CD29 Mouse, Unlabeled, Clone: 18, BD

Description

• Integrins are membrane receptors that mediate cell-cell or cell-matrix adhesion
• All integrins are transmembrane heterodimers composed of α and β subunits and are connected to the cytoskeleton
• At least 20 integrins, formed from combinations of 12 α and 9 β subunits, have been reported
• Many of these have been implicated as transducers of molecular signals
• The β1 subgroup of this receptor family comprises at least six different dimer combinations
• Among these combinations, α2β1 is associated with type I collagen and laminin binding and regulation, α3β1 is a receptor for laminin and epiligrin, and α5β1 is a fibronectin receptor
• β1 integrins play an important role in several aspects of epidermal differentiation and morphogenesis
• Expression of the β1 subunit is regulated by growth factors such as TGF-β1
• Integrin activation, which enhances binding of T cells to endothelium, is regulated in part by phosphatidylinositol 3-kinase
• Focal adhesion kinase (FAK) and paxillin have been reported to independently bind the C-terminal, cytoplasmic domain of the β1 subunit
• FAK is reported to be enzymatically activated upon engagement of integrins with their ligands and paxillin is phosphorylated on tyrosine upon activation of FAK
• Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting