Recombinant Mouse EGF, Animal-Free Protein
Recombinant Mouse EGF, Animal-Free Protein Summary
Animal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.
Product Specifications
Asn977-Arg1029, with an N-terminal Met
Produced using non-animal reagents in an animal-free laboratory.
Analysis
Product Datasheets
Carrier Free
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.
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.
AFL2028
| Formulation | Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. |
| Reconstitution | Reconstitute at 0.1 mg/mL in sterile PBS. |
| 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.
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Animal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.
Reconstitution Calculator
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 1217 amino acid (aa) mouse 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 mouse EGF shares 70% and 77% aa sequence identity with mature human 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.
- Gray, A. et al. (1983) Nature 303:722.
- 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.
Manufacturing Specifications
Animal-Free Manufacturing ConditionsOur dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.
Production
- All molecular biology procedures use animal-free media and dedicated labware.
- Dedicated fermentors are utilized in committed animal-free areas.
Purification
- Protein purification columns are animal-free.
- Bulk proteins are filtered using animal-free filters.
- Purified proteins are stored in animal-free containers in a dedicated cold storage room.
- Low Endotoxin Level.
- No impairment of biological activity.
- High quality product obtained under stringent conditions.
- For ex vivo research or bioproduction, additional documentation can be provided.
FAQs
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