VPS24 is a part of the ESCRT-III complex, which is involved in the final stages of MVB formation. It interacts directly with other ESCRT-III components, such as CHMP2 and CHMP4, to facilitate the disassembly of the complex in an ATP-dependent manner . This interaction is critical for the proper functioning of the ESCRT machinery and the regulation of protein sorting within the cell.
One of the notable functions of VPS24 is its involvement in the budding and exocytosis of viral proteins, particularly during HIV-1 infection. The virus hijacks the ESCRT-III complex to mediate the release of viral particles from the host cell. Overexpression of VPS24 has been shown to strongly inhibit HIV-1 release, highlighting its potential as a therapeutic target .
Recombinant human VPS24 protein is typically produced in Escherichia coli (E. coli) and purified using conventional chromatography techniques. The recombinant protein often includes an N-terminal His-tag to facilitate purification and detection. The amino acid sequence of the recombinant VPS24 corresponds to the full-length human protein, ensuring its functionality in research applications .
Recombinant VPS24 is widely used in various research studies to understand its role in cellular processes and disease mechanisms. It is particularly valuable in studies related to protein sorting, viral budding, and the development of potential therapeutic interventions for diseases involving the ESCRT machinery.
For optimal stability, recombinant VPS24 should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid repeated freeze-thaw cycles to maintain the protein’s integrity. The protein is typically supplied in a buffer containing Tris-HCl, glycerol, NaCl, and DTT to ensure its stability and functionality .