EGF (1-51), Human
Saccharomyces cerevisiae
Urogastrone, URG, EGF.
Sterile Filtered White lyophilized (freeze-dried) powder.
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
Epidermal Growth Factor (1-51 a.a.) Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 6.0kDa. The EGF is purified by proprietary chromatographic techniques.
Product Specs
Epidermal growth factor (EGF) plays a crucial role in cell differentiation, acting as a potent mitogen for various cultured cells. It stimulates the growth of epidermal, epithelial, and fibroblast cells. EGF is synthesized as a membrane-bound precursor and then proteolytically cleaved into a 53-amino acid peptide hormone that promotes cell division.
This product is a recombinant human Epidermal Growth Factor (EGF) comprising amino acids 1-51. It is produced in yeast and purified as a single, glycosylated polypeptide chain with a molecular weight of 6.0 kDa. The purification process involves proprietary chromatographic techniques.
Sterile, lyophilized powder with a white color.
The product is lyophilized from a 0.2 µm filtered solution in phosphate-buffered saline (PBS) at pH 7.4.
To reconstitute, dissolve the lyophilized EGF in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions.
The lyophilized EGF is stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated below -18°C. After reconstitution, store the solution at 4°C for up to 7 days. For long-term storage, keep it at -18°C. Avoid repeated freeze-thaw cycles.
The purity of this product is greater than 98%, as determined by reversed-phase high-performance liquid chromatography (RP-HPLC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
The ED50, determined by a cell proliferation assay using murine Balb/c 3T3 cells, is less than 0.1 ng/ml. This corresponds to a specific activity greater than 1.0 × 107 IU/mg.
Urogastrone, URG, EGF.
Saccharomyces cerevisiae
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Product Science Overview
Epidermal Growth Factor (EGF) is a crucial cytokine that plays a significant role in regulating various cellular processes. The recombinant form of EGF, specifically the 1-51 amino acid sequence, has been extensively studied for its potential therapeutic applications. This article delves into the background, molecular dynamics, and therapeutic promise of Epidermal Growth Factor (1-51 a.a.)(Human Recombinant).
Epidermal Growth Factor (1-51 a.a.) Human Recombinant is a single, glycosylated polypeptide chain containing 51 amino acids. It has a molecular mass of approximately 6.0 kDa . The recombinant EGF is produced in yeast (Saccharomyces cerevisiae) and is purified using proprietary chromatographic techniques .
EGF exerts its effects by binding to the EGF receptor (EGFR), a 170 kDa protein kinase. This binding initiates various cellular pathways, including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC, and STAT modules . These pathways are crucial for cell proliferation, differentiation, and survival. The ED50 of EGF (1-51 a.a.) is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is less than 0.1 ng/ml, corresponding to a specific activity of greater than 1.0 × 10^7 IU/mg .
Recombinant human EGF has shown promise in various therapeutic applications. It is used to treat diabetic foot ulcers, where it can be administered by injection into the wound site or applied topically . EGF stimulates the growth of several epidermal and epithelial tissues in vivo and in vitro, making it a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin .
Lyophilized EGF is stable at room temperature for up to three weeks but should be stored desiccated below -18°C for long-term storage. Upon reconstitution, it should be stored at 4°C for short-term use (2-7 days) and below -18°C for future use. It is essential to prevent freeze-thaw cycles to maintain its stability .
