EGF Human

Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.

EGF was lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.

Greater than 98.0% as determined by SDS-PAGE.

The ED₅₀ as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x10⁷ IU/mg.

1.Title:Activation of the Hedgehog pathway in pilocytic astrocytomas.
Publication:Neuro Oncol (2010) 12 (8): 790-798. doi: 10.1093/neuonc/noq026 First published online: March 11, 2010
Link:EGF prospec publication

2.Title:Evaluation of bioactivity and effect of polymeric stabilizers during heat treatment for the unfolded fraction of human epidermal growth factor.
Publication:SEN'I GAKKAISHI vol.67,nov.8(2011)
Link:EGF Human prospec publication

3.Title:GPR56 is essential for testis development and male fertility in mice.
Publication:Article first published online: 27 OCT 2010 DOI: 10.1002/dvdy.22468
Link:Epidermal Growth Factor prospec publication

4.Title:Changing the Receptor Specificity of Anthrax Toxin.
Publication:doi: 10.1128/?mBio.00088-12 1 May 2012 mBio vol. 3 no. 3 e00088-12
Link:Epidermal Growth Factor Human prospec publication

5.Title:Characterization of Non-Specific Cytotoxic Cell Receptor Protein 1: A New Member of the Lectin-Type Subfamily of F-Box Proteins.
Publication:Kallio H, Tolvanen M, J?nis J, Pan P-w, Laurila E, et al. (2011) Characterization of Non-Specific Cytotoxic Cell Receptor Protein 1: A New Member of the Lectin-Type Subfamily of F-Box Proteins. PLoS ONE 6(11): e27152. doi:10.1371/journal.pone.0027152
Link:EGF Protein prospec publication

Publication:   Blood 116.5 (2010): 759-766.
Link: Epidermal Growth Factor Protein prospec publication   

SDS

About EGF:

In the sphere of biomedical studies, epidermal boom factor (EGF) is a cornerstone that gives precious insights into the mechanisms underlying tissue healing, differentiation, and mobile proliferation. In this article we will explore the characteristics and uses of epidermal growth factor (EGF).  

Description:

Epidermal growth factor (EGF) is a 6-kDa protein consisting of 53 amino acid residues and 3 intramolecular disulfide linkages. Human tissues, such as platelets, the parotid gland, and the submandibular gland, are rich in EGF. EGF, which was first discovered in human urine and the submaxillary glands of mice, functions as a major modulator of cell proliferation by attaching to its receptor, EGFR, which is found on the cell membrane. EGF triggers autophosphorylation of transmembrane protein tyrosine kinase EGFR upon binding, hence initiating downstream signaling cascades through pathways such as phosphatidylinositol and ras. Beyond the cell membrane, EGF has a variety of roles as it also initiates cytoplasmic processes such actin depolymerization and membrane ruffle formation. Studies indicate that EGF and its receptor might possibly be important components of the nucleus, highlighting the complexity of EGF-mediated cellular responses. 

Function:

By attaching to the epidermal growth factor receptor (EGFR), EGF promotes the survival, differentiation, and multiplication of cells. This connection is essential for boosting many physiological processes and stimulating cell proliferation. The preservation of oro-esophageal and stomach tissue integrity is greatly supported by salivary EGF, which is regulated by dietary inorganic iodine. Its actions include the healing of gastric and oral ulcers, the inhibition of gastric acid secretion, the stimulation of DNA synthesis, and the protection of mucosal surfaces against harmful substances such as bile acids, gastric acid, and bacteria. Salivary EGF's role extends to repairing gastric tissue and addressing oro-esophagal issues, showcasing its healing ability in resolving oral and gastrointestinal ailments, including ulcers. 

Mechanism:

EGF functions by forming a strong bond with the cell surface's epidermal growth factor receptor (EGFR), which triggers ligand- induced dimerization. This incident sets off the intrinsic protein-tyrosine kinase activity of EGFR, which in turn initiates a signal transduction cascade inside the cell. Numerous biochemical changes are brought about by this cascade, such as increased intracellular calcium levels, increased glycolysis and protein synthesis, and increased expression of particular genes, most notably the EGFR gene. These carefully planned alterations eventually promote DNA synthesis and cell division, illuminating the complex process by which EGF directs basic biological functions and modulates cellular responses.