EGF Mouse Protein

Epidermal Growth Factor Mouse Recombinant
Cat. No.
BT3344
Source
Escherichia Coli.
Synonyms
Urogastrone, URG, EGF.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Epidermal Growth Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids including 3 intramolecular disulfide-bonds and having a molecular mass of 6 kDa.
The EGF is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Epidermal growth factor (EGF) plays a crucial role in cell differentiation, acting as a potent mitogen for various cultured cells of ectodermal and mesodermal origin. The EGF precursor, initially a membrane-bound molecule, undergoes proteolytic cleavage to produce a 53-amino acid peptide hormone that stimulates cell division. EGF promotes the growth of epidermal and epithelial tissues both in vivo and in vitro, as well as some fibroblast types in cell culture.
Description
Recombinant Mouse Epidermal Growth Factor, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 53 amino acids. It contains 3 intramolecular disulfide bonds and has a molecular weight of 6 kDa. This EGF product is purified using proprietary chromatographic techniques.
Physical Appearance
White lyophilized (freeze-dried) powder, sterile and filtered.
Formulation
The protein is lyophilized without any additives.
Solubility
To reconstitute the lyophilized Epidermal Growth Factor, it is recommended to dissolve it in sterile 18MΩ-cm H2O at a concentration of at least 100µg/ml. This solution can then be further diluted into other aqueous solutions as needed.
Stability
Lyophilized Recombinant Epidermal Growth Factor is stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated at a temperature below -18°C. Once reconstituted, EGF should be stored at 4°C for 2-7 days. For extended storage after reconstitution, store it below -18°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of this product is greater than 98.0%, as determined by: (a) RP-HPLC analysis. (b) SDS-PAGE analysis.
Biological Activity
Biological activity is assessed by the dose-dependent proliferation of mouse BALB/c 3T3 cells, typically exhibiting an activity level of less than 0.1ng/ml.
Synonyms
Urogastrone, URG, EGF.
Source
Escherichia Coli.
Amino Acid Sequence
NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR.

Product Science Overview

Structure and Production

EGF is produced by epithelial cells, fibroblasts, and many other cell types . It is initially synthesized as a large transmembrane precursor with a molecular weight of approximately 130,000 . Through proteolysis, this precursor is cleaved to generate a low molecular weight soluble form of EGF, which is biologically active .

Mechanism of Action

EGF exerts its effects by binding to the EGF receptor (EGFR), also known as HER1 or ErbB1 . This binding induces receptor dimerization, either as homodimers or heterodimers with other members of the HER/ErbB family . The activation of EGFR triggers several downstream signaling pathways, including the MAPK, PI3K/Akt, and Stat5 pathways . These pathways are involved in regulating various cellular processes such as proliferation, differentiation, and survival .

Biological Activity

Recombinant mouse EGF (mEGF) is commonly produced in Escherichia coli (E. coli) and is supplied in a lyophilized form . The bioactivity of recombinant mEGF is typically assessed using cell proliferation assays, such as those involving BALB/c 3T3 mouse embryonic fibroblast cells . The effective dose (ED50) for mEGF in these assays is usually less than or equal to 0.25 ng/mL .

Applications and Therapeutic Potential

EGF and its receptors are involved in many cancers and are targets for therapeutic intervention . The EGF family includes several other members, such as TGF-alpha, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin-binding EGF-like growth factor (HB-EGF), epigen, and the neuregulins (NRG)-1 through -6 . These growth factors share structural similarities and often have overlapping biological functions.

Recombinant mouse EGF is widely used in cell culture, differentiation studies, and functional assays . It is an essential component of many cell culture media formulations and is used to study the mechanisms of cell growth and differentiation.

Storage and Handling

Recombinant mouse EGF is typically supplied as a lyophilized powder and should be reconstituted with sterile water or PBS at a concentration of 0.1 mg/mL . For long-term storage, it is recommended to aliquot the reconstituted solution and store it at -20°C to -80°C to prevent loss of potency . Avoid multiple freeze-thaw cycles to maintain the stability and activity of the protein .

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