Active Recombinant Human EGF protein

Species :	Human
Source :	E. coli
Tag :	Non
Protein Length :	971-1023 aa
Form :	Lyophilized from 0.22μm filtered solution in PBS (pH 7.4).
Bio-activity :	Measured in a cell proliferation assay using Balb/C 3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.1 - 0.2 ng/mL.
Molecular Mass :	The protein has a predicted MW of 5.6 kDa same as Bis-Tris PAGE result.
Endotoxin :	Less than 0.2 EU per μg by the LAL method.
Purity :	> 95% as determined by Bis-Tris PAGE > 95% as determined by HPLC
Storage :	-20 to -80°C for 12 months as supplied from date of receipt. -80°C for 3 months after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Reconstitution :	It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.

Gene Name	EGF epidermal growth factor [ Homo sapiens ]
Official Symbol	EGF
Synonyms	EGF; epidermal growth factor; epidermal growth factor (beta urogastrone); pro-epidermal growth factor; beta-urogastrone; URG; HOMG4;
Gene ID	1950
mRNA Refseq	NM_001178130
Protein Refseq	NP_001171601
MIM	131530
UniProt ID	P01133

Case 1: Liu X, et al. Mol Med. 2022

Recent research reveals EGF-activated EGFR/Erk signaling drives Sox10-mediated astrocyte-to-oligodendrocyte transdifferentiation, enhancing spinal cord injury repair through dual-phase reprogramming (astrocyte precursors → O4+ iOPCs) and glial scar reduction. In vitro/vivo studies confirm EGF promotes Olig1/Olig2 expression via Erk1/2, offering therapeutic potential for neural regeneration and remyelination in CNS disorders. Key mechanisms involve pathological niche modulation and EGFR-dependent neural repair pathways.

Fig1. Purified cells were immunoreactive to GFAP and EGFR antibodies.

Fig2. Western blotting analysis of GFAP, Nestin and Olig2 on d5 during the transdifferentiation process.

Case 2: Pascarelli S, et al. J Biol Chem. 2021

Recent study uncovers EGFR’s biased signaling via single EGF mutations, revealing conserved residues critical for receptor dimer stability and pathway activation. Combining molecular dynamics simulations with biochemical assays, researchers demonstrated that targeted EGF mutations alter EGFR phosphorylation patterns and cell proliferation without affecting ligand binding affinity. These findings highlight ligand-specific modulation of tyrosine kinase receptor outcomes, advancing precision drug design for cancer and neurological disorders through EGFR signaling pathways. Key insights include dimer interface dynamics and paralog-divergent residues as therapeutic targets in receptor-ligand interactions.

Fig1. Short-term effects on the phosphorylation level of EGFR Tyr-1173 after treating A431 cells.

Fig2. Apoptosis effect of WT or mutant EGF on A431 cells.

1. Applications of Recombinant EGF Protein in Biomedical and Therapeutic Fields Recombinant epidermal growth factor (EGF) protein, a bioactive molecule engineered through genetic modification, plays a pivotal role in tissue regeneration, wound healing, and cancer therapeutics. By activating EGFR signaling pathways, recombinant EGF accelerates cell proliferation, migration, and differentiation, making it invaluable in treating chronic wounds (e.g., diabetic ulcers) and corneal injuries. Clinical studies demonstrate its efficacy in reducing healing time by up to 40% compared to standard therapies. Additionally, its integration into advanced skincare formulations targets aging-related skin damage by stimulating collagen synthesis and epidermal repair. 2. Innovations in Research and Industrial Applications Beyond clinical use, recombinant EGF is critical in biotechnology and regenerative medicine. It serves as a key component in cell culture systems, enhancing the growth of stem cells and organoids for disease modeling and drug screening. In cancer research, EGF-dependent pathways are exploited to study tumor progression and develop targeted therapies. Emerging applications include tissue engineering scaffolds for nerve regeneration and 3D-printed implants. With advancements in personalized medicine, engineered EGF variants are being optimized for precision therapies, aligning with trends in CRISPR-based protein engineering and AI-driven drug design.