PFDN4 Human

The prefoldin complex is a heterohexameric structure composed of six subunits: two alpha and four beta subunits. PFDN4 belongs to the beta subunit family and plays a significant role in the assembly and function of the prefoldin complex . The complex forms a double beta barrel assembly with six protruding coiled-coils, which are crucial for its chaperone activity .

Prefoldin binds to nascent polypeptide chains and stabilizes them, preventing premature folding and aggregation. It then transfers these polypeptides to the cytosolic chaperonin (c-CPN) for further folding and maturation . This process is vital for the proper functioning of various cellular processes, including protein synthesis, assembly, and degradation.

Recombinant Human PFDN4 is a laboratory-produced version of the natural protein, expressed in Escherichia coli for research purposes. It is typically purified to a high degree of purity (>95%) and is used in various biochemical assays, including SDS-PAGE and HPLC . The recombinant protein is often tagged with a His tag at the N-terminus to facilitate purification and detection .

Recombinant PFDN4 is widely used in research to study protein folding mechanisms, chaperone activity, and the role of prefoldin in cellular homeostasis. It is also used in structural biology to understand the assembly and function of the prefoldin complex .

Dysfunction in the prefoldin complex, including mutations in PFDN4, has been implicated in various diseases, such as neurodegenerative disorders. The prefoldin complex has been shown to inhibit the early stages of α-synuclein aggregation and assist in the autophagy-dependent degradation of pathogenic proteins, highlighting its potential therapeutic importance .