Recombinant Human EGFR Protein

R&D Systems, part of Bio-Techne | Catalog # 1095-ER

R&D Systems, part of Bio-Techne
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1095-ER-002
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Key Product Details

Source

NS0

Accession #

CAA25240

Conjugate

Unconjugated

Applications

Bioactivity

View all EGFR Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human EGFR protein
Met1-Ser645

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Leu25

Predicted Molecular Mass

68.6 kDa

SDS-PAGE

110-115 kDa, reducing conditions

Activity

Bioassay data are not available.

Reviewed Applications

Read 1 review rated 4 using 1095-ER in the following applications:

Formulation, Preparation and Storage

1095-ER
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitution Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
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.

Background: EGFR

The epidermal growth factor receptor (EGFR) subfamily of receptor tyrosine kinases comprises four members: EGFR (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER2), ErbB3 (HER3), and ErbB4 (HER4). All family members are type I transmembrane glycoproteins that have an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGFR gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 alpha in the absence of a co-receptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis (1-3).

References

  1. Daly, R.J. (1999) Growth Factors, 16:255.
  2. Schlessinger, J. (2000) Cell. 103:211.
  3. Maihle, N.J. et al. (2002) Cancer Treat. Res. 107:247.

Long Name

Epidermal Growth Factor Receptor

Alternate Names

EGF R, ErbB, ErbB1, HER-1

Entrez Gene IDs

1956 (Human); 13649 (Mouse); 24329 (Rat); 102138724 (Cynomolgus Monkey)

Gene Symbol

EGFR

UniProt

CAA25240

Additional EGFR Products

Product Documents for Recombinant Human EGFR Protein

Product Datasheets

Certificate of Analysis

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Product Specific Notices for Recombinant Human EGFR Protein

For research use only

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