Recombinant Human Epidermal Growth Factor
(rHuEGF)
Catalog Number: C22-105-04
Source: Escherichia coli.
Molecular Weight: Approximately 6.2k Da, a single non-glycosylated polypeptide chain containing 53 amino acids.
Quantity: 100μg/500μg/1000μg
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 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 0.2μm filtered concentrated solution in PBS, pH 7.4.
Endotoxin: Less than 1EU/μg 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 Shanghai Corning Bio-Tech for research, laboratory or further
evaluation purposes. NOT FOR HUMAN USE.
Human Epidermal Growth Factor
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. 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 EGFCatalog Number: C22-105-04
Source: Escherichia coli.
Molecular Weight: Approximately 6.2k Da, a single non-glycosylated polypeptide chain containing 53 amino acids.
Quantity: 100μg/500μg/1000μg
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 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 0.2μm filtered concentrated solution in PBS, pH 7.4.
Endotoxin: Less than 1EU/μg 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 Shanghai Corning Bio-Tech for research, laboratory or further
evaluation purposes. NOT FOR HUMAN USE.
Human Epidermal Growth Factor
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. 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.
receptor and was reported to be biologically active.