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Human EGF

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Cat-Nr.100-008
Size100 µg
Price65 €
SourceE. coli
Formulationlyophilized
Purity Confirmation> 95% by SDS-PAGE
Length [aa]54
Molecular Weight6.35 kDa
N Terminal SequenceMNSDSECPLS
Endotoxin Levels< 0.1 ng/µg of protein (<1EU/µg)
Biological ActivityThe biological activity was determined by the ability to induce EGF receptor phosphorylation in the A431 tumor cell line [Soler et al, J Chromatography B, 788, 2003] and the induction of proliferation in NHDF cells (Normal Human Dermal Fibroblasts).
Species Reactivityhuman, mouse
BufferPBS
ReconstitutionWe recommend a quick spin followed by reconstitution in water to a concentration of 0.1-1.0 mg/ml.
Stability and StorageThe lyophilized protein is stable for a few weeks at room temperature, but best stored at -20°C. Reconstituted EGF should be stored in working aliquots at -20°C.
SynonymsEpidermal growth factor; EGF; URG; HOMG4; Urogastrone
DescriptionEpidermal growth factor (EGF) is the founding member of the EGF family that also includes TGFα, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin-binding EGF-like growth factor (HBEGF), epigen, and the neuregulins (NRG) 1 through 6. Members of the EGF family share a structural motif, the EGF-like domain, which is characterized by three intra-molecular disulfide bonds that are formed by six similarly spaced conserved cysteine residues. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. The 1207 amino acid (aa) human EGF precursor contains nine EGF domains and nine LDLR class B repeats. The mature protein consists of 53 aa and is generated by proteolytic excision of the EGF domain proximal to the transmembrane region. Mature human EGF shares 70% aa sequence identity with mature mouse and rat EGF. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2. Biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture.
Protein SequenceMNSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELR
Uniprot IDP01133
Protein RefSeqNP_001954.2
mRNA RefSeqNM_1963.4

Figures

Figure 1.
SDS-PAGE analysis of recombinant human EGF. Sample was loaded in 18% SDS-polyacrylamide gel under reducing conditions and stained with Silver stain.
Figure 2.
EGF-induced phosphorylation of EGFR in the A431 tumor cell line (L. Ferrer Soler et al., J Chromatogr B Analyt Technol Biomed Life Sci. 2003 May 5;788(1):113-23.).
Figure 3.
EGF-induced proliferation of NHDF cells (Normal Human Dermal Fibroblast cells).

Reference

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