Anti-STIP1/STI1 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

STIP1 also known as STI1 is a stress-induced phosphoprotein that assists in the folding and stabilization of other proteins. The protein has a mass of approximately 63 kDa. It acts as a co-chaperone and interacts with key chaperones like HSP70 and HSP90 facilitating the transfer of client proteins between them. STIP1 is expressed in various tissues with significant presence in the nervous system and reproductive organs. It contributes to the protein homeostasis by modulating chaperone activity and protecting cells during stress conditions like high temperatures or oxidative stress.

Biological function summary

The stress-induced phosphoprotein STIP1 functions within cytoplasm and is pivotal for cellular integrity. It forms a complex with HSP70 and HSP90 that regulates the folding and activation of a range of client proteins including steroid hormone receptors and kinases. This modulation influences protein activity stability and degradation. STIP1 impacts signal transduction pathways cellular growth and stress responses by influencing how effectively client proteins perform their biological roles within cells.

Pathways

The protein STIP1 plays a significant part in the steroid hormone signaling pathway and the protein folding network. It helps facilitate the proper folding and function of steroid hormone receptors through its interaction with major chaperone proteins HSP70 and HSP90. Both these pathways are important for cell survival and proper cell regulation. By helping with the maturation and activation of client proteins STIP1 ensures that cellular responses to various internal and external signals proceed efficiently.

Associated diseases and disorders

The involvement of STIP1 emerges most clearly in neurodegenerative conditions like Alzheimer's disease and cancer. In Alzheimer's disease STIP1 interacts with prion proteins which influence amyloid-beta aggregation and may impact disease progression. In cancer the protein assists in stabilizing client proteins essential for tumor progression such as steroid hormone receptors and protein kinases. Disruption in STIP1 function can lead to impaired cellular stress responses and may contribute to disease pathogenesis.