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Cat. #:GMP-105-04
Recombinant Human Epidermal Growth Factor GMP
rHuEGF GMP
Technical Parameters
SynonymsUrogastrone
Species
AccessionP01133
GeneID1950
Source Escherichia coli.
Molecular Weight Approximately 6.2 kDa, a single non-glycosylated polypeptide chain containing 53 amino acids.
Quantity 5µg/100µg/1mg
AA Sequence NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR
Purity > 98 % by SDS-PAGE and HPLC analyses.
Biological Activity Fully biologically active when compared to standard. 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 > 1.0 × 107 IU/mg.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.
Endotoxin Less than 0.01 EU/μg of rHuEGF GMP as determined by LAL method.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Usage This GMP product can be for research use or further manufacturing use.
Quality statement The manufacture and testing of this product is in compliance with ICH Q7a guidelines.
Reference1. Chevalier RL, Goyal S, Thornhill BA. 1999. J Urol, 162: 1532-6.
2. Gehm BD, McAndrews JM, Jordan VC, et al. 2000. Mol Cell Endocrinol, 159: 53-62.
3. Yang H, Sun X, Wang Z, et al. 2003. J Membr Biol, 194: 47-58.
4. Cohen S. 2008. J Biol Chem, 283: 33793-7.
BackgroundEpidermal Growth Factor (EGF) was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. Human EGF was isolated from urine based on its inhibitory effect on gastric secretion and named urogastrone, accordingly. EGF is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit (defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds) in their extracellular domain. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature human EGF shares 70 % a.a. sequence identity with mature mouse and rat EGF.