Amphiphysin/AMPH Antibody

AMPH (Amphiphysin; also AMPH1) is a 128 kDa member of the Amphiphysin family, BAR superfamily of proteins. Although its calculated MW is only 78 kDa, it runs anomalously in SDS-Page at 125-128 kDa. It is expressed in neurons, Sertoli cells, possibly in anterior pituitary endocrine cells and apparently cardiac muscle. It appears to form heterodimers with AMPH2, and in this configuration, promotes clathrin-associated endocytic vesicle formation. Furthermore, and perhaps related, AMPH also interacts with N-WASP, initiating actin polymerization. Human AMPH is 695 amino acids (aa) in length. It contains an N-terminal BAR domain (aa 24-240) that binds lipids, a central region that binds AP2 (aa 322-340) and clathrin (aa 347-386), and a C-terminal SH3 domain (aa 622-695) that binds proline-rich ligands. There is one known 108 kDa splice variant that shows a deletion of aa 425-466. Over aa 204-300, human AMPH shares 98% aa identity with mouse AMPH.