EGF Human, Pichia
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
The EGF is purified by proprietary chromatographic techniques.
Product Specs
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
Product Science Overview
EGF is a small polypeptide consisting of 53 amino acids and three disulfide bonds, with a molecular mass of approximately 6.2 kDa . It was first discovered in the mouse submaxillary gland and later isolated from human urine . EGF functions by binding to its receptor, EGFR, on the cell surface, triggering a cascade of downstream signaling pathways that lead to cellular proliferation and differentiation .
Pichia pastoris is a species of yeast commonly used as an expression system for producing recombinant proteins. It offers several advantages, including high growth rates, the ability to perform post-translational modifications, and the capacity to grow in simple, inexpensive media . The production of human recombinant EGF in Pichia pastoris involves the insertion of the human EGF gene into the yeast’s genome, followed by fermentation and purification processes .
The recombinant EGF produced in Pichia pastoris is typically purified using chromatographic techniques to achieve a purity greater than 98% . The protein is often lyophilized (freeze-dried) to enhance its stability and shelf life. 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 and below -18°C for long-term use, with the addition of a carrier protein to prevent freeze-thaw cycles .
The biological activity of recombinant EGF is measured by its ability to stimulate the proliferation of cells. For instance, the ED₅₀ (the dose required to achieve half-maximal effect) for murine BALB/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of 1 x 10⁷ Units/mg . This high level of activity makes recombinant EGF a valuable tool in research and therapeutic applications.
Recombinant EGF has a wide range of applications in both research and medicine. It is used in cell culture to promote the growth of various cell types, including epidermal and epithelial tissues . In medicine, EGF is explored for its potential in wound healing, treatment of ulcers, and other regenerative therapies . Its ability to stimulate cell proliferation and tissue repair makes it a promising candidate for developing new treatments for various conditions.
