WB-Western Blot IP-Immunoprecipitation IHC-Immunohistochemistry IF-Immunofluorescence ICC-Immunocytochemistry FC-Flow Cytometry

Integrin αV also known as CD51, ITGAV is a transmembrane glycoprotein that pairs with various β subunits (β1, β3, β5, β6, and β8) to form functional receptors involved in cell adhesion, migration, and signal transduction. Integrin αV undergoes crucial post-translational modifications, particularly N-linked glycosylation, which is essential for proper folding, stability, and ligand-binding affinity. Glycosylation of Integrin αV influences interaction with extracellular matrix proteins such as vitronectin, fibronectin, and osteopontin, thereby affecting cellular processes like angiogenesis, wound healing, and tumor progression. These post-translational modifications play a key role in modulating protein function and involvement in various physiological and pathological conditions, including cancer metastasis and inflammatory diseases.