Epidermal Growth Factor, human (hEGF) 11376454001

Recombinant Epidermal Growth Factor, human (hEGF), is produced in E. coli and purified by standard chromatographic techniques. It is a 100µg white lyophilizate, filtered through 0.2µm pore size membrane, recombinant from E. coli.
Epidermal growth factor (EGF) is a small mitogenic polypeptide which is present in many mammalian species and is distributed throughout a wide number of tissues and body fluids EGF is produced in the tubular cells of the submaxillary gland of the mouse, in the acinar cells of the human submaxillary gland, and in the human duodenal glands.
Human EGF is identical to -urogastrone, a polypeptide which was recognized and isolated on the basis of its ability to inhibit gastric acid secretion. 37 amino acids of the 53 amino acids comprising the longer urogastrone (human EGF) and mouse EGF are common to both peptides (70% homology) and the three disulfide bonds are formed in the same relative positions. The biological activity of human EGF is similar to that of mouse EGF. The cellular receptor for EGF is the best understood growth factor receptor. The oncogene v-erbB codes for a product homologous to a portion of the EGF receptor in which the EGF-binding domain has been deleted. Evidence exists suggesting that this truncation of the EGF receptor may lead to constitutive activation without requirement for ligand binding.
EGF stimulates the proliferation and differentiation of awide variety of cells of ectodermal and mesodermal origin (e.g., fibroblasts, glial cells, keratinocytes, epithelial cells, endothelial cells, chondrocytes). EGF is a constituent of many serum-free media formulations for a variety of cells.
Specificity
Species Specificity: Human EGF is effective on human and mouse cells.
Specific activity: <0.5 ng/ml, at least the same specific activity (EC50) compared to the indicated standard is guaranteed.
Epidermal growth factor (EGF) stimulates the proliferation and differentiation of a wide variety of cells of ectodermal and mesodermal origin, and is a constituent of many serum-free media formulations. It has been used in the cell differentiation assay.
Sequence
The primary structure of recombinant, human EGF (one polypeptide chain, 54 amino acids) is identical to that of human, natural EGF (β-urogastrone) (53 amino acids), however, recombinant EGF has an additional methionine at the amino-terminus.
Chain Length 54 AA
Unit Definition
Unit Conversion: 1 BM unit = 3.25 NBSB units (natural IL-2)1 BM unit = 3.25 NBSB units (natural IL-2)
Unit Definition: EC50 defintion: The concentration of hEGF that is required to support half-maximal stimulation of cell proliferation (MTT cleavage) with MK cells.
Physical form
White lyophilizate, filtered through 0.2 μm pore size membrane
Preparation Note
Working concentration: 0.5 to 20 ng/ml
Human EGF exerts its biological activity in the concentration range of 0.5 to 20 ng/ml. Recommended concentration for serum-free cell culture is 1 to 10 ng/ml
Working solution: In sterile water (final concentration: 500 µg/ml), further dilution with medium or PBS (phosphate buffered saline) containing 1 mg/ml BSA (bovine serum albumin), or 1 to 10% serum.
Storage conditions (working solution): -15 to -25 °C
It is recommended to store the reconstituted solution in aliquots at -15 to -25 °C.
Note: Avoid repeated freezing and thawing.
For life science research only. Not for use in diagnostic procedures.

Quality Level	100
biological source	human
recombinant	expressed in E. coli
assay	>95% (HPLC)
form	lyophilized
potency	<0.5 ng/mL EC50
mol wt	6200 Da
packaging	pkg of 100 µg
Торговая марка	Roche
storage condition	avoid repeated freeze/thaw cycles
color	white
UniProt accession no.	Q6QBS2,
shipped in	dry ice
storage temp.	20°C
Gene Information	human ... EGF(1950)

RIDADR	NONH for all modes of transport
WGK Germany	WGK 1
Flash Point F	does not flash
Flash Point C	does not flash