AP2M1 polyclonal antibody

The AP-2 coat assembly protein complex is an important component of clathrin-coated pits involved in receptor-mediated endocytosis at the plasma membrane (1-3) . Each AP-2 heterotetramer is composed of α, β, μ, and σ protein subunits. The 50 kDa μ subunit (AP-2μ, AP2M1) is located at the core of the AP-2 complex and mediates interaction between the cargo protein and the clathrin-coated pit (1-4) . The carboxy-terminal AP2M1 region recognizes the tyrosine-based, endocytotic sorting motif YXXφ found in cargo proteins and helps to bring the cargo protein to the clathrin-coated pit. Non-canonical, tyrosine-based endocytotic sorting signals can also promote interaction between cargo proteins and AP2M1 (5,6) . AP2M1 plays an essential role in molecular signaling as it couples receptor-mediated endocytosis and pathways involving membrane receptors (7-9), matrix metalloproteinases (10), and ion channel proteins (11) . Phosphorylation of specific AP2M1 residues and binding of lipids to this adaptor protein can regulate AP2M1 activity (12,13) . Phosphorylation of AP2M1 at Thr156 by adaptor-associated kinase 1 (AAK1) stimulates affinity binding of AP2M1 to cargo protein signals (14) .

Adapter-related protein complex 2 mu subunit; Adaptin mu 1; Adaptin-mu2; Adaptor protein complex AP 2 subunit mu; Adaptor protein complex AP-2 subunit mu; Adaptor related protein complex 2 mu 1 subunit; AP 2 mu 2 chain; AP-2 complex subunit mu; AP-2 mu chain; AP2M 1; Ap2m1; AP2M1_HUMAN; AP50; CLAPM1; Clathrin adaptor complex AP2 mu subunit; Clathrin assembly protein complex 2 medium chain; Clathrin associated/assembly/adaptor protein medium 1; Clathrin coat adaptor protein AP50; Clathrin coat assembly protein AP50; Clathrin coat associated protein AP50; Clathrin coat-associated protein AP50; HA2 50 kDA subunit; mu2; Plasma membrane adaptor AP 2 50kDA protein; Plasma membrane adaptor AP-2 50 kDa protein

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .