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E5160

Sigma-Aldrich

Epidermal Growth Factor from mouse

EGF

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NACRES:
NA.77

biological source

mouse

Quality Level

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.

storage temp.

−20°C

Gene Information

mouse ... Egf(13645)

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This Item
E1257E5036E3641
recombinant

expressed in E. coli

recombinant

-

recombinant

expressed in E. coli

recombinant

-

assay

≥90% (SDS-PAGE)

assay

≥98% (SDS-PAGE)

assay

>97% (SDS-PAGE)

assay

-

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

buffered aqueous glycerol solution

potency

0.05-1 ng/mL ED50/EC50

potency

0.02-2.0 ng/mL EC50

potency

0.08-0.8 ng/mL EC50

potency

5000.00-30000.00 units/mg

mol wt

~6 kDa

mol wt

-

mol wt

~6 kDa

mol wt

~170 kDa

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. Four ErbB (HER) family receptor tyrosine kinases, including EGFR/ErbB1, ErbB2, ErbB3, and ErbB4 mediate responses to EGF family members. 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.

Application

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

Biochem/physiol Actions

EGF (epidermal growth factor) is involved in cellular proliferation, differentiation, and survival. 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. EGF is mitogenic for a large variety cell types, including fibroblasts, epithelial cells, endothelial cells, chondrocytes, and SV40-3T3 cells.

Physical form

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

Citation

1. Carpenter, G., and Cohen, S., Epidermal growth factor. Annu. Rev. Biochem., 48, 193-216 (1979).
2. Jorissen, R.N., et al., Epidermal growth factor: mechanisms of activation and signaling. Exp. Cell Res., 284, 31-53 (2003).
3. Herbst, R.S., Review of epidermal growth factor receptor biology. Int.J. Radiat. Oncol. Biol., Phys., 59, S21-S26 (2004).
4. Mehta, V.B., and Besner, G.E., HB-EGF promotes angiogenesis in endothelial cells via PI3-kinase and MAPK signaling pathways. Growth Factors, 25, 253-263 (2007).
5. Bower, J.M., et al., The inhibition of gastric acid secretion by epidermal growth factor. Experientia, 31, 825-826 (1975).
6. Schonbrunn, A., et.al., Epidermal growth factor and thyrotropin-releasing hormone act similarly on a clonal pituitary cell strain. Modulation of hormone production and inhibition of cell proliferation. J. Cell Biol., 85, 786-797 (1980).
7. Mimura, Y., et al., Epidermal growth factor induces fibronectin expression in human dermal fibroblasts via protein kinase C delta signaling pathway. J. Invest. Dermatol., 122, 1390-1398 (2004).
8. Warner, M.R. et al., Ametantrone inhibits prostaglandin-mediated resorption in bone organ culture. Prostaglandins, 28, 469-476 (1984).
9. Grotendorst, G.R., et al., EGF and TGF-alpha are potent chemoattractants for endothelial cells and EGF-like peptides are present at sites of tissue regeneration. J. Cell. Physiol., 139, 617623 (1989).
10. Schultz, G., et al., EGF and TGF-alpha in wound healing and repair. J. Cell. Biochem., 45, 346-352 (1991).
11. George-Nascimento, C., et al., Characterization of recombinant human epidermal growth factor produced in yeast. Biochemistry, 27, 797-802 (1988).

Storage Class Code

11 - Combustible Solids

WGK

WGK 1


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Customers Also Viewed

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Characterization of recombinant human epidermal growth factor produced in yeast.
George-Nascimento C et al.
Biochemistry, 27, 797-797 (1988)
EGF and TGF-alpha are potent chemoattractants for endothelial cells and EGF-like peptides are present at sites of tissue regeneration.
Grotendorst GR et al.
Journal of Cellular Physiology, 139, 617623 -617623 (1989)
Dynamics of lineage commitment revealed by single-cell transcriptomics of differentiating embryonic stem cells
Semrau S, et al.
Nature Communications, 8(1), 1096-1096 (2017)
EGF and TGF-alpha in wound healing and repair.
Schultz G et al.
Journal of Cellular Biochemistry, 45, 346-346 (1991)
Epidermal growth factor induces fibronectin expression in human dermal fibroblasts via protein kinase C delta signaling pathway.
Mimura Y et al.
The Journal of Investigative Dermatology, 122, 1390-1390 (2004)

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