Alix, a phylogenetically conserved cytosolic scaffold protein, contains an N-terminal Bro1 domain, a coiled-coil region and a C-terminal proline-rich domain. Originally identified as an ALG-2 (apoptosis-linked gene 2)-interacting protein involved in programmed cell death, Alix also regulates many other cellular processes, such as endocytic membrane trafficking and cell adhesion through interactions with ESCRT (endosomal sorting complex required for transport) proteins, endophilins, and CIN85 (Cbl-interacting protein of 85kD). Apoptosis-linked gene-2 interacting protein X (ALIX) is also known as Programmed cell death 6-interacting protein or Hp95. ALIX is a 868aa and a ~90kDa cytoplasmic protein containing a single BRO1 domain implicated in endosomal targeting. ALIX was first reported to play a role in apoptosis dependent on its association with PDCD6 but has subsequently shown to be involved in endocytosis, viral budding and actin cytoskeletal assembly. This product has been used extensively for the detection of ALIX by Western blot and for the identification of an ALIX homologue in the sea urchin Paracentrotus lividus.