11376454001
Roche
Epidermal Growth Factor, human (hEGF)
recombinant (E. coli)
Synonym(s):
EGF, human
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About This Item
UNSPSC Code:
12352207
Recommended Products
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
manufacturer/tradename
Roche
storage condition
avoid repeated freeze/thaw cycles
technique(s)
cell culture | mammalian: suitable
color
white
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... EGF(1950)
General description
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.[1][2]
Human EGF is identical to β-urogastrone, a polypeptide which was recognized and isolated on the basis of its ability to inhibit gastric acid secretion.[1][2][3] 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.[4] 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.[5]
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).[1][2][5] EGF is a constituent of many serum-free media formulations for a variety of cells.
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.[1][2]
Human EGF is identical to β-urogastrone, a polypeptide which was recognized and isolated on the basis of its ability to inhibit gastric acid secretion.[1][2][3] 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.[4] 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.[5]
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).[1][2][5] 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.
Specific activity: <0.5 ng/ml, at least the same specific activity (EC50) compared to the indicated standard is guaranteed.
Application
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.[6]
Sequence
Chain Length 54 AA
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.
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.
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.
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.
Other Notes
For life science research only. Not for use in diagnostic procedures.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
does not flash
flash_point_c
does not flash
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Epidermal growth factor.
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Isolation and structure of urogastrone and its relationship to epidermal growth factor.
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The effects were examined of biosynthetic human epidermal growth factor (Bh-EGF) produced from cloned E. coli on DNA synthesis and all divisions of 13 different kinds of primary and established cell lines. Primary cultures of mammary epithelia, hepatocytes and stomach
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