NECAP2 Human

The recombinant form of NECAP2 is typically expressed in Escherichia coli and is purified to a high degree of purity, often exceeding 85% as validated by SDS-PAGE . The full-length protein consists of 263 amino acids and has a predicted molecular weight of approximately 31 kDa . The protein is tagged with a His tag at the N-terminus to facilitate purification and detection .

NECAP2 contains two characteristic WXXF motifs that are crucial for its function. These motifs mediate the binding of accessory proteins to the ear-domain of adapter protein complexes such as AP-1 and AP-2 . The selective binding to these domains is influenced by the acidic context surrounding the motif and the properties of the second residue of the motif itself .

NECAP2 is primarily localized to the cytoplasmic vesicles, particularly the clathrin-coated vesicle membrane . It colocalizes with AP-2 at the plasma membrane, where it plays a significant role in the formation and regulation of clathrin-coated vesicles . These vesicles are essential for the internalization of various molecules, including nutrients, receptors, and other macromolecules, into the cell.

The proper functioning of NECAP2 is vital for efficient endocytosis. Disruptions in its function can lead to defects in vesicle formation and trafficking, which can have downstream effects on cellular processes and signaling pathways. NECAP2 is also associated with various cellular pathways, including vesicle-mediated transport and clathrin-mediated endocytosis .

Recombinant NECAP2 is used in various research applications to study its role in endocytosis and vesicle trafficking. It is also utilized in mass spectrometry and SDS-PAGE for protein analysis . The availability of recombinant NECAP2 allows researchers to investigate its interactions with other proteins and its involvement in cellular processes.