Anti-Calpain 9 antibody [EPR13422]

Supplementary info

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

Activity summary

Calpain 9 also known as CAPN9 is a calcium-dependent cysteine protease enzyme that plays a role in proteolytic processes. It has a molecular mass of approximately 114 kDa. Capable of autolytic activation Calpain 9 becomes functional in the presence of calcium ions. Expression of Calpain 9 occurs mainly in the gastrointestinal tract particularly in the stomach and small intestine. This enzyme has distinct activities compared to other calpains partially due to its unique conserved domains affecting substrate specificity.

Biological function summary

The enzyme assists in maintaining cellular homeostasis through its proteolytic functions. Calpain 9 does not usually exist as part of large protein complexes but it interacts dynamically with substrates and other cellular components. It participates in various cellular processes such as cell cycling differentiation and apoptosis. Essentially Calpain 9 regulates specific protein modifications and degradations which affect cellular structural integrity and signal transduction mechanisms.

Pathways

Calpain 9 influences intracellular signaling and remodeling being particularly linked to the non-canonical Wnt signaling pathway and calcium signaling pathways. Within these pathways Calpain 9 works alongside other related proteins such as GSK-3β in the Wnt pathway and calmodulin in calcium signaling. These pathways are important for the modulation of cellular responses to stimuli and contribute to the fine-tuning of cellular activities impacting tissue development and repair processes.

Associated diseases and disorders

The dysregulation of Calpain 9 takes part in gastric cancer progression and susceptibility to inflammatory bowel disease (IBD). It contributes to tumorigenesis when proteolytic balance within cellular environments shifts unfavorably. Furthermore alterations in Calpain 9 expression or activity influence interactions with proteins like E-cadherin within cancer progression. Understanding these relationships may provide insights into novel therapeutic targets or diagnostic markers for specific diseases involving impaired protease regulation.