This recombinant human EGF is expressed as a GST-fusion protein, which allows for easy detection via western blot. The fusion junction of the protein harbors an engineered thrombin cleavage site and a protein kinase A (PKA) phosphorylation site. The GST portion of the fusion protein can be cleaved off by thrombin if necessary. The fusion protein can also be radioactively labeled with 32P-r-ATP and PKA.
Epidermal growth factor (EGF) is the founding member of the EGF family of mitogens possessing potent biological activities on numerous cell types. Other notable members of the family include HB-EGF, TGF-alpha, and four neuregulin isoforms. Human EGF is synthesized as a large precursor (1,208 amino acids), which is cleaved to generate the mature form containing 53 amino acids with three intramolecular disulfide linkages mediated by six highly conserved cysteine residues. The mature EGF peptide binds with high affinity to EGF receptor (ErbB) and elicits a signaling cascade, ultimately promoting DNA replication and cell proliferation. While insufficient ErbB signaling can cause degenerative diseases, excessive receptor activation is associated with oncogenic development.
From the laboratory of Te-Chung Lee, PhD, University at Buffalo.
Part of The Investigator's Annexe program.
|Name:||Human Epidermal Growth Factor (EGF)-GST|
|Source:||Recombinant, purified from E. coliBL21|
|Molecular Weight:||6.2kDa (~32 kDa with GST)|
|Amino Acid Sequence:||NSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELR|
|Storage:||Store at -80C|
EGF Activity Analysis
EGF activity assessed by its ability to stimulate the proliferation of HeLa cells in the absence of fetal bovine serum. Cells were treated with GST-EGF at the concentrations indicated, and MTT assay was performed 3 days after treatment.
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