Recombinant Human EGFR His-tag Protein, CF

Catalog #: 11302-ER Datasheet / COA / SDS

HEK293 Expressed

Catalog #	Availability	Size / Price	Qty
11302-ER-050

Recombinant Human EGFR His-tag Protein Binding Activity.

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Product Details

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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

11302-ER

Product Datasheet

COA

SDS

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

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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

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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.

Reconstitution Calculator

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

Singh, A.B. and R.C. Harris (2005) Cell. Signal. 17:1183.
Shilo, B.Z. (2005) Development 132:4017.
Guillaudeau, A. et al. (2012) PLoS One. 7:1.
Reiter J.L. et al. (2001) Genomics 71:1.
Gan HK et al. (2013) FEBS J. 280:5350
Freed, D. M. et al. (2017) Cell. 171:683.
Burgess, A.W. et al. (2003) Mol. Cell 12:541.
Faria, J.A. et al. (2016) BBRC. 478:39.
An Z. et al. (2018) Oncogene. 37:1561.
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