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EGF Protein, Canine, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 8.3 kDa and the accession number is Q9BEA0.
Pack Size | Price | Availability | Quantity |
---|---|---|---|
100 μg | $256 | 7-10 days | |
1 mg | $1,400 | 7-10 days |
Biological Activity | Measured in a cell proliferation assay using Balb 3T3 mouse embryonic fibroblasts. The EC50 for this effect is typically 0.5-3 ng/ml. |
Description | EGF Protein, Canine, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 8.3 kDa and the accession number is Q9BEA0. |
Species | Canine |
Expression System | E. coli |
Tag | N-His |
Accession Number | Q9BEA0 |
Synonyms | epidermal growth factor |
Construction | A DNA sequence encoding the mature form of canine EGF (Q9BEA0) (Asn 973-Arg 1024) was fused with a polyhistidine tag at the N-terminus. Predicted N terminal: Met |
Protein Purity | > 98 % as determined by SDS-PAGE |
Molecular Weight | 8.3 kDa (predicted); 12 kDa (reducing conditions) |
Endotoxin | Please contact us for more information. |
Formulation | Lyophilized from a solution filtered through a 0.22 μm filter, containing PBS, pH 7.5. Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization. |
Reconstitution | A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information. |
Stability & Storage | It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping | In general, Lyophilized powders are shipping with blue ice. |
Research Background | EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. EGF contains 9 EGF-like domains and 9 LDL-receptor class B repeats. Human EGF is a 6045-Da protein with 53 amino acid residues and three intramolecular disulfide bonds. As a low-molecular-weight polypeptide, EGF was first purified from the mouse submandibular gland, but since then it was found in many human tissues including submandibular gland, parotid gland. It can also be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is a growth factor that stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. It results in cellular proliferation, differentiation, and survival. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. EGF acts by binding with high affinity to epidermal growth factor receptor on the cell surface and stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity, in turn, initiates a signal transduction cascade that results in a variety of biochemical changes within the cell - a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR - that ultimately lead to DNA synthesis and cell proliferation. |
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