Caveolin-1 (Tyr-14), Phosphospecific Antibody

Caveolins are the primary structural components of the plasma membrane microdomains, caveolae. Three members of the caveolin family (caveolin-1, -2, and -3) have been identified, and each has distinct expression patterns. Caveolins are involved in diverse biological functions, including vesicular trafficking, cholesterol homeostasis, cell adhesion and apoptosis. Caveolins can interact with various signaling molecules, including G-proteins, receptor tyrosine kinases, PKCs, and Src family kinases. Phosphorylation at Tyr-14 is essential for caveolin association with SH2 or PTB domain-containing adaptor proteins, while phosphorylation at Ser-80 regulates caveolin binding to the ER membrane and entry into the secretory pathway.

Clone M283 was generated from a phospho-Caveolin-1 (Tyr-14) synthetic peptide corresponding to amino acids surrounding tyrosine 14 in human Caveolin-1.

This antibody detects a 21 kDa* protein corresponding to the apparent molecular mass of caveolin-1 on SDS-PAGE immunoblots of human A431 cells treated with EGF or pervanadate, and is not observed in untreated cells. This sequence has significant homology to the conserved site in rat and mouse Caveolin-1.