|Calculated MW||20472 Da|
|Other Names||Caveolin-1, CAV1, CAV|
|Target/Specificity||A phospho specific peptide corresponding to residues surrounding tyrosine 14 of human caveolin-1 was used as an immunogen. This antibody detects caveolin-1 phosphorylated at tyrosine 14.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Caveolin-1 Antibody Phospho (pY14) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)- mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3- dependent manner. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway.|
|Cellular Location||Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein Membrane, caveola; Peripheral membrane protein. Membrane raft Note=Colocalized with DPP4 in membrane rafts. Potential hairpin- like structure in the membrane. Membrane protein of caveolae|
|Tissue Location||Expressed in muscle and lung, less so in liver, brain and kidney|
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Provided below are standard protocols that you may find useful for product applications.
Caveolins make up a family of proteins that are principal structural components of hairpin-like domains in the plasma membrane (1). It is believed that caveolins serve as scaffolding proteins for the integration of signal transduction. Three members of caveolins (caveolin-1, -2 and -3) have been identified, possessing different tissue distributions (2). Caveolins interact with multiple signaling molecules, such as the G-protein alpha subunit (1), tyrosine kinase receptors, PKCs, Src family tyrosine kinases and eNOS (2,3). Caveolin-1 has been implicated in the pathogenesis of mammary epithelial cell hyperplasia (4). Endothelial cell (EC) migration is a critical event during multiple physiological and pathological processes. The phosphorylatable Tyr14 residue of caveolin-1 is required for polarization of the protein during transmigration but does not alter polarization during planar movement.
1. Glenney, Jr., J.R. FEBS Lett. 314: 45
2. Okamoto, T., et al. J. Biol. Chem. 273: 5419
3. Smart, E.J., et al. Mol. Cell. Biol. 19: 7289
4. Lee, H., et al. Am J Pathol. 161: 1357
5. Parat MO, et al. Mol Biol Cell 14(8):3156-68, 2003
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