STIP1 Human

The STIP1 gene is located on chromosome 11q13.1 and consists of 14 exons . The protein itself is characterized by the presence of nine tetratricopeptide repeat (TPR) motifs, which are clustered into domains of three TPRs each . These motifs are essential for protein-protein interactions, allowing STIP1 to bind both Hsp70 and Hsp90, facilitating the transfer of substrate proteins between these chaperones .

STIP1 functions as a molecular scaffold, bringing together Hsp70 and Hsp90 to form a chaperone complex that assists in the proper folding of newly synthesized proteins and the refolding of misfolded proteins . This process is vital for maintaining cellular protein homeostasis, especially under stress conditions where the demand for protein folding increases .

In addition to its role in protein folding, STIP1 is involved in various cellular processes, including signal transduction, cell cycle regulation, and apoptosis . It has been shown to interact with several signaling molecules, such as the protein tyrosine kinase JAK2, and modulate their activity through phosphorylation .

STIP1 is commonly overexpressed in various types of cancer, where it contributes to tumor progression by promoting cell proliferation and survival . Its interaction with Hsp90 is particularly important in cancer cells, as Hsp90 stabilizes many oncogenic proteins. Therefore, targeting the STIP1-Hsp90 interaction is being explored as a potential therapeutic strategy for cancer treatment .

Human recombinant STIP1 is produced using recombinant DNA technology, which involves inserting the human STIP1 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in research to study its structure, function, and interactions with other proteins, as well as in drug development to screen for potential inhibitors of its activity .