Recombinant AP-1 complex subunit mu-1 (AP1M1) fragment (residues 2-423) from Homo sapiens, encompassing the complete MHD functional domain. This high-purity protein is an essential tool for investigating clathrin-mediated vesicle trafficking, protein sorting mechanisms, and adaptor complex functions in cellular transport pathways.

The AP-1 complex subunit mu-1 is a crucial component of the clathrin-associated adaptor protein complex 1, which plays a fundamental role in protein sorting within the trans-Golgi network (TGN) and endosomes. AP complexes facilitate clathrin recruitment to membranes and recognize sorting signals in the cytosolic tails of transmembrane cargo molecules. This protein localizes to the Golgi apparatus and clathrin-coated vesicle membranes, where it functions as a peripheral membrane protein on the cytoplasmic side, forming part of the coat structure that surrounds coated vesicles at the Golgi complex. The mu-1 subunit specifically contributes to cargo recognition and sorting spe