Integrins are cell adhesion molecules that can mediate bidirectional transfer of signals across the plasma membrane. The cytoplasmic domains of integrin family members interact with components of the signal transduction apparatus within cells. Integrin receptors contain noncovalently associated α and β subunits that consist of a large extracellular region (the ligand-binding domain), a short transmembrane region, and a cytoplasmic domain of varying length. In mammals, at least 17 α subunits and 8 β subunits have been identified and these proteins can heterodimerize to form at least 22 different receptors. Integrin α5 and integrin β1 form a receptor for fibronectin and fibrinogen. This receptor is important for vascular development. Both integrin subunits of the fibronectin receptor are heavily glycosylated in their extracellular domains. This modification is essential for proper cell attachment to basal membranes. Integrin α5 has been reported to suppress apoptosis by a Bcl-2 pathway and the C-terminal region is critical for cell motility and cytoskeletal rearrangements.
Wang, L. et al. (2012) J Cell Physiol. 227(2):474.
*For more information, see UniProt Accession P08648
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: