JAML Extracellular Domain (human, recombinant)

Junctional adhesion molecule-like (JAML) is a junctional adhesion molecule and member of the immunoglobulin superfamily with roles in maintenance of tight junctions and immune regulation. It is composed of an N-terminal extracellular domain, which contains two immunoglobulin-like domains, a transmembrane domain, and a C-terminal cytoplasmic tail. JAML is expressed by neutrophils, monocytes, activated CD8+ T cells, alphabeta T cells, tissue-resident gammadelta T cells, and renal podocytes and localizes to the plasma membrane at cell-cell contact regions but is absent at free cell boundaries. It regulates leukocyte adhesion and transendothelial migration, functions as a co-regulatory receptor for T cell activation, and regulates lipid metabolism in podocytes. Podocyte-specific Jaml knockout reduces podocyte injury and proteinuria in db/db diabetic mice and in a mouse model of doxorubicin-induced nephropathy. Increased JAML expression is associated with improved median and overall survival in patients with subcutaneous melanoma. Cayman's JAML Extracellular Domain (human, recombinant) protein consists of 267 amino acids, has a calculated molecular weight of 30. kDa and a predicted N-terminus of Leu20 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 40 kDa due to glycosylation.