Integrins are heterodimers composed of noncovalently associated transmembrane a and b subunits. The 16 a and 8 b 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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of Integrin &alphaE of mouse, rat and human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 864-1123 mapping within an extracellular domain of Integrin &alpha E of human origin
Tissue Specificity
epitope corresponding to amino acids 864-1123 mapping within an extracellular domain of Integrin αE of human origin