Integrin Beta4 (Tyr-1494), phospho-specific polyclonal, anti-human, mouse, rat

Background:
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 α6β4receptors are found in basement membrane along with laminin-5. These receptors are expressed in epithelial, schwann, endothelial and some immune cells. The cytoplasmic domain of the Integrin β4 subunit recruits the adaptor protein Shc and is required for assembly of hemidesmosomes. Tyrosine phosphorylation of multiple sites within the cytoplasmic domain regulates these cellular events. In particular, tyrosine 1526 interacts with the phosphotyrosine binding domain of Shc and is required for Shc activation. In addition, tyrosine 1494 is required for integrin-mediated IRS-2 phosphorylation and activation of PI3-kinase. More importantly this site is critical for integrin α6β4 increases in carcinoma invasion.

Immunogen: Phospho-Integrin β4 (Tyr-1494) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 1494 of human Integrin β4. This peptide sequence is found in all three Integrin β4 isoforms and is highly conserved in rat and mouse Integrin β4.

Specificity: This antibody was cross-adsorbed to phospho-tyrosine coupled to agarose then affinity purified using phospho-Integrin β4 (Tyr-1494) peptide (without carrier). The antibody detects a 200kDa* protein corresponding to the molecular mass of Integrin β4 on SDS-PAGE immunoblots of A431 cells treated with pervanadate, but not in control cells. Similar results were also observed in src-transformed Hct116 cells treated with pervanadate.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.