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Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. EGF is believed to exist as a membrane bound molecule which is proteolytically cleaved to generate the 53 amino acid peptide hormone that stimulates cells to divide. EGF stimulated the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Recombinant Human EGF produced in E.coli is a single, non-glycosylated, polypeptide of 53 amino acids and a molecular weight of 6222 Dalton.
Amino acid sequence: NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR
Genaxxon’s rHuEGF is fully biologically active when compared to standards. The ED50, calculated by the dose-dependent proliferation of BALB/c 3T3 cells (measured by 3H-thymidine uptake) is 0.1ng/mL, corresponding to a specific activity of 1x10E7 units/mg.
Purity: > 98.0% (by RP-HPLC, SDS-PAGE).
First 5 amino acids: NSDSE
Sterile Filtered White lyophilized (freeze-dried) powder. The lyophilized rHuEGF is soluble in water and most aqueous buffers above the isoelectric point (pI=4.49)
Sicherheits Hinweise / Safety
Klassifizierungen / Classificationeclass-Nr: 34-16-04-90
Dokumente - Protokolle - Downloads
Here you will find information and further literature on rec. Human Epidermal Growth Factor (rHuEGF). For further documents (certificates with additional lot numbers, safety data sheets in other languages, further product information) please contact Genaxxon biosience at: firstname.lastname@example.org or phone: +49 731 3608 123.