EGF Mouse, His Active

Epidermal Growth Factor (EGF) is a protein that plays a crucial role in cell growth, proliferation, and differentiation. The recombinant form of EGF, specifically His-tagged EGF from mice, is widely used in research and biotechnology for its ability to stimulate cellular processes.

Mouse recombinant EGF is typically produced in Escherichia coli (E. coli) expression systems. The protein consists of 53 amino acid residues and has a molecular weight of approximately 6 kDa . The His-tag, a sequence of histidine residues, is added to the N-terminus of the protein to facilitate purification through affinity chromatography .

EGF exerts its biological effects by binding to the Epidermal Growth Factor Receptor (EGFR), a 170 kDa protein kinase . Upon binding, EGFR undergoes dimerization and autophosphorylation, initiating a cascade of downstream signaling pathways. These pathways include the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC, and STAT modules . These signaling cascades regulate various cellular processes such as proliferation, differentiation, and survival.

Recombinant mouse EGF is used extensively in cell culture to promote the growth and differentiation of various cell types derived from ectoderm and mesoderm . It is also employed in functional assays to study cellular responses to growth factor stimulation . The His-tagged version of EGF allows for easy purification and detection in experimental setups .

The lyophilized form of recombinant mouse EGF should be stored at -20°C and reconstituted in sterile PBS to a concentration of 0.1-1.0 mg/mL . Once reconstituted, the protein should be aliquoted and stored at ≤-20°C to avoid repeated freeze-thaw cycles .