Recombinant Human epidermal growth factor Protein, Tag Free, Animal Free

• Cat.No.: EGF-06H
• Product Overview: Recombinant human EGF (971-1023aa) protein without tag was expressed in E. coli and purified by conventional column chromatography, after refolding of the isolated inclusion bodies in a renaturation buffer. Produced using nonanimal reagents in an animal-free laboratory.

Specification

• Species: Human
• Source: E.coli
• Tag: Non
• Protein Length: 971-1023aa
• Description: This gene encodes a member of the epidermal growth factor superfamily. The encoded preproprotein is proteolytically processed to generate the 53-amino acid epidermal growth factor peptide. This protein acts a potent mitogenic factor that plays an important role in the growth, proliferation and differentiation of numerous cell types. This protein acts by binding with high affinity to the cell surface receptor, epidermal growth factor receptor. Defects in this gene are the cause of hypomagnesemia type 4. Dysregulation of this gene has been associated with the growth and progression of certain cancers. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed.
• Tag: Non
• Form: Liquid
• Bio-activity: Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 0.1 ng/mL.
• Molecular Mass: 6.3 kDa
• AA Sequence: MNSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELRGeneralReferences
• Endotoxin: < 1 EU/μg of protein (determined by LAL method)
• Purity: > 95% by SDS-PAGE
• Applications: SDS-PAGE, Bioactivity
• Notes: For research use only. This product is not intended or approved for human, diagnostics or veterinary use.
• Storage: Can be stored at +2 to +8 centigrade for 1 week. For long term storage, aliquot and store at -20 to -80 centigrade. Avoid repeated freezing and thawing cycles.
• Storage Buffer: Phosphate-Buffered Saline (pH 7.4)
• Concentration: 1 mg/mL (determined by Bradford assay)
• References: 1. Riese., et al (1998 ) Bioessays. 20: 41-48.
  2. Cohen S., (1983) Cancer. 15: 1787-1791.
  3. Carpenter G., et al (1979) Annu. Rev. Biochem., 48: 193-216.

Gene Information

• Gene Name: EGF epidermal growth factor [ Homo sapiens (human) ]
• Official Symbol: EGF
• Synonyms: EGF; epidermal growth factor; URG; HOMG4; pro-epidermal growth factor; beta-urogastrone
• Gene ID: 1950
• mRNA Refseq: NM_001963
• Protein Refseq: NP_001954
• MIM: 131530
• UniProt ID: P01133

Case Study

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.

Application

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.

Fig1. Proposed model of synergistic induction of transdifferentiation from astrocytes to oligodendrocytes by EGF and Sox10. (Xinyu Liu, 2022)