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P01133-Human EGF-3d structure.jpg P01133-Human EGF-3d structure.jpg

Human EGF+Cell Based Assay.jpg Human EGF+Cell Based Assay.jpg Induces proliferation in BALB/c 3T3 cells. ED50: 60-450 pg/ml (QC verified).

Induces proliferation in BALB/c 3T3 cells. ED50: 60-450 pg/ml (QC verified).

Human EGF+SDS-PAGE.jpg Human EGF+SDS-PAGE.jpg Greater than 95% as determined by reducing SDS-PAGE.

Greater than 95% as determined by reducing SDS-PAGE.

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Recombinant Human EGF is a human-derived recombinant epidermal growth factor, expressed in Escherichia coli without a tag. It is a small-molecule polypeptide consisting of 53 amino acids and containing three disulfide bonds, classified as a potent mitogenic factor. It participates in the regulation of molecular mechanisms related to normal cell growth, can stimulate the proliferation of epidermal, epithelial tissues and some fibroblasts in in vitro assays, shares high sequence and functional homology with human transforming growth factor α (hTGF α), and can competitively bind to EGF receptor sites.

Synonyms: Recombinant Human EGF; Pro-Epidermal Growth Factor; EGF

4.5 *For Research Use Only! Not for Human Use. We Do Not Sell to Patients.

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Product Details of Human EGF

M.W : 6.2 KDa
SMILES Code : NONE
Synonyms :
Recombinant Human EGF; Pro-Epidermal Growth Factor; EGF
English Name :Recombinant Human EGF

Safety of Human EGF

Isoform Comparison

Biological Activity

Description
Epidermal growth factor (EGF) is a small protein consisting of 53 amino acid residues with three disulfide bridges. As a small mitogenic protein, it is involved in mechanisms such as normal cell growth and wound healing. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro, as well as some fibroblasts in cell culture. This protein shows high sequential and functional homology with human type-alpha transforming growth factor (hTGF alpha), a competitor for EGF receptor sites. EGF is a single-pass type I membrane protein containing 8 LDL-receptor class B repeats and 9 EGF-like domains, which regulates cellular proliferation, differentiation, and survival. Initially purified from the mouse submandibular gland, EGF has since been found in many human tissues including the submandibular gland and parotid gland. Salivary EGF, which is also regulated by dietary inorganic iodine, plays an important physiological role in maintaining the integrity of oro-esophageal and gastric tissues. Its biological effects include stimulating DNA synthesis and protecting the mucosa from intraluminal injurious factors such as gastric acid, bile acids, pepsin, trypsin, as well as physical, chemical and bacterial agents. This recombinant protein is applicable for molecular mechanism research related to epithelial tissue growth regulation and mucosal protection.
 

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