| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | beta-urogastrone,EGF,epidermal growth factor, MEGF, HOMG4, URG, Urogastrone; EGF，beta-urogastrone,EGF,epidermal growth factor, MEGF, 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, MEGF, HOMG4, URG, Urogastrone; EGF，beta-urogastrone,EGF,epidermal growth factor, MEGF, HOMG4, URG, Urogastrone.
Species origin: Mouse.
Endotoxin:<0.1 EU per 1 μg of the protein by the LAL method.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some
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: Mouse
- Molecular weight: The protein has a calculated MW of 6.98 kDa.
- Protein length: The recombinant mouse EGF consists of 55 amino acids and predicts a molecular mass of 6.2 KDa
- Expression region: Amino acid sequence derived from Mouse EGF (Met978-Arg 1029)(P01132) was expressed
- Purity: > 95% 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.
