Recombinant Human Epidermal Growth Factor (rHuEGF)

Catalogue Numbers: PR1019-100, PR1019-500, PR1019-1000

Sizes: 100µg, 500µg, 1.0mg (contact us for the 1.0mg option)

Source: Escherichia coli

Molecular Weight: 6222 Da, a single non-glycosylated polypeptide chain containing 53 amino acids.

Purity: >98% by SDS-PAGE and HPLC analyses.

Biological Activity: Fully biologically active when compared to standard. The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is less than 0.1 ng/ml. , corresponding to a specific activity of > 1.0x 107 units/mg.

Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation: Lyophilized from a 0.2mm filtered concentrated solution in PBS, pH 7.4.

AA Sequence: NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR

Endotoxin: Less than 1EU/mg of rHuEGF 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.

Storage: This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.

Usage: This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE. Made in China

Description: 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.