Recombinant Human EGFR Fc Chimera Avi-tag Protein, CF

Catalog #: AVI344 Datasheet / COA / SDS

Biotinylated

Catalog #	Availability	Size / Price	Qty
AVI344-050

Recombinant Human EGFR Fc Chimera Avi-tag Protein Binding Activity

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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human EGFR Fc Chimera Avi-tag Protein, CF Summary

Learn more about Avi-tag Biotinylated Proteins

Product Specifications

Accession #

CAA25240.1

Structure / Form

Disulfide-linked homodimer, biotinylated via Avi-tag

Predicted Molecular Mass

97 kDa

SDS-PAGE

110-130 kDa, under reducing conditions

Product Datasheets

AVI344

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.

AVI344

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:	Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.

Scientific Data

Binding Activity

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When Human EGFR (Research Grade Cetuximab Biosimilar) Antibody (Catalog # MAB9577) is immobilized at 0.25 µg/mL, 100 µL/well, the concentration of Recombinant Human EGFR Fc Chimera Avi-tag (Catalog # AVI344) that produces 50% of the optimal binding response is approximately 2-15 ng/mL.

SDS-PAGE

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2 μg/lane of Biotinylated Recombinant Human EGFR Fc Chimera Avi-tag (Catalog # AVI344) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 110-130 kDa and 220-260 kDa, respectively.

Reconstitution Calculator

Background: EGFR

The EGFR subfamily of receptor tyrosine kinases comprises four members: EGFR (also known as HER-1, ErbB1, or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoproteins with an extracellular ligand binding domain containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain followed by multiple tyrosine autophosphorylation sites (1-4). Soluble receptors consisting of the extracellular ligand binding domain are generated by alternate splicing in human and mouse (5‑7). Within the mature ECD, human EGFR shares 88% aa sequence identity with mouse and rat EGFR. Human EGFR shares 43%-44% aa sequence identity with the ECD of human ErbB2, ErbB3, and ErbB4. 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 (8‑12). 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 (13, 14). EGFR is overexpressed in a wide variety of tumors and is the target of several anti-cancer drugs (15).

References

Singh, A.B. and R.C. Harris (2005) Cell. Signal. 17:1183.
Shilo, B.Z. (2005) Development 132:4017.
Lin, C. et al. (1984) Science 224:843.
Ullrich, A. et al. (1984) Nature 309:418.
Reiter, J.L. and N.J. Maihle (1996) Nucleic Acids Res. 24:4050.
Reiter J.L. et al. (2001) Genomics 71:1.
Xu, Y.H. et al. (1984) Nature 309:806.
Graus-Porta, D. et al. (1997) EMBO J. 16:1647.
Yarden, Y. et al. (1987) Biochemistry 26:1434.
Burgess, A.W. et al. (2003) Mol. Cell 12:541.
Lemmon, M.A. et al. (1997) EMBO J. 16:281.
Cohen, S. et al. (1982) J. Biol. Chem. 257:1523.
Sibilia, M. and E.F. Wagner (1995) Science 269:234.
Miettinen, P.J. et al. (1995) Nature 376:337.
Roskoski Jr., R. (2004) Biochem. Biophys. Res. Commun. 319:1.

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