EGF Protein, Human

EGF proteins act as potent stimulators of growth in a variety of epidermal and epithelial tissues in both in vivo and in vitro settings, while promoting the proliferation of specific fibroblasts in cell culture. This multifaceted protein also acts as a magnesium stimulating hormone, driving magnesium reabsorption in the renal distal tubule through engagement of EGFR and activation of the magnesium channel TRPM6. EGF Protein, Human is the recombinant human-derived EGF protein, expressed by E. coli , with tag free.

EGF Protein emerges as a potent stimulator of the growth of diverse epidermal and epithelial tissues in both in vivo and in vitro environments, along with fostering the proliferation of specific fibroblasts in cell culture. This multifaceted protein also acts as a magnesiotropic hormone, driving magnesium reabsorption in the renal distal convoluted tubule through the engagement of EGFR and activation of the magnesium channel TRPM6. Notably, EGF Protein possesses the capability to induce neurite outgrowth in motoneurons of the pond snail Lymnaea stagnalis in vitro. Its molecular interactions include binding to EGFR, thereby promoting EGFR dimerization, and interacting with RHBDF2, suggesting involvement in diverse cellular processes. Furthermore, EGF Protein engages with RHBDF1, potentially influencing the retention of EGF in the endoplasmic reticulum and regulating its degradation through endoplasmic reticulum-associated degradation (ERAD).

EGF Protein, Human (0-500 ng/mL, 72 h) promotes the proliferation of NIH 3T3 cells^[3].

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]

Full Length of EGF

NSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELR

Approximately 5-11 kDa, based on SDS-PAGE under reducing conditions.

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.
2.Lyophilized from a 0.22 μm filtered solution of 10 mM PB, 200 mM NaCl, pH 7.0.
3.Lyophilized from a 0.22 μm filtered solution of 50 mM Tris-HCl, 200 mM NaCl, pH 8.0.
4.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 5% trehalose, 5% mannitol, 0.01% Tween 80.
5.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
6.Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 200 mM NaCl, pH 8.0.
Please refer to the lot-specific COA for specific buffer information.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<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 from date of receipt. 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]. Pouranvari S, et al., Cloning, Expression, and Cost Effective Purification of Authentic Human Epidermal Growth Factor With High Activity. Iran Red Crescent Med J. 2016 Mar 20;18(3):e24966.  [Content Brief]