Reactivity | RtSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | 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 10-60 pg/mL. |
Source | E. coli-derived rat EGF protein Asn974-Arg1026, with an N-terminal Met |
Accession # | |
N-terminal Sequence | Met |
Protein/Peptide Type | Recombinant Proteins |
Gene | Egf |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 6.3 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile 10 mM Acetic Acid. |
Epidermal growth factor (EGF) is a small, potent growth factor capable of inducing cell proliferation, differentiation, and survival. EGF is the founding member of the EGF family that also includes TGF-alpha, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin‑binding EGF‑like growth factor (HB‑EGF), epigen, and the neuregulins (NRG)-1 through -6 (1). Members of The EGF family are characterized by a shared structural motif, the EGF‑like domain, which contains three intramolecular disulfide bonds that are formed by six similarly spaced, conserved cysteine residues (2). These disulfide bonds are essential for proper protein conformation and receptor binding. 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 full length EGF protein is 1207 amino acids (aa) (EGF precursor) containing nine EGF domains and nine LDLR class B repeats. However, the mature protein is much smaller, only 53 aa, and is generated by proteolytic cleavage of the EGF domain proximal to the transmembrane region (3). EGF is well conserved across mammals with mature human EGF 70% identical to mature mouse and rat EGF. Physiologically, EGF is found in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid (4). EGF is a high affinity ligand of the EGF receptor (ErbB). Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members (5). EGF binding induces dimerization of the EGF receptor resulting in activation of the protein tyrosine kinase signaling pathway. These receptors undergo a complex pattern of ligand-induced homo- or hetero-dimerization 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.
Using EGF Protein from Novus Biologicals EGF (epidermal growth factor) stimulates differentiation, proliferation and cell growth by binding to its receptor, EGFR. EGF was first discovered in the mouse submandibular gland in 1986 by Stanley Cohen of Vanderbilt University, leading to a Nobel P... Read full blog post. |
Myosin is More than Just a Heavy Lifter Myosin is a well-known, hexameric molecular motor that is a key cytoskeletal component. It consists of a pair of myosin heavy chain subunits (MHC), a pair of essential myosin light chain subunits (MLC), and a pair of regulatory light chain subunits (R... Read full blog post. |
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