Integrins are heterodimers composed of noncovalently associated transmembrane alpha and beta subunits. The 16 alpha and 8 beta subunits heterodimerize to produce more than 20 different receptors. Most integrin receptors bind ligands that are components of the extracellular matrix, including fibronectin, collagen and vitronectin. Certain integrins can also bind to soluble ligands such as fibrinogen, or to counterreceptors on adjacent cells such as the intracellular adhesion molecules (ICAMs), leading to aggregation of cells. Ligands serve to cross-link or cluster integrins by binding to adjacent integrin receptors, both receptor clustering and ligand occupancy are necessary for the activation of integrin-mediated responses. In addition to mediating cell adhesion and cytoskeletal organization, integrins function as signaling receptors. Signals transduced by integrins play a role in many biological processes, including cell growth, differentiation, migration and apoptosis.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200 IF: 1:50~1:200
Application Notes:
ITGB1 (Y783) polyclonal antibody detects endogenous levels of ITGB1 protein.
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