Growth Factors
Product List
MFGE8 Mouse
Milk Fat Globule-EGF Factor 8 Protein Mouse Recombinant
MFGE8 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (23-426a.a.) and having a molecular mass of 46kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
MFGE8 is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
EGF (1-51), Human
Epidermal Growth Factor (1-51 a.a.)Human Recombinant
Epidermal Growth Factor (1-51 a.a.) Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 6.0kDa. The EGF is purified by proprietary chromatographic techniques.
Saccharomyces cerevisiae
Sterile Filtered White lyophilized (freeze-dried) powder.
EGF (Leu 21) Human
Epidermal Growth Factor (Leu-21) Human Recombinant
The EGF 21-Leu is purified by proprietary chromatographic techniques.
EGF Human
Epidermal Growth Factor Human Recombinant
Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.
EGF Human, Pichia
Epidermal Growth Factor Human Recombinant, Pichia
The EGF is purified by proprietary chromatographic techniques.
EGF Long Human
Epidermal Growth Factor Long Human Recombinant
The EGF Long is purified by proprietary chromatographic techniques.
EGF Mouse
Epidermal Growth Factor Mouse
The EGF is purified by proprietary chromatographic techniques.
EGF Mouse Protein
Epidermal Growth Factor Mouse Recombinant
The EGF is purified by proprietary chromatographic techniques.
EGF Mouse, Biotin
Epidermal Growth Factor Mouse Recombinant, Biotin
EGF Mouse, His
Epidermal Growth Factor Mouse Recombinant, His Tag
EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
Epidermal Growth Factor (EGF) is a protein that stimulates cell growth, proliferation, and differentiation by binding to its receptor, EGFR (Epidermal Growth Factor Receptor). It was first discovered in the submaxillary glands of mice and later found in human urine . EGF is classified as a polypeptide growth factor and is part of a larger family of growth factors that includes Transforming Growth Factor-alpha (TGF-α) and Heparin-binding EGF-like growth factor (HB-EGF) .
Key Biological Properties: EGF is a small protein composed of 53 amino acids and has a molecular weight of approximately 6 kDa. It contains three intramolecular disulfide bonds that are crucial for its stability and function .
Expression Patterns: EGF is expressed in various tissues, including the submandibular and parotid glands, platelets, urine, saliva, milk, tears, and blood plasma . It is also found in the brain, where it plays a role in neurogenesis .
Tissue Distribution: EGF is widely distributed in the body and can be found in multiple tissues and fluids, including the gastrointestinal tract, liver, kidneys, and skin .
Primary Biological Functions: EGF primarily stimulates cell growth, proliferation, and differentiation. It plays a crucial role in wound healing by promoting the proliferation of epithelial cells . EGF also influences the development of various tissues and organs, including the lungs, kidneys, and reproductive system .
Role in Immune Responses and Pathogen Recognition: EGF has been shown to modulate immune responses by influencing the activity of various immune cells. It can enhance the proliferation and differentiation of T cells and macrophages, thereby playing a role in pathogen recognition and immune defense .
Mechanisms with Other Molecules and Cells: EGF exerts its effects by binding to the EGFR on the cell surface. This binding induces dimerization of the receptor, leading to its activation . The activated EGFR then triggers a cascade of downstream signaling pathways, including the MAPK/ERK, PI3K/Akt, and JAK/STAT pathways .
Binding Partners and Downstream Signaling Cascades: EGF interacts with various binding partners, including PLCγ (phospholipase C-γ), PLD (phospholipase D), and STAT (signal transducer and activator of transcription) proteins . These interactions lead to the activation of multiple signaling cascades that regulate cell proliferation, survival, and differentiation .
Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of EGF are tightly regulated at multiple levels. Transcriptional regulation involves various transcription factors that bind to the promoter region of the EGF gene . Post-translational modifications, such as phosphorylation and glycosylation, also play a crucial role in modulating the activity and stability of EGF .
Transcriptional Regulation and Post-Translational Modifications: EGF gene expression is regulated by several transcription factors, including Sp1 and AP-2 . Post-translational modifications, such as phosphorylation by protein kinases, can enhance or inhibit the activity of EGF .
Biomedical Research: EGF is widely used in biomedical research to study cell growth, differentiation, and signaling pathways. It is also used in tissue engineering and regenerative medicine to promote wound healing and tissue repair .
Diagnostic Tools: EGF and its receptor, EGFR, are used as biomarkers in the diagnosis and prognosis of various cancers, including lung, breast, and colorectal cancers .
Therapeutic Strategies: EGF has therapeutic applications in the treatment of chronic wounds, such as diabetic foot ulcers and pressure ulcers. It is also being explored as a potential treatment for neurodegenerative diseases and certain types of cancer .
Role Throughout the Life Cycle: EGF plays a vital role throughout the life cycle, from development to aging and disease. During embryonic development, EGF is essential for the proliferation and differentiation of various cell types . In adults, EGF continues to play a role in tissue maintenance and repair . Dysregulation of EGF signaling has been implicated in aging and the development of age-related diseases, such as cancer and neurodegenerative disorders .
