DESCRIPTION
Source E. coliderived
Asn974Arg1026,
with an Nterminal
Met
Accession # P07522
Nterminal
Sequence
Analysis
Met
Predicted Molecular
Mass
6.3 kDa
SPECIFICATIONS
Activity Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. Rubin, J.S. et al. （1991） Proc. Natl. Acad. Sci. USA
88:415.
The ED50 for this effect is typically 1060
pg/mL.
Endotoxin Level <1.0 EU per 1 μg of the protein by the LAL method.
Purity >97%, by SDSPAGE
under reducing conditions and visualized by silver stain.
Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein. See Certificate of Analysis for details.
PREPARATION AND STORAGE
Reconstitution Reconstitute at 100 μg/mL in sterile 10 mM Acetic Acid containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediay at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freezethaw
cycles.
l 12 months from date of receipt, 20
to 70
°C as supplied.
l 1 month, 2 to 8 °C under sterile conditions after reconstitution.
l 3 months, 20
to 70
°C under sterile conditions after reconstitution.
BACKGROUND
Epidermal growth factor （EGF） is the founding member of the EGF family that also includes TGFα,
amphiregulin （AR）, betacellulin （BTC）, epiregulin （EPR）, heparinbinding
EGFlike
growth factor（HBEGF）,
epigen, and the neuregulins （NRG）1
through 6
（1）. Members of the EGF family share a structural motif, the EGFlike
domain, which is characterized by three intramolecular disulfide bonds that are formed by six similarly spaced conserved cysteine residues （2）. 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 （1）. The 1133 amino acid （aa） rat 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 （3）. Mature rat EGF shares
70% and 77% aa sequence identity with mature human and mouse EGF, respectively. EGF is present in various body fluids, including blood, milk, urine, saliva,
seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid （4）. Four ErbB （HER） family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and
ErbB4, mediate responses to EGF family members （5）. These receptors undergo a complex pattern of ligand induced homoor
heterodimerization
to transduce EGF
family signals （6, 7）. EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2. Dimerization results in
autophosphorylation of the receptor at specific tyrosine residues to create docking sites for a variety of signaling molecules （5, 8）. Biological activities ascribed to
EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture.
References:
1. Harris, R.C. et al. （2003） Exp. Cell Res. 284:2.
2. Carpenter, G. and Cohen, S. （1990） J. Biol. Chem. 265:7709.
3. Saggi, S.J. et al. （1992） DNA Cell Biol. 11:481.
4. Carpenter, G. and Zendegui, J.G. （1986） Exp. Cell Res. 164:1.
5. Jorissen, R.N. et al. （2003） Exp. Cell Res. 284:31.
6. Gamett, D.C. et al. （1997） J. Biol. Chem. 272:12052.
7. Qian, X. et al. （1994） Proc. Natl. Acad. Sci. 91:1500.
8. Qian, X. et al. （1999） J. Biol. Chem. 274:574.
Recombinant Rat EGF
Catalog Number: 3214-EG
www.
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