Epidermal growth factor (EGF), a founding member of the EGF-family of proteins is a 6 kilodalton protein belonging to the EGF-protein family. EGF binds to the epidermal growth factor receptor (EGFR) and stimulates cell growth and differentiation . In humans, this protein is made of 53 amino acid residues and its tertiary structure is held together by 3 intramolecular disulfide bonds. Researchers first identified EGF in human urine and mice submaxillary glands as a secreted protein. Since then, EGF has been found in tears, saliva, milk, plasma, and tissues, including the parotid gland and submandibular gland-urogastrone or its trade name Heberprot-P.
Heberprot-P equals EGF, an important and necessary protein for wound healing processes. From the beginning of your own life, it has been part of you. As a growth factor, EGF is essential in many phases of the wound healing process. Wound strength and optimal scar quality requires a balanced amount of EGF. If too little EGF is present there could be complications in wound healing; too much EGF may also lead to uncontrolled cell formation.
EGF is a peptide of 53 amino acids that binds to the epidermal growth factor receptor (EGFR) and stimulates cell growth and differentiation. It was originally identified as specific mitogen for mouse submandibular gland epithelial cells (1). EGF is synthesized as a monomeric protein, which is then processed by enzymatic cleavage to generate the active EGF dimer. It is secreted in various forms, including big, middle, and small forms.
Fas ligand or FasL (CD178 or CD95L) is a homotrimeric human type II transmembrane protein. The Fas ligand gene (FASLG) on chromosome 1q24.3 encodes the Fas ligand protein. Cytotoxic T lymphocytes express FasL on their surfaces that belong to the TNF family of proteins. By binding to its receptors, FasL induces apoptosis in cells. A matrix metalloproteinase MMP-7 cleaves membrane-bound FasL and generates a soluble FasL. FasL interacts with its receptors and plays a crucial role in immune system regulation and cancer progression.
Fas ligand (FasL) is a tumor necrosis factor family member that induces apoptosis in cells expressing its receptor, Fas. The interaction of FasL with Fas regulates immune system development, maintenance and progression. Furthermore, it plays a crucial role in anti-tumor immunity and cancer progression. The matrix metalloproteinase MMP-7 generates soluble FasL which mediates the induction of cell death by activating a distinct set of downstream signaling events. This antibody detects an epitope located near the cell surface.
Fas ligand (CD178 or CD95L) is a monomeric type II transmembrane human protein that belongs to the TNF family of proteins. Fas ligand is expressed on the surfaces of activated cytotoxic T lymphocytes that belong to the immune system. Binding through their receptors causes programmed cell death or apoptosis in cells. Soluble FasL exists in biological fluids such as serum and may induce apoptosis via the soluble FasR protein.Fas ligand (FasL) is a protein that helps to regulate the apoptosis, or programed cell death, of cells. This can be useful in preventing tumor growth: by causing the death of cells that have become cancerous.
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