Human Pro-EGF Antibody Summary
Ser21-Arg1023
Accession # CAA28240
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of Pro-EGF by Western Blot XSMOC-1 does not potentiate MAPK signaling by pro-EGF, but can bind to pro-EGF when bound to heparin sepharose.(A) Immunoblot of 32D/EGFR cell lysates showing Erk phosphorylation (dpErk) following a six minute exposure to a dilution series (0–500ng/ml) of pro-EGF. Total Erk is shown as loading control. (B) Graph showing relative dpErk fluorescence obtained on immunoblots from triplicate experiments of 32D/EGFR cells following a six minute exposure to submaximal concentrations of pro-EGF (2ng or 5ng/ml) in the presence or absence of XSMOC-1 (100μg/ml).The level of dpErk by pro-EGF was not significantly affected by XSMOC-1. (C) Coomassie-stained SDS-PAGE showing the heparin sepharose (HS) elution profile of pro-EGF in the presence of increasing concentrations of NaCl (D) Coomasie-stained SDS-PAGE showing HS elution profiles (±) following incubation of 5μg XSMOC-1 with 5μg of either pro-EGF or EGF in PBS/500mM NaCl, compared to each protein alone. A standard (std) lane is provided for pro-EGF and EGF to demonstrate their expected migration position. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/27101391), licensed under a CC0-1.0 license. Not internally tested by R&D Systems.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: EGF
Epidermal growth factor (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 share a structural motif, the EGF-like 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 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 (3). 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 (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 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.
- Harris, R.C. et al. (2003) Exp. Cell Res. 284:2.
- Carpenter, G. and Cohen, S. (1990) J. Biol. Chem. 265:7709.
- Bell, G.I. et al. (1986) Nucl. Acids Res. 14:8427.
- Carpenter, G. and Zendegui, J.G. (1986) Exp. Cell Res. 164:1.
- Jorissen, R.N. et al. (2003) Exp. Cell Res. 284:31.
- Gamett, D.C. et al. (1997) J. Biol. Chem. 272:12052.
- Qian, X. et al. (1994) Proc. Natl. Acad. Sci. 91:1500.
- Qian, X. et al. (1999) J. Biol. Chem. 274:574.
Product Datasheets
Citation for Human Pro-EGF Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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SMOC Binds to Pro-EGF, but Does Not Induce Erk Phosphorylation via the EGFR
Authors: JT Thomas, L Chhuy-Hy, KR Andrykovic, M Moos
PLoS ONE, 2016-04-21;11(4):e0154294.
Species: Human
Sample Types: Cell Lysates, Recombinant Protein
Applications: Immunodepletion, Western Blot
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