ICAM1 Human HEK

ICAM-1 is composed of an extracellular domain, a single transmembrane domain, and a cytoplasmic domain . The extracellular domain is heavily glycosylated and contains multiple loops created by disulfide bridges, which are essential for its function . The primary role of ICAM-1 is to facilitate the adhesion and transmigration of leukocytes (white blood cells) across the endothelium to sites of inflammation .

Upon cytokine stimulation, the expression of ICAM-1 is significantly upregulated . It binds to integrins, specifically LFA-1 (CD11a/CD18) and Mac-1 (CD11b/CD18), on leukocytes, which allows these cells to adhere to the endothelial cells and migrate into tissues . This process is vital for the immune response, as it enables leukocytes to reach and combat sites of infection or injury .

ICAM-1 is a key player in various inflammatory diseases. Its expression is increased in conditions such as ulcerative colitis, rheumatoid arthritis, and neurodegenerative diseases like Parkinson’s disease . In these diseases, ICAM-1 facilitates the recruitment of leukocytes to the affected tissues, contributing to the inflammatory response .

Human recombinant ICAM-1 is produced using HEK293 cells, a type of human embryonic kidney cell line . This recombinant protein is used in research to study the function and role of ICAM-1 in various biological processes and diseases . The recombinant ICAM-1 protein expressed in HEK293 cells is typically tagged with a His-tag for easy purification and detection .

Recombinant ICAM-1 is widely used in research to investigate its role in cell signaling, immune response, and disease mechanisms. It is particularly valuable in studying the interactions between leukocytes and endothelial cells, as well as the molecular pathways involved in inflammation and immune responses .