Recombinant mouse EGF protein (Qk066)

Protein background

Epidermal growth factor (EGF), a member of the EGF family of proteins including transforming growth factor alpha (TGF-α), amphiregulin, and betacellulin, plays a significant role in regulating cellular processes such as cell growth, proliferation, differentiation, development, and tissue homeostasis [1-3].

Mouse EGF, sharing substantial homology with its human counterpart, serves as a vital tool in studying cellular mechanisms, tissue regeneration, and disease pathology due to its close resemblance to human EGF. Widely utilized in cell culture, mouse EGF stimulates cell growth and sustains viability, particularly in stem cell applications, where it maintains pluripotency and facilitates the expansion of embryonic and induced pluripotent stem cells [4]. Additionally, mouse EGF directs stem cell differentiation towards specific lineages such as neural, epithelial or mesenchymal cells, crucial for applications in regenerative medicine, disease modelling and drug discovery [5-6]. In organoid cultures, mouse EGF is a key component of organoid culture media, supporting the development and maintenance of organoid structures derived from various tissues, including intestine, liver, brain and pancreas, by regulating stem cell self-renewal and differentiation, enabling the long-term expansion and differentiation of organoid cultures [7-8].

Aberrant expression of EGF has been implicated in diseases like cancer and skin disorders, offering therapeutic targets [1]. EGF-based therapies, including recombinant EGF proteins or EGFR-targeting drugs, are being explored for their potential in treating diseases [9-10]. Mouse EGF is also employed in tissue engineering strategies aimed at generating functional tissues and organs for transplantation. By incorporating EGF into scaffolds or growth factor cocktails, researchers can promote the growth, differentiation, and maturation of stem cells into tissue-specific cell types, facilitating the development of engineered tissues for regenerative medicine applications [6,11].

Structurally, mouse EGF shares a high sequence homology with human EGF, maintaining overall structural and functional conservation, although minor differences may exist in specific amino acid residues or post-translational modifications [12]. Mouse EGF contains EGF-like domains akin to human EGF, each typically composed of 40-50 amino acids with six conserved cysteine residues forming three intramolecular disulfide bonds, crucial for domain stability [13]. The arrangement of disulfide bonds in mouse EGF is similar to human EGF, essential for maintaining tertiary structure and biological activity [14]. Additionally, some EGF-like domains in mouse EGF may feature a calcium-binding site, facilitating stability and function. Mouse EGF’s receptor-binding region interacts with the extracellular domain of the EGF receptor (EGFR), initiating signaling cascades upon ligand-receptor binding [1]. This structural flexibility enables efficient recognition and binding to EGFR, facilitating downstream signaling pathways involved in cell growth, proliferation, and differentiation [1]. Overall, understanding these structural features is fundamental for elucidating mouse EGF’s functional mechanisms in regulating various cellular processes, including development, tissue homeostasis, and disease modeling.

In summary, mouse EGF plays a crucial role in stem cell maintenance, directed differentiation, organoid culture, disease modeling, drug screening, tissue engineering, and regenerative medicine. Its versatility and importance in these applications underscore its significance as a key factor in advancing research and therapeutic interventions aimed at understanding and treating various diseases and disorders.