EEA1 Monoclonal Antibody (1G11), eBioscience™, Invitrogen™

Description

• Description: The monoclonal antibody 1G11 recognizes human, mouse and rat early endosome antigen 1 (EEA1)
• EEA1 is a hydrophilic peripheral membrane protein found in the cytosol and present on early endosome membranes
• EEA1 is a dimer that is localized to early endosomes via a cysteine-rich zinc-finger-like FYVE domain
• EEA1 interacts with Rab5-GTP, syntaxin 6 and syntaxin 13 (SNARES)
• EEA1 is required for endocytic membrane docking and fusion, which allows for the recycling of receptors from the plasma membrane or their delivery to lysosomes for degradation
• In neurons, early endosomes are involved in the recycling of neurotransmitter receptors
• Autoantibodies to EEA1 have been found in patients with neurological deficits which result in enhanced excitatory synaptic transmission
• Applications Reported: This 1G11 antibody has been reported for use in western blotting, immunohistochemical staining of formalin-fixed paraffin embedded tissue sections, microscopy, ELISA, and immunocytochemistry
• Applications Tested: This 1G11 antibody has been tested by immunocytochemistry of fixed and permeabilized HeLa cells and can be used at less than or equal to 1 μg/mL
• It is recommended that the antibody be carefully titrated for optimal performance in the assay of interest
• Purity: Greater than 90%, as determined by SDS-PAGE
• Aggregation: Less than 10%, as determined by HPLC
• Filtration: 0.2 μm post-manufacturing filtered
• Early endosomal antigen 1 (EEA1) is a 162 kDa membrane bound protein component specific to the early endosome and is essential for fusion between early endocytic vesicles
• Early endosomes are cytoplasmic compartments which fuse with endocytic vesicles for redistribution of extracellular compounds to alternate destinations
• Zinc-finger-like domains, reminiscent of those found in nucleic acid binding proteins, are located in the amino and carboxyl-terminal domains of EEA1
• The carboxyl-terminal zinc-finger-like-domain is conserved in several other non-nuclear proteins, some of which are also involved in intracellular protein trafficking
• In addition, this domain is an authentic zinc-binding domain and is critical to the intracellular localization of EEA1
• Membrane association of EEA1 has been shown dependent on phosphatidyl 3-kinase activity, inhibitors of which cause EEA1 to dissociate from early endosomes.