Recombinant Human Epidermal Growth Factor (rHuEGF)
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.
Product Specifications
Source
Escherichia coli.
Field of Research
Stem Cell & Developmental Biology
Endotoxin
Less than 1EU/mg of rHuEGF as determined by LAL method.
Purity
>98% by SDS-PAGE and HPLC analyses.
Bioactivity
Form
Lyophilized from a 0.2mm filtered concentrated solution in PBS, pH 7.4.
Molecular Weight
6222 Da, a single non-glycosylated polypeptide chain containing 53 amino acids.
Storage Conditions
Notes
For research use only.
Applications Notes
Preservative
Lyophilized from a 0.2mm filtered concentrated solution in PBS, pH 7.4.
AA Sequence
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR
Available Sizes
Frequently Asked Questions
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