Description
Integrins are heterodimeric transmembrane receptors that mediate cell-cell or cell-matrix adhesion. They 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. Although there is a high degree of redunancy, each integrin has a specific biological function. For example, the β3 subunit associates with αIIb in platelets where this glycoprotein complex acts as a fibrinogen receptor and mediates platelet aggregation. In endothelial cells (EC), β3 complexes with the αv subunit to form the vitronectin receptor. This receptor mediates endothelial cell adhesion to vitronectin, fibrinogen, von Willebrand factor, thrombospondin, laminin, and fibronectin. In confluent EC cultures, the αvβ3 integrin localizes to focal adhesions at the cell body and cell-cell borders. Thus, continued study of individual integrin subunits will provide insights to mechanisms of cell adhesion and signaling.
The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
