Recombinant mouse EGF protein (Animal Free) is a Mouse Full Length protein, in the 977 to 1029 aa range, expressed in Escherichia coli, with >97% purity, < 0.05 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS, HPLC.
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EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 (By similarity).
Pro-epidermal growth factor, EGF, Egf
Recombinant mouse EGF protein (Animal Free) is a Mouse Full Length protein, in the 977 to 1029 aa range, expressed in Escherichia coli, with >97% purity, < 0.05 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS, HPLC.
Constituents: 0.16% Sodium phosphate
Purity is greater than 97% as determined by reducing and non-reducing SDS-PAGE and analytical HPLC.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 (By similarity).
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Epidermal Growth Factor (EGF) also known as urogastrone is a single polypeptide that facilitates cell growth proliferation and differentiation by binding to the Epidermal Growth Factor Receptor (EGFR). The EGF protein is characterized by a relatively small molecular weight of approximately 6.4 kDa. It is expressed in various tissues including the kidney submandibular glands and Brunner's glands in the mouse and other species. The presence of anti-EGF antibodies can further enhance the understanding of its mechanical actions and functions in different organisms.
The epidermal growth factor plays a pivotal role in the regulation of cell signaling. It functions outside a complex interacting mainly with EGFR located on the cell surface. Upon ligand binding EGF induces the receptor dimerization leading to autophosphorylation which activates intrinsic intracellular signaling cascades. This activation is critical for cellular responses such as DNA synthesis and the progression of the cell cycle. EGF recombinant proteins such as HEGF are utilized in laboratories to examine its biological activity meticulously.
EGF engages in key cellular pathways that mediate various essential functions. It significantly activates the MAPK and PI3K-AKT signaling pathways which govern processes such as cell division and survival. These pathways require the participation of several other proteins including Ras Raf and PDK1 which help modulate their downstream effects. The interplay of EGF with associated proteins highlights its importance in maintaining proper signaling dynamics necessary for healthy cellular function. EGF ELISA kits as well as EGF ELISAs are tools developed for robust analysis of its pathway interactions in research and clinical settings.
Altered EGF signaling is associated with increased risk of certain cancers and inflammatory diseases. Overexpression or mutations in the EGF-EGFR axis can lead to the progression of carcinomas such as those found in the lung and breast as well as disorders like psoriasis. These aberrant signaling events are often linked with other proteins such as HER2 and VEGF which can exacerbate disease severity. The study and detection of EGF products therefore offer significant insights into both the progression and potential therapeutic targeting of these conditions.
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SDS-PAGE analysis of Anti-Repulsive Guidance Molecule A antibody ab216643 (1 μg) stained with Coomassie blue:
Lane 1: Non-reduced
Lane 2: Reduced
4-20% Tris-Glycine gel
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