Anti-SI-CLP antibody [1B8]

Supplementary info

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

Activity summary

SI-CLP also known as ClpB or Caseinolytic Peptidase B is an ATP-dependent protease with a molecular mass of approximately 95 kDa. It plays a critical role in disaggregating proteins facilitating their refolding in stress conditions. The target is mainly expressed in prokaryotic organisms and some eukaryotic mitochondria. Its mechanism involves using energy derived from ATP hydrolysis to remodel protein aggregates making it essential for maintaining cellular protein homeostasis.

Biological function summary

SI-CLP proteins interact with other chaperone systems to assist in the recovery of proteins from aggregates. It forms part of a larger Clp/Hsp100 chaperone complex working together with co-chaperones like DnaK and GroEL to efficiently manage protein misfolding. This association with other molecular chaperones allows SI-CLP to execute its role in cellular stress response ensuring damaged or misfolded proteins are effectively processed or refolded.

Pathways

SI-CLP contributes significantly within the cellular protein quality control and stress response pathways. In these pathways it closely associates with DnaK facilitating protein quality control under stress conditions. Related proteins such as Hsp70 also engage in similar pathways highlighting their coordinated roles in preserving cellular function especially during stress.

Associated diseases and disorders

SI-CLP proteins have associations with neurodegenerative diseases like Alzheimer’s disease where protein aggregation occurs. It connects with proteins involved in managing protein aggregates such as Hsp70. Furthermore its role in cellular stress responses implicates it in some infectious diseases where pathogens hijack host protein quality control systems. The involvement of SI-CLP in these disorders highlights its potential as a therapeutic target to modulate protein aggregation-related pathologies.