| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | beta-urogastrone,EGF,epidermal growth factor, hEGF, HOMG4, URG, Urogastrone; EGF，beta-urogastrone,EGF,epidermal growth factor, hEGF, HOMG4, URG, Urogastrone |
| Biological Activity | |
| Expression System | |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Protein Length | |
| Purity | |
| Shipping | |
| Species | |
| Storage | |
| Target |
Background
EGF is supplied as a recombinant protein reagent for research use only. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.
Also known as: beta-urogastrone,EGF,epidermal growth factor, hEGF, HOMG4, URG, Urogastrone; EGF，beta-urogastrone,EGF,epidermal growth factor, hEGF, HOMG4, URG, Urogastrone.
Species origin: Human.
Endotoxin:<0.1 EU per 1 μg of the protein by the LAL method.
Epidermal growth factor (EGF) is a small growth factor containing 53 amino acid residues that promotes the proliferation of mesenchymal and epidermal cells. Mature proteins, much smaller than 53aa, are produced by protein hydrolysis in the proximal EGF domain across the membrane. EGF is well preserved in mammals, and the EGF in mature humans is 70% the same as that in mice and mice. EGF and fibroblast growth factor 2 (fgf-2) induce the proliferation of neural precursor cells isolated from specific parts of the embryonic and adult brain. EGF and somatopodin c supplemental medium were substituted for 5% thrombocytopenic anemia plasma (PPP) and had the ability to inhibit BALB/C-3T3 cell density. The biological activities of EGF include epithelium formation, angiogenesis, inhibition of gastric acid secretion, proliferation of fibroblasts, and colony formation of epidermal cells in culture.
Biological significance and function
Functionally, EGF mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as Oncology & Angiogenesis.
Molecular characteristics
Molecular characteristics: Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.
- Source species: Human
- Molecular weight: The protein has a calculated MW of 6.35 kDa.
- Protein length: The recombinant human EGF consisting of 54 amino acids and has a calculated molecular mass of 6.35 kDa as estimated in SDS-PAGE under reducing conditions
- Expression region: Amino acid sequence derived from Human EGF protein (Met 970-Arg1023)(P01133) was expressed
- Purity: > 96% as determined by SDS-PAGE.
Post-translational considerations: E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.
Expression and purification strategy
Expression system: E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.
Tagging: No tag tags are commonly used to streamline purification and enable capture/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.
Formulation: The protein was lyophilized from sterile 150 mM NaCl 20 mM Tris , pH 8.0. If you have any concerns or special requirements, please confirm with us.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.
Research interpretation
Research interpretation: Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.
