ICAM2 Human

ICAM-2 is composed of two extracellular immunoglobulin-like domains, a transmembrane region, and a short cytoplasmic tail . It is predominantly found at endothelial junctions, where it supports homophilic adhesion, meaning it can bind to other ICAM-2 molecules on adjacent cells . This localization is essential for maintaining endothelial integrity and vascular homeostasis.

1. Leukocyte Trafficking: ICAM-2 interacts with integrins such as lymphocyte function-associated antigen-1 (LFA-1) and macrophage-1 antigen (Mac-1), facilitating the adhesion and transmigration of leukocytes across the endothelium . This process is vital for immune surveillance and response to inflammation.

2. Angiogenesis: ICAM-2 is involved in the formation of new blood vessels from pre-existing ones. It regulates endothelial cell migration, survival, and tube formation, which are critical steps in angiogenesis . ICAM-2-deficient endothelial cells exhibit impaired angiogenesis, highlighting its importance in this process .

3. Vascular Permeability: ICAM-2 plays a role in maintaining the barrier function of endothelial cells. It regulates the localization of N-Cadherin at cell junctions and activates the small GTPase Rac-1, which is essential for endothelial barrier integrity . ICAM-2-deficient mice show increased vascular permeability, indicating its role in controlling endothelial junctions .

Human recombinant ICAM-2 is produced using recombinant DNA technology, which involves inserting the gene encoding ICAM-2 into a suitable expression system, such as bacteria or mammalian cells. This allows for the large-scale production of ICAM-2 for research and therapeutic purposes.

Recombinant ICAM-2 is used in various studies to understand its role in physiological and pathological processes. It is also being explored as a potential therapeutic target for diseases involving inflammation and angiogenesis.