Thermo Fisher Scientific Human EGF Recombinant Protein, eBioscience

Applications

• Assay-dependent
• Control (Ctrl): Assay-dependent
• Publications: 3 references available on PubMed

Product Specifications

Product Specific Information

Recombinant Human EGF produced in E. coli is a single, non-glycosylated polypeptide chain containing 53 amino acids and has a molecular mass of approximately 6.2 kDa.
Epidermal growth factor (EGF) profoundly influences differentiation of specific cells in vivo and acts as a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin.

The EGF precursor exists as a membrane-bound molecule that is proteolytically cleaved to generate the 53-amino acid peptide hormone stimulating cell division. EGF promotes growth of various epidermal, epithelial tissues, and fibroblasts both in vivo and in vitro.

Purity: >98%
Molecular Weight: 6.2 kDa

Target Information

EGF (Epidermal Growth Factor) functions by binding to the EGF Receptor (EGFR), a 170 kDa protein kinase. EGFR activation triggers diverse cellular pathways in response to environmental stimuli. Upon EGF binding, EGFR forms homo- or heterodimers with other family members, each initiating distinct signaling cascades through recruitment of SH2-containing effector proteins.

EGF is widely expressed in kidney, cerebrum, prostate, and salivary glands. It acts as a potent mitogenic factor, and phosphorylated EGFR recruits adapter proteins such as GRB2 to activate complex downstream signaling cascades. EGF activates multiple signaling pathways including RAS-RAF-MEK-ERK, PI3K-AKT, PLCγ-PKC, and STAT modules. Studies also suggest involvement in NF-κB signaling regulation.

Defects in the EGF gene are associated with hypomagnesemia type 4 and dysregulation has been linked to cancer progression.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.