A. Western blot analysis on HeLa cell lysates using anti-Phospho-Caveolin2 (pY27) RabMAb (Cat. #AJ1141b), 1:2000 dilution. Cells were either (A) untreated (B) treated with pervanadate.
May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity)
Tissue Specificity
Expressed in endothelial cells, smooth muscle cells, skeletal myoblasts and fibroblasts
Cellular Localization
Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin (By similarity). Tyr-27- phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments
A. Western blot analysis on HeLa cell lysates using anti-Phospho-Caveolin2 (pY27) RabMAb (Cat. #AJ1141b), 1:2000 dilution. Cells were either (A) untreated (B) treated with pervanadate.
Application Notes
WB:1:1000
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Storage Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.