGFR (Research Grade Cetuximab Biosimilar) Antibody (MAB9577) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human EGFR His-tag (Catalog # 11302-ER) binds with an ED50 of 1.25-15.0 ng/mL.

SDS-PAGE View Larger

2 μg/lane of Recombinant Human EGFR His-tag Protein (Catalog # 11302-ER) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 94-104 kDa.

Background: EGFR

Epidermal growth factor receptor (EGFR), also known as HER-1 and ErbB1, is a member of a subfamily of receptor tyrosine kinases comprised of four members: EGFR, ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoproteins with an extracellular domain (ECD) containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a tyrosine kinase domain followed by multiple tyrosine autophosphorylation sites (1, 2). Several soluble isoforms lacking the intracellular domain are generated by alternate splicing, along with a tumor specific mutant EGFRvIII, are known to exist (3-5). The ECD of mature, full-length EGFR shares 88% and 89% amino acid sequence identity with mouse and rat EGFR, respectively. EGFR binds a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, HB-EGF, and epigen (1, 2). Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, heterodimerization tyrosine phosphorylation and cell signaling (6-8). EGFR can also be recruited to form heterodimers with the ligand‑activated ErbB3 or ErbB4. EGFR signaling regulates multiple biological functions including cell proliferation, differentiation, motility, and apoptosis (6-8). EGFR is overexpressed in a wide variety of tumors, with EGFRvIII overexpressed particularly in glioblastoma multiforme (GMB) and is the target of several anti-cancer therapeutics (5,9,10).

References
  1. Singh, A.B. and R.C. Harris (2005) Cell. Signal. 17:1183.
  2. Shilo, B.Z. (2005) Development 132:4017.
  3. Guillaudeau, A. et al. (2012) PLoS One. 7:1.
  4. Reiter J.L. et al. (2001) Genomics 71:1.
  5. Gan HK et al. (2013) FEBS J. 280:5350
  6. Freed, D. M. et al. (2017) Cell. 171:683.
  7. Burgess, A.W. et al. (2003) Mol. Cell 12:541.
  8. Faria, J.A. et al. (2016) BBRC. 478:39.
  9. An Z. et al. (2018) Oncogene. 37:1561.
  10. Lee, C. K. et al. (2017) J. Thoracic Oncology. 12:403.
Long Name
Epidermal Growth Factor Receptor
Entrez Gene IDs
1956 (Human); 13649 (Mouse); 24329 (Rat); 102138724 (Cynomolgus Monkey)
Alternate Names
avian erythroblastic leukemia viral (v-erb-b) oncogene homolog; cell growth inhibiting protein 40; cell proliferation-inducing protein 61; EC 2.7.10; EC 2.7.10.1; EGF R; EGFR; epidermal growth factor receptor (avian erythroblastic leukemia viral (v-erb-b)oncogene homolog); epidermal growth factor receptor; ErbB; ErbB1; ERBB1PIG61; HER1; HER-1; mENA; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1

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