Analytical Data
-
Gene name
EGF
- Application
-
Alternative Names
URG; Beta-Urogastrone; Pro-epidermal growth factor
-
Species
Dog
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 97% as determined by SDS-PAGE.
-
Uniprot
Q9BEA0
-
Expression Region
Ala611~Gly753
-
Protein Length
Partial
-
Molecular Weight
18kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Epidermal Growth Factor (EGF) is a crucial protein that plays a significant role in cell growth, proliferation, and differentiation, particularly within the epithelial tissues. The discovery of EGF in the 1960s by Herbert Tobias and subsequently its characterization by Jeffrey Lane, which led to the awarding of the Nobel Prize to Stanley Cohen in 1986, underscored its importance in various biological processes. EGF is recognized for its ability to bind to the EGF receptor (EGFR), activating signaling pathways that are critical in normal cellular functions, yet it is also implicated in several pathological conditions, notably cancer. As research progressed, the recombinant production of EGF became a focal point for both therapeutic and cosmetic applications. Recombinant EGF is synthesized using biotechnology techniques, which enable the production of high-purity EGF for use in wound healing, tissue regeneration, and skin care products. The therapeutic potential of EGF has led to extensive studies examining its effects on skin rejuvenation, scar reduction, and treatment of various dermatological disorders. Furthermore, its role in enhancing tissue repair and regeneration has spurred research into its applications in regenerative medicine. By understanding the mechanisms of EGF action and its interactions at the molecular level, researchers aim to optimize its therapeutic efficacy and explore novel applications, such as in cancer treatment and tissue engineering, highlighting the protein's versatility and importance in both health and disease management.
