|EEA1 in HeLa Human Cell Line. EEA1 was detected in formaldehyde fixed HeLa human cervical epithelial carcinoma cell line using Sheep Anti-Human/Mouse/Rat EEA1 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF8047) at 15 µg/mL overnight at 4 °C. Cells were stained using the NorthernLights™ 557-conjugated Streptavidin (orange; Catalog # NL999) and counterstained with DAPI (blue). Specific staining was localized to endosomes. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.|
EEA1 (Early Endosome Autoantigen 1; also known as Endosome-associated protein p162 and Zn-finger FYVE domain-containing protein 2) is a 170-180 kDa protein that serves as an identifying marker for early endosomes. It is ubiquitously expressed, and found in both the cytosol and on cellular membranes. Its activity has been described as that of a tethering factor which links endosomes to endocytic vesicles, allowing for their fusion via a SNARE complex. Normally, EEA1 exists as a homodimer in the cytoplasm and appears to make transient contacts with endosome membrane phosphatidylinositol. When endosome fusion is not required, EEA1 serves as a substrate for p97, promoting EEA1 dissociation and endosome independence. When endosome fusion is required, EEA1 interacts with NSF, resulting in its removal from a large endosome-associated complex and subsequent endosomal vesicle fusion. Human EEA1 is synthesized as a 1411 amino acid (aa) protein that contains one C2H2-type Zn finger region (aa 41-64) and one FYVE Zn finger domain (aa 1352-1410). There is one isoform variant that contains a nine aa substitution for aa 925-1411. Over aa 1249-1356, human EEA1 shares 99% aa sequence identity with mouse EEA1.
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