Anti-EGFR Antibody, neutralizing, clone LA1

Descrição detalhada : Reacts with external domain of EGF receptor on all human cells. Competes with EGF and TGF-alpha for binding on human cells., Epidermal growth factor receptor (UniProt: P00533; also known as EC:2.7.10.1, Proto-oncogene c-ErbB-1, Receptor tyrosine-protein kinase erbB-1) is encoded by the EGFR (also known as ERBB, ERBB1, HER1) gene (Gene ID: 1956) in human. EGFR is a single-pass type I membrane glycoprotein that is ubiquitously expressed. It is synthesized with a signal peptide (1-24), which is subsequently cleaved off to produce the mature form that contains an extracellular domain (aa 25-645), a transmembrane domain (aa 646-668), and a long cytoplasmic domain (669-1210). It possesses receptor tyrosine kinase activity and upon binding of ligands activates several signaling cascades. Ligand binding is known to trigger receptor homo- and/or heterodimerization, which stimulates its intrinsic intracellular protein-tyrosine kinase activity. As a result, autophosphorylation of tyrosine residues in the C-terminal domain of EGFR occurs, which results in activation of several downstream signaling cascades, including the Ras-RAF-MEK-ERK, PI3 kinase-Akt, PLCgamma-PKC, and STAT. EGFR phosphorylation at serine 695 is reported to be only partial and occurs only if threonine 693 is phosphorylated. EGFR also undergoes mono and polyubiquitination upon EGF stimulation. However, this ubiquitination does not affect tyrosine kinase activity of the receptor or its signaling capacity. EGFR is commonly overexpressed and is mutated in many human malignancies and is often associated with aggressive phenotypes.
Sinónimos : Anti-ERBB; Anti-ERBB1; Anti-ERRP; Anti-HER1; Anti-NISBD2; Anti-PIG61; Anti-mENA
Armazenamento : -20°C
Embalagem : 1X1EA