EGF Long Human
Epidermal Growth Factor Long Human Recombinant
Cat. No.
BT3222
Source
Escherichia Coli.
Synonyms
Urogastrone, URG, EGF.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs 
In Stock 
Description
Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa.
The EGF Long is purified by proprietary chromatographic techniques.
The EGF Long is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Epidermal growth factor (EGF) plays a crucial role in cell differentiation and acts as a potent mitogen for various cultured cells. Synthesized as a membrane-bound precursor, EGF undergoes proteolytic cleavage to release the active 53-amino acid peptide hormone. This hormone stimulates the growth of epidermal, epithelial, and fibroblast cells. Long EGF, a recombinant analog of Human EGF, serves as a suitable replacement for therapeutic cell culture, effectively substituting Recombinant Human or native EGF. It encompasses the Human EGF amino acid sequence with an additional 53 amino acid N-terminal extension peptide.
Description
Produced in E.coli cells, Recombinant Human EGF Long is a non-glycosylated polypeptide chain composed of 106 amino acids, with a molecular weight of 12.3kDa. The purification process utilizes proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.
Solubility
Reconstitute the lyophilized EGF Long in sterile 100mM acetic acid (AcOH) at a minimum concentration of 100µg/ml. This solution can be further diluted with other aqueous solutions.
Stability
Lyophilized EGF Long remains stable at room temperature for up to 3 weeks. For extended storage, store desiccated below -18°C. Reconstituted EGF Long should be stored at 4°C for 2-7 days or below -18°C for longer periods. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 95.0% as determined by: (a) RP-HPLC analysis and (b) SDS-PAGE analysis.
Biological Activity
The ED50, as determined by a cell proliferation assay using murine Balb/c 3T3 cells, is less than 1.0 ng/ml. This corresponds to a specific activity greater than 1.0 × 106 IU/mg.
Synonyms
Urogastrone, URG, EGF.
Source
Escherichia Coli.
Amino Acid Sequence
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
Product Science Overview
Structure and Composition
Production and Purity
LONG® EGF is produced in Escherichia coli (E. coli) and is free of animal-derived components . It is manufactured according to current Good Manufacturing Practices (cGMP) standards, ensuring high purity and consistency . The production facility is regularly audited by European and US contract manufacturers and biopharmaceutical companies .
Applications
Handling and Usage
The recommended concentration range for LONG® EGF in media is 10 - 50 μg/l, with a maximum concentration not exceeding 100 μg/l . It is advised to reconstitute the vial to the recommended concentration of 1 mg/ml in 10 mM HCl . Care should be taken to perform all activities in a controlled environment using aseptic techniques .
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