VCP is a member of a family that includes putative ATP-binding proteins involved in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. VCP, as a structural protein, is associated with clathrin, and heat-shock protein Hsc70, to form a complex. VCP has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, spindle pole body function, and ubiquitin-dependent protein degradation.
Clathrin is a structural protein found in coated pits and vesicles, organelles which are important in membrane trafficking functions such as endocytosis and Golgi sorting. A 100-kD protein, designated valosin-containing protein or VCP by early investigators, is a structural protein complexed with clathrin.
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