Epidermal growth factor (EGF) was discovered and found to promote, proliferate, and mediate survival of epithelial and mesenchymal cells through binding to its high-affinity receptor – EGF receptor. Since then, over 20 EGF-like polypeptides were found in vertebrates and several EGF-family proteins were identified. If you’re an entrepreneur, you’ll know the importance of sales. If your company doesn’t have a good conversion rate on your website or an effective marketing campaign in place, you could easily find yourself going out of business soon.
Running ads and blogs are great but they don’t always work on their own. For this reason, we’re going to talk about an awesome little thing called EGF Test. This gene encodes epidermal growth factor (EGF), 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.
Human epidermal growth factor (EGF) is a member of the EGF family and a founding member of the EGF-family of proteins. As such, it’s only natural that this protein binds to the epidermal growth factor receptor (EGFR). It may not seem like a giant leap when you think about it — after all, the extra “k” in EGF stands for krillin. This was included to differentiate between fast-acting proteins like chicken egg albumen protein, which was eventually extracted from fish ovaries.
Fas (also known as APT1L and CD178) is a transmembrane receptor that plays an important role in the regulation of cell death. Immunoreceptor tyrosine-based activation motif (ITAM) is usually present in the cytoplasmic region of the cytokine receptors and it contains ‘S/I’ motifs. These motifs serve as docking sites for protein tyrosine kinases such as Janus kinase or Fyn, which are activated by trans-plasma membrane signaling via basic leucine zipper (bZIP). Other proteins that can bind to ITAM include adapter protein with pleckstrin homology (PH domain) as well as Src homology 2 (SH2 domain). Fas is not just involved in normal cell death; it has a role in immune response too.
What is fasl? Often referred to FASL (Fas ligand) or CD95L, Fas receptor is a type of tumor necrosis factor (TNF) receptor. It has 2 extracellular domains, one short transmembrane domain, and one intracellular domain that can be divided into three regions: domain I is responsible for the death signal transduction, domain II is involved in the regulation of activation signal transduction and domain III contains several phosphorylation sites. Fas receptor belongs to a family of TNFSF 6-like receptors. Fas co-stimulatory signal pathway is vital for the activation of T cell proliferation. Activated T cells produce up to 20-30 molecules of IL2 per minute via exterior receptors and crosslinking by other activated T cells which stimulates growth factor production and replication of activated precursor B cells that have become plasma cells. FasL activates caspase 8 which in turn activates caspase 3, the ultimate executioner protease that causes apoptosis.
