The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Class E vacuolar protein sorting (vps) proteins are necessary for appropriate sorting of receptors in the yeast endocytic pathway. The yeast Vps4p is a member of the AAA protein family (ATPases associated with diverse cellular activities) and plays an important role in transporting proteins out of a prevacuolar endosomal compartment. In human, two non-allelic orthologous proteins (VPS4A and VPS4B) of yeast Vps4p are known and can form heteromeric complexes with each other. Both VPS4 (also known as SKD1 in mouse) proteins are class E VPSs and are involved in intracellular protein trafficking, similar to Vps4p in yeast. A human CHMP1 protein, which is implicated in multivesicular body formation, physically interacts with VPS4 . HIV-1 uses cellular machinery to bud from infected cells and requires VPS4 and TSG101/VPS23 for this budding process. Dominant negative mutant of VPS4 inhibit vacuolar protein sorting and also arrest HIV-1 and MLV budding. Thus, retroviruses normally use the VPS pathway to form multivesicular bodies during the budding process.
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Protein Aliases: cell migration-inducing 1; Cell migration-inducing gene 1 protein; MIG1; Protein SKD1; SKD1; Suppressor of K(+) transport growth defect 1; suppressor of K+ transport defect 1; vacuolar protein sorting 4B; Vacuolar protein sorting-associated protein 4B; VPS42; VPS4B
Gene Aliases: 8030489C12Rik; MIG1; SKD1; SKD1B; VPS4-2; VPS42; VPS4B