A recombinant human partial protein (amino acids 282-415) was used as the immunogen for the Occludin antibody.
Occludin is a tetraspan integral membrane protein in epithelial and endothelial tight junction (TJ) structures that can contain two extracellular loops. The protein exists in a variety of phosphorylated forms. Phosphorylation is involved in regulating both the localization and the function of Occludin. Expression of Occludin is upregulated by polyunsaturated fatty acids, increasing trans-endothelial cell resistance and reducing cellular permeability to large molecules. The level of Occludin varies greatly depending on tissue, in brain tissue, Occludin is highly expressed at cell-cell contact sites. Non-neural tissues show lower expression and discontinuous distribution. Up-regulation of epithelial Occludin may play a role in enhancing paracellular permeability and be related to the damage to the tight junction.
