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.
Target:
Caveolin-1 (Tyr-14)
Application Dilute:
WB(1:300-5000)
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