EGF, Epidermal Growth Factor, human: Human 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.
Source: Escherichia coli.
Molecular Weight: 6222 Da, a single non-glycosylated polypeptide chain containing 53 amino acids.
Quantity: 100ug/500ug/1000µg
Purity: >98% by SDS-PAGE and HPLC analyses.
Biological Activity: Fully biologically active when compared to standard. The ED50 as calculated by the dose-dependent proliferation of murine BALB/c 3T3 cells (measured by 3 Hthymidine 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 (1mg/ml) 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