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.