详细说明
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
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 ED 50 for this effect is 1-5 ng/mL.
Source
Mouse myeloma cell line, NS0-derived Trp29-Arg1029, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
AnalysisTrp29
Predicted Molecular Mass
110 kDa
SDS-PAGE
160 kDa, reducing conditions
Carrier Free
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
What formulation is right for me?
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
4095-EG |
| 4095-EG/CF |
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. | Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | |
Reconstitution Reconstitute at 50 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. | Reconstitution Reconstitute at 100 μg/mL in sterile PBS. | |
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | |
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
| Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: EGF
EGF is the prototypic member of a family of growth factors that also includes amphiregulin, betacellulin, epigen, epiregulin, HB-EGF, neuregulins-1 through -6, and TGF-alpha (1). These proteins contain EGF-like domains with three intramolecular disulfide bonds between conserved cysteines (2). EGF family members are synthesized as transmembrane preproproteins with varying numbers of EGF-like domains (3). The extracellular region of mouse pro-EGF contains eight LDL R class B repeats and nine EGF-like domains (4). Mature EGF is derived from the juxtamembrane EGF-like domain. EGF binds ErbB1 and induces the formation of homodimers or heterodimers containing ErbB2 (5). Pro-EGF is most highly expressed in the submaxillary gland and kidney (6). In the kidney, the 190 kDa preproprotein is cleaved by membrane-associated serine proteases, liberating the extracellular region which is subsequently processed into smaller fragments including the 6 kDa mature EGF (7 - 10). The various cleavage products produced in the kidney also are present in urine (9 - 11). In the submaxillary gland, however, nearly all EGF is processed intracellularly and stored in secretory vesicles (6, 12). The soluble precursor binds ErbB1 and induces cellular proliferation, although it is significantly less potent than mature EGF (8, 9). In human thyroid carcinoma cells, a splice variant of pro-EGF with a deletion in the cytoplasmic domain induces increased proliferative activity relative to wild-type pro-EGF (13). Within the extracellular region, mouse pro-EGF shares 79% amino acid sequence identity with rat pro-EGF and 67% - 69% with human, canine, feline, and porcine pro-EGF.
References:
Singh, A.B. and R.C. Harris (2005) Cell. Signal. 17:1183.
Wouters, M.A. et al. (2005) Prot. Sci. 14:1091.
Sanderson, M.P. et al. (2006) Growth Factors 24:121.
Gray, A. et al. (1983) Nature 303:722.
Jorissen, R.N. et al. (2003) Exp. Cell Res. 284:31.
Rall, L.B. et al. (1985) Nature 313:228.
Le Gall, S.M. et al. (2004) Regul. Pept. 122:119.
Breyer, J.A. and S. Cohen (1990) J. Biol. Chem. 265:16564.
Parries, G. et al. (1995) J. Biol. Chem. 270:27954.
Le Gall, S.M. et al. (2003) J. Biol. Chem. 278:45255.
Lakshmanan, J. et al. (1990) Biochem. Biophys. Res. Commun. 173:902.
Pasquini, F. et al. (1974) Exp. Cell Res. 86:233.
Pyka, J. et al. (2005) Cancer Res. 65:1343.
Long Name:
Epidermal Growth Factor
Entrez Gene IDs:
1950 (Human); 13645 (Mouse); 25313 (Rat)
Alternate Names:
beta-urogastrone; EGF; epidermal growth factor (beta-urogastrone); epidermal growth factor; HOMG4; pro-epidermal growth factor; URG; Urogastrone