EGF Protein, Human

EGF Protein is a potent epidermal growth factor that belongs to EGF-family of proteins. EGF Protein stimulates cell growth and differentiation by binding to epidermal growth factor receptor (EGFR) found in many human tissues, including platelets, submandibular gland (submaxillary gland) and parotid gland. EGF Protein has effects such as wound healing, anti-intestinal atrophy, anti-cancer, reducing ureteral obstruction and assisting in nerve tissue regeneration, mainly used in wound healing applications. EGF Protein (Human) is a recombinant protein with tag free that consists of 53 amino acids with three intramolecular disulfide bonds and is produced in E. coli^{[1],[2],[3],[4],[5],[6],[7]}.

Recombinant Human Epidermal Growth Factor is chemically identical to the natural material, exhibits full biological activity and is ued in wound healing applications. Recombinant Human Epidermal Growth Factor (rhEGF) stimulates proliferation of the fibroblast BALB/c3T3 cell line. Recombinant Human Epidermal Growth Factor released from hydrogels keeps its bioactivity, induces EGF receptor expression, causes proliferating cell nuclear antigen and shows therapeutic potential in enhancing diabetic wound healing^[1,2].
EGF Protein (Human) promotes cellular proliferation, differentiation and survival by binding to epidermal growth factor receptor (EGFR) on the cell surface with high affinity^[1].
The biological effects of salivary EGF Protein (Human) include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents^[3].
EGF Protein (Human) works as an enhancer of mineralization during differentiation of mesenchymal stem cells (MSCs) derived from bone marrow. EGF Protein (Human) is capable of increasing calcium deposit formation as well as ALP and OCN gene expression, which is promising for research of an effective adjuvant to improve bone regeneration in periodontics and oral implantology^[4,5].

EGF Protein (Human) (10 ng/mL, 7 days) shows polygonalshaped appearance with spherical-peripheral nuclei, low cytoplasm content and shows strongt inhibitory effect on the expression levels of CD146 and CD10 in dental pulp stem cells (DPSCs)^[4].
EGF Protein (Human) (10 ng/mL, 21 days) induces a clear increase in abundance and size of calcium deposit, as well as in the mineralization levels evaluated by Alizarin red S (ARS) (HY-120601) (1686.31 μg/mL)^[4].
EGF Protein (Human) significantly enhances tyrosine phosphorylation, increases activity of alkaline phosphatase and enhances formation of mineralization nodules in human mesenchymal stem cells (hMSC)^[5].
EGF Protein (Human) (10 ng/μL, 21 days) promotes the Sox10-mediated astrocyte fate switch to oligodendrocyte precursor cells (iOPCs) which are capable of further diferentiating into myelinating oligodendrocytes (OLs)^[7].

EGF Protein (Human) (10 μg/g, cream, a single dose for 7 days) reduces inflammatory infiltrate and results in wound re-epithelialization in rats with full thicknessskin wounds^[1].
EGF Protein (Human) (50 μg/g, cream, every 24 h for 7 days) significantly stimulates re-epithelialization at high levels, preferably in combination with a protease inhibitor in pigs with thickness wounds on the back^[1].
EGF Protein (Human) (30 μg/kg, s.c., daily for 3 weeks) attenuates the oesophageal damage normally caused by the sclerotherapy (surgical dilation of the oesophagus) procedure in Gottingen minipigs^[1].

Measured in a cell proliferation assay using BALB/c 3T3 cells. The ED₅₀ for this effect is <300 pg/mL.

• 
  Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.The ED₅₀ for this effect is 53.08 pg/mL, corresponding to a specific activity is 1.88×10⁷ units/mg.

Human

E. coli

Tag Free

P01133-1 (N971-R1023)

1950  [NCBI]

NSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELR

Approximately 7-10 kDa due to the glycosylation

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

Lyophilized powder

Lyophilized from a 0.2 μm filtered solution of 10 mM Phosphate buffer, pH 7.0, 200 mM NaCl or 20 mM PB, 150 mM NaCl, pH 7.4 or 20 mM Tris, 200 mM NaCl, pH 8.0 or 50 mM Tris-HCL, 200 mM NaCl, pH 8.0 or PBS, pH 7.4, 5% trehalose, 5% mannitol and 0.01% Tween80 or PBS, pH 7.4, 8% trehalose.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Wong WR, et al. Applications, and efficient large-scale production, of recombinant human epidermal growth factor. Biotechnol Genet Eng Rev. 2001;18:51-71.  [Content Brief]

  [2]. Lao G, et al. Controlled release of epidermal growth factor from hydrogels accelerates wound healing in diabetic rats. J Am Podiatr Med Assoc. 2012 Mar-Apr;102(2):89-98.  [Content Brief]

  [3]. Venturi S, et al. Iodine in evolution of salivary glands and in oral health. Nutr Health. 2009;20(2):119-34.  [Content Brief]

  [4]. Del Angel-Mosqueda C, et al. Epidermal growth factor enhances osteogenic differentiation of dental pulp stem cells in vitro. Head Face Med. 2015 Sep 3;11:29.  [Content Brief]

  [5]. Kratchmarova I, et al. Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation. Science. 2005 Jun 3;308(5727):1472-7.  [Content Brief]

  [6]. Li X, et al. Common and rare variants of EGF increase the genetic risk of Alzheimer's disease as revealed by targeted sequencing of growth factors in Han Chinese. Neurobiol Aging. 2023 Mar;123:170-181.  [Content Brief]

  [7]. Liu X, et al. EGF signaling promotes the lineage conversion of astrocytes into oligodendrocytes. Mol Med. 2022 May 4;28(1):50.  [Content Brief]