Integrins are integral membrane protein complexes that play a critical role in cellular adhesion by linking the extracellular matrix (ECM) to the cytoskeleton. First identified through their binding to fibronectin, integrins mediate essential interactions within the ECM and are now recognized as versatile targets for therapeutic intervention in diseases such as cancer, inflammation, and fibrosis. Integrins interact with a variety of ECM proteins through specific recognition motifs, such as the Arg–Gly–Asp (RGD), Leu–Asp–Val (LDV), and GFOGER sequences.

Based on their binding characteristics, integrins are classified into four main categories: leukocyte adhesion integrins, RGD-binding integrins, collagen-binding integrins, and laminin-binding integrins. Each category plays distinct roles in modulating cell adhesion, migration, and signaling pathways. Notably, RGD-binding integrins, including αvβ3, αvβ5, and α5β1, are key players in cancer cell adhesion and metastasis, while collagen-binding integrins, such as α1β1 and α2β1, are involved in tissue remodeling and fibrosis. Leukocyte adhesion integrins (e.g., αLβ2, α4β1) are pivotal for immune cell trafficking, making them important in inflammation-related therapies.

ICE Bioscience offers specialized biochemical and cell-based assays to support integrin-targeted drug discovery. For biochemical binding assays, we utilize ELISA and fluorescence polarization (FP) technologies to provide high-sensitivity measurements of integrin-ligand interactions. 

To quantify the number of adhered cells, we utilize the CellTiter-Glo (CTG) luminescence assay, which measures cellular ATP as an indicator of viable, adherent cells. This provides a sensitive and accurate quantification of cell adhesion, allowing us to assess how different factors or treatments affect integrin-mediated adhesion. 

Integrin-Targeted Binding Assays