JAM2 Human, Sf9

Junctional Adhesion Molecule 2 (JAM2) is a type I membrane protein that belongs to the immunoglobulin superfamily. It is primarily localized at the tight junctions of both epithelial and endothelial cells. JAM2 plays a crucial role in regulating paracellular permeability and leukocyte transmigration, making it a significant molecule in the context of cellular adhesion and immune response.

JAM2 consists of an extracellular domain with two immunoglobulin-like loops, a single-pass transmembrane region, and a short cytoplasmic tail. The extracellular domain is responsible for homophilic interactions, which are critical for its adhesive functions. JAM2 functions as an adhesive ligand, interacting with various immune cell types, and may have a role in lymphocyte homing to secondary lymphoid organs .

The recombinant form of Human JAM2 is produced in Sf9 Baculovirus cells. This recombinant protein is a single, glycosylated polypeptide chain containing 452 amino acids, with a molecular mass of approximately 50.7 kDa . The use of Sf9 cells, derived from the fall armyworm Spodoptera frugiperda, is a common practice for producing recombinant proteins due to their high efficiency in post-translational modifications.

JAM2’s localization at tight junctions and its role in leukocyte transmigration highlight its importance in maintaining the integrity of cellular barriers and facilitating immune surveillance. The homophilic binding of JAM2 is essential for its function in adhesive interactions and junctional organization. This binding is regulated by serine phosphorylation, which moderates its localization and interaction with other tight junction proteins like PAR-3 and ZO-1 .

Recombinant Human JAM2 produced in Sf9 cells is used in various research applications, including studies on cell adhesion, immune response, and tight junction dynamics. It serves as a valuable tool for investigating the molecular mechanisms underlying cellular interactions and barrier functions.