Recombinant Rat Epidermal Growth Factor

Synonyms Urogastrone, URG

Accession P07522

GeneID 25313

Source Escherichia coli.

Molecular Weight Approximately 6.1 kDa, a single non-glycosylated polypeptide chain containing 53 amino acids, including 3 intramolecular disulfide-bonds.

Quantity 20µg/100µg/1mg

AA Sequence NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR

Purity > 97 % 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 solution in PBS, pH 7.4.

Endotoxin Less than 1 EU/μg of rRtEGF 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 material is offered by Shanghai PrimeGene Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.

SDS-PAGE

Reference 1. 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.

Background Epidermal 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. It 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 rat EGF shares 70 % a.a. sequence identity with mature human EGF.