Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Phospho-Caveolin-1 (Tyr14) Antibody #3251

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Mk (Dg) Endogenous 23, 25 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  Dg=Dog
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-Caveolin-1 (Tyr14) Antibody detects endogenous levels of caveolin-1 only when phosphorylated at tyrosine 14. The antibody does not cross-react with paxillin, caveolin-2, -3 or caveolin-1beta, the short isoform of caveolin-1.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr14 of human caveolin-1. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa cells, untreated (-) or H2O2-treated (+), using Phospho-Caveolin-1 (Tyr14) Antibody (upper) and Caveolin-1 (D46G3) XP® Rabbit mAb #3267 (lower).

Background

The 21-24 kDa integral proteins, caveolins, are the principal structural components of the cholesterol/sphingolipid-enriched plasma membrane microdomain caveolae. Three members of the caveolin family (caveolin-1, -2, and -3) have been identified with different tissue distributions. Caveolins form hetero- and homo-oligomers that interact with cholesterol and other lipids (1). Caveolins are involved in diverse biological functions, including vesicular trafficking, cholesterol homeostasis, cell adhesion, and apoptosis, and are also implicated in neurodegenerative disease (2). Caveolins interact with multiple signaling molecules such as Gα subunit, tyrosine kinase receptors, PKCs, Src family tyrosine kinases, and eNOS (1,2). It is believed that caveolins serve as scaffolding proteins for the integration of signal transduction. Phosphorylation at Tyr14 is essential for caveolin association with SH2 or PTB domain-containing adaptor proteins such as GRB7 (3-5). Phosphorylation at Ser80 regulates caveolin binding to the ER membrane and entry into the secretory pathway (6).

  1. Okamoto, T. et al. (1998) J Biol Chem 273, 5419-22.
  2. Smart, E.J. et al. (1999) Mol Cell Biol 19, 7289-304.
  3. Nomura, R. et al. (1999) Mol. Biol. Cell 10, 975-986.
  4. Volonte, D. et al. (2001) J. Biol. Chem. 276, 8094-8103.
  5. Lee, H. et al. (2000) Mol Endocrinol 14, 1750-75.
  6. Schlegel, A. et al. (2001) J Biol Chem 276, 4398-408.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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