E5160

Epidermal Growth Factor from mouse

≥90% (SDS-PAGE), recombinant, expressed in E. coli, lyophilized powder, suitable for cell cutlure

• Synonym(s): Mouse EGF, Mouse Epidermal Growth Factor
• UNSPSC Code: 12352202
• NACRES: NA.77
• Biological source: mouse
• Recombinant: expressed in E. coli
• Assay: ≥90% (SDS-PAGE)
• Form: lyophilized powder
• Mol wt: ~6 kDa
• Impurities: ≤1 EU/μg endotoxin (Protein)

Properties

• Product Name: Epidermal Growth Factor from mouse, EGF
• biological source: mouse
• recombinant: expressed in E. coli
• assay: ≥90% (SDS-PAGE)
• form: lyophilized powder
• potency: 0.05-1 ng/mL ED₅₀/EC₅₀
• mol wt: ~6 kDa
• packaging: pkg of 100 μg
• storage condition: avoid repeated freeze/thaw cycles
• technique(s): cell culture | mammalian: suitable
• impurities: ≤1 EU/μg endotoxin (Protein)
• color: white
• solubility: water: soluble 0.10 mL, clear, colorless
• UniProt accession no.: P01132
• storage temp.: −20°C
• Quality Level: 200
• Gene Information: mouse ... Egf(13645)

Description

Application

Epidermal Growth Factor from mouse has been used as a basal (N2B27) medium supplement for culturing differentiated mouse embryonic stem (E14) cells.[1]

Biochem/physiol Actions

EGF (epidermal growth factor) is involved in cellular proliferation, differentiation, and survival.[2] Moreover, it was found to affect various biological activities like angiogenesis, inhibition of gastric acid secretion, modulation of the synthesis of a number of hormones, synthesis and turn-over of proteins of the extracellular matrix, calcium release from bone tissue (thus promoting bone resorption), chemoattraction of fibroblasts and epithelial cells, and alone or in combination with other cytokines, mediation of wound healing processes.[3][4][5][6][7][8][9] EGF is mitogenic for a large variety cell types, including fibroblasts, epithelial cells, endothelial cells, chondrocytes, and SV40-3T3 cells.[10]

General description

Epidermal Growth Factor (EGF) is a small mitogenic polypeptide (∼6kDa) present in many mammalian species and distributed throughout a wide number of tissues and body fluids.[11] Four ErbB (HER) family receptor tyrosine kinases, including EGFR/ErbB1, ErbB2, ErbB3, and ErbB4 mediate responses to EGF family members.[12] Human and mouse EGFs are very similar, but not identical in their physical and chemical properties. Of the 53 amino acid residues comprising each of the two polypeptides, 37 are common to both molecules, and three disulfide bonds are formed in the same relative positions.[10]

Physical form

The product is lyophilized from a 0.2 μm-filtered solution of phosphate buffered saline (PBS), pH 7.4.

Safety Information

• Storage Class: 11 - Combustible Solids
• wgk: WGK 1