Fractalkine Mouse

Fractalkine, also known as CX3CL1, is a unique chemokine that plays a crucial role in the immune system. It is the only member of the CX3C chemokine family and is known for its distinctive structure and function. Fractalkine exists in two forms: a membrane-bound form and a soluble form. The membrane-bound form acts as an adhesion molecule, while the soluble form functions as a chemoattractant for immune cells.

Fractalkine is synthesized as a transmembrane protein with an extracellular chemokine domain, a mucin-like stalk, a transmembrane helix, and a short cytoplasmic tail . The chemokine domain is responsible for its chemoattractant properties, while the mucin-like stalk provides structural support. The soluble form of fractalkine is generated through proteolytic cleavage by enzymes such as ADAM10 and ADAM17 .

Fractalkine plays a significant role in various physiological and pathological processes. It is involved in the recruitment of immune cells to sites of inflammation and injury. The interaction between fractalkine and its receptor, CX3CR1, is crucial for the migration and adhesion of leukocytes . This chemokine is also associated with the development of several diseases, including rheumatoid arthritis, multiple sclerosis, and atherosclerosis .

Recombinant mouse fractalkine is produced using various expression systems, including E. coli and insect cells. The recombinant protein is often used in research to study the function and signaling pathways of fractalkine. It is also utilized in bioactivity assays to investigate its chemoattractant properties .

Recombinant mouse fractalkine is widely used in immunological research. It is employed in studies focusing on the mechanisms of immune cell migration and adhesion. Additionally, it is used to explore the role of fractalkine in disease models and to develop potential therapeutic strategies targeting the CX3CL1-CX3CR1 axis .