Calumenin Human

Calumenin contains six EF-hand domains, which are crucial for its calcium-binding properties . It is expressed at high levels in various tissues, including the heart, placenta, and skeletal muscle . The protein is secreted and plays a significant role in the endoplasmic reticulum (ER), where it binds to various proteins and assists in their proper folding and function .

Calumenin has been implicated in several cellular processes, including:

1. Protein Folding and Quality Control: As a molecular chaperone, calumenin assists in the proper folding of newly synthesized proteins within the ER .
2. Calcium Homeostasis: By binding calcium ions, calumenin helps maintain calcium homeostasis within the ER .
3. Tumor Development: Recent studies have shown that calumenin plays a role in tumor development, particularly in lung adenocarcinoma. It enhances the proliferation and migration of cancer cells, making it a potential target for cancer therapy .

Recombinant calumenin is produced using recombinant DNA technology, which involves inserting the gene encoding calumenin into a suitable expression system, such as bacteria or mammalian cells. This allows for the large-scale production of the protein for research and therapeutic purposes .

Calumenin’s role in various cellular processes and its involvement in diseases like cancer make it a significant target for research. Understanding its mechanisms can lead to the development of new therapeutic strategies for conditions such as lung adenocarcinoma .