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Key Documents

Safety Information

SRP3027

Sigma-Aldrich

EGF human

Animal-component free, recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture

Synonym(s):

Epidermal Growth Factor, URG, Urogastrone

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CN¥1,140.29

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1 KIT
CN¥1,140.29

About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

CN¥1,140.29


Available to ship onApril 17, 2025Details


Request a Bulk Order

biological source

human

recombinant

expressed in E. coli

Assay

≥98% (HPLC)
≥98% (SDS-PAGE)

form

lyophilized

potency

≤0.2 ng/mL

mol wt

6.2 kDa

packaging

pkg of 500 μg

technique(s)

cell culture | mammalian: suitable

impurities

<0.1 EU/μg endotoxin, tested

color

white to off-white

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This Item
E9644SRP3182SRP6166
hEGF EGF, recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture

E9644

hEGF

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in HEK 293 cells

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

assay

≥98% (HPLC), ≥98% (SDS-PAGE)

assay

≥97% (SDS-PAGE)

assay

≥98% (HPLC), ≥98% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

form

lyophilized

form

lyophilized powder

form

lyophilized

form

lyophilized

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−70°C

General description

The gene EGF (epidermal growth factor) is mapped to human chromosome 4q25-27.[1] The EGF gene encodes for a large type I membrane–anchored precursor protein which is cleaved into pro-EGF for generation of peptide hormone EGF. The mRNA is expressed in kidney, salivary gland, cerebrum and prostate.[2] Recombinant human EGF is a 6.2kDa globular protein containing 53 amino acid residues including 3 intramolecular disulfide-bonds.

Application

EGF (epidermal growth factor) human has been used in the culture medium for the maintenance of MCF10A cells (human mammary epithelial cells).[2]

Biochem/physiol Actions

EGF (epidermal growth factor) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells.[3] Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing.[4][5] EGF signals through a receptor known as c-erbB, which is a class I tyrosine kinase receptor.[6] This receptor also binds with TGF (transforming growth factor)-α and VGF (vaccinia virus growth factor). Mutation in the EGF gene might be associated with risk of non- small cell lung adenocarcinoma.[1] It is also involved in anaplastic thyroid cancer and renal hypomagnesemia. It controls cell differentiation and neurotrophic processes.[7][8]

Sequence

NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR

Physical form

Lyophilized with no additives.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a stabilizer (example 5% Trehalose) and store in working aliquots at -20°C to -80°C.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Basal p21 controls population heterogeneity in cycling and quiescent cell cycle states.
Overton KW
Proceedings of the National Academy of Sciences of the USA, 111, E4386-E4393 (2014)
Neurotrophic actions of a novel molluscan epidermal growth factor.
Hermann PM
The Journal of Neuroscience, 20, 6355-6364 (2000)
Clinical Implication of EGF A61G Polymorphism in the Risk of Non Small Cell Lung Adenocarcinoma Patients: A Case Control Study.
Masroor M
Asian Pacific Journal of Cancer Prevention, 16, 7529-7534 (2015)
Epidermal growth factor therapy and wound healing--past, present and future perspectives.
Hardwicke J
The Surgeon : Journal of the Royal Colleges of Surgeons of Edinburgh and Ireland, 6, 172-177 (2008)
Reactive oxygen species (ROS) are essential mediators in epidermal growth factor (EGF)-stimulated corneal epithelial cell proliferation, adhesion, migration, and wound healing.
Huo Y
Experimental Eye Research, 89, 876-886 (2009)

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