EGF Mouse Protein

Epidermal Growth Factor Mouse Recombinant
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Description

Molecular Structure and Production

EGF Mouse Protein is synthesized via recombinant DNA technology in E. coli, ensuring high purity (>95%) and animal origin-free production . Key structural features include:

PropertyDetails
Molecular Weight6–6.2 kDa (53–54 amino acids)
Disulfide BondsThree intramolecular bonds (Cys6-Cys20, Cys14-Cys31, Cys33-Cys42)
Homology to Human EGF~70% sequence similarity
Bioactivity (EC50)10–263 pg/mL in cell proliferation assays

Biological Functions and Mechanisms

EGF Mouse Protein activates EGFR, a 170 kDa receptor tyrosine kinase, initiating downstream signaling cascades such as:

  • MAPK/ERK pathway: Regulates cell cycle progression and differentiation .

  • PI3K/Akt pathway: Enhances cell survival and inhibits apoptosis .

  • NF-κB pathway: Modulates inflammatory responses and tissue repair .

Key Applications in Research:

  • Stem Cell Maintenance: Sustains pluripotency in embryonic and induced pluripotent stem cells .

  • Organoid Culture: Supports intestinal, hepatic, and pancreatic organoid growth .

  • Muscle Regeneration: Restores muscle strength in Duchenne muscular dystrophy (DMD) mouse models by enhancing asymmetric stem cell division .

3.1. Muscle Regeneration in DMD

  • Study Design: Humanized EGF was expressed in dystrophin-deficient mice .

  • Results:

    • 18% increase in muscle mass.

    • 30% more muscle fibers and 32% greater strength .

    • Reduced fibrosis and sustained benefits for ≥5 months .

3.2. Tissue-Specific Hypomorphism

  • Humanized EGFR Mice: Exhibited rescued neurodegeneration but developed heart hypertrophy and bone abnormalities due to tissue-specific EGFR expression .

3.3. Cancer and Tissue Engineering

  • Tumor Microenvironment: EGF promotes chemoresistance and radiation tolerance in cancer cells .

  • Scaffold Integration: Enhances engineered tissue maturation for transplantation .

Future Directions and Challenges

  • Therapeutic Delivery: Systemic administration methods for EGF-based therapies require optimization .

  • Pathway Crosstalk: Interactions between EGFR and other signaling networks (e.g., Wnt, Notch) remain poorly understood .

  • Safety Profile: Long-term EGFR activation risks oncogenic transformation .

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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