Anti-Human ITGB7 Antibody Pair

Product Description: Integrin subunit beta 7 (ITGB7) is a transmembrane glycoprotein encoded by the ITGB7 gene, playing a critical role in cell adhesion and immune regulation. It pairs with alpha subunits ITGA4 (forming alpha4beta7) or ITGAE (forming alphaEbeta7), creating receptors that mediate lymphocyte migration and homing to gut-associated lymphoid tissues (GALT). The extracellular domain of ITGB7 contains an I-like domain for ligand binding, a PSI domain, hybrid domain, EGF repeats, and a beta-tail domain. These structural features enable interactions with adhesion molecules like MAdCAM-1 and E-cadherin, facilitating mucosal immunity and epithelial binding. ITGB7 dynamically regulates ligand affinity through conformational changes and interacts with intracellular signaling proteins via its cytoplasmic tail. Clinically, ITGB7 is implicated in inflammatory bowel diseases due to its role in lymphocyte trafficking to inflamed gut tissues. Protein Function: Integrin ITGA4/ITGB7 (alpha-4/beta-7) (Peyer patches-specific homing receptor LPAM-1) is an adhesion molecule that mediates lymphocyte migration and homing to gut-associated lymphoid tissue (GALT) (Probable). Integrin ITGA4/ITGB7 interacts with the cell surface adhesion molecules MADCAM1 which is normally expressed by the vascular endothelium of the gastrointestinal tract (PubMed:10837471, PubMed:14608374). Also interacts with VCAM1 and fibronectin, an extracellular matrix component (Probable). It recognizes one or more domains within the alternatively spliced CS-1 region of fibronectin (Probable). Interactions involve the tripeptide L-D-T in MADCAM1, and L-D-V in fibronectin (Probable). Integrin ITGAE/ITGB7 (alpha-E/beta-7, HML-1) is a receptor for E-cadherin (PubMed:10837471) , (Microbial infection) Binds to HIV-1 gp120, thereby allowing the virus to enter GALT, which is thought to be the major trigger of AIDS disease. Interaction would involve a tripeptide L-D-I in HIV-1 gp120 [The Uniprot Consortium]