BD Transduction Laboratories™ Purified Mouse Anti- Caveolin-1 (pY14)
Clone 56/Caveolin (pY14) (RUO)
Western blot analysis of caveolin-1 (pY14) on lysates from A431 cells (Human epithelial carcinoma; ATCC CRL-1555) treated with 100 ng/mL EGF. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti- caveolin-1 (pY14) antibody.
Immunohistochemistry: Zinc-fixed paraffin-embedded rat brain section stained with the mouse anti- caveolin-1 (pY14) antibody (40X magnification).
Western blot analysis of caveolin-1 (pY14) on lysates from A431 cells (Human epithelial carcinoma; ATCC CRL-1555) treated with 100 ng/mL EGF. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti- caveolin-1 (pY14) antibody.
Immunohistochemistry: Zinc-fixed paraffin-embedded rat brain section stained with the mouse anti- caveolin-1 (pY14) antibody (40X magnification).
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
Caveolin (VIP21) localizes to non-clathrin membrane invaginations (caveolae) on the inner surface of the plasma membrane. In addition, it is present in the trans-Golgi network (TGN) and in apically and basolaterally destined transport vesicles. Caveolin is a transmembrane adaptor molecule that recognizes GPI-linked proteins and interacts with downstream cytoplasmic signaling molecules, such as src-family tyrosine kinases and hetero-trimeric G proteins. Caveolin forms large lipid-binding oligomers, which are thought to play a role in caveolae formation. It may also function as a scaffolding protein, which organizes signaling molecules. This functional role is supported by the fact that caveolin interacts directly with inactive ras and G-protein α subunits. Phosphorylation of caveolin at Tyr-14, Ser-88, and other residues in v-src transformed cells leads to flattening, aggregation, and fusion of caveolae and caveolae-derived vesicles. Thus, caveolin is the principle protein of caveolae and may be involved in v-src mediated cellular transformation.
This antibody has also been reported to cross-react to paxillin in mouse embryonic fibroblasts (MEF), observable to migrate at ~ 68 kDa .
Development References (6)
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Glenney JR, Soppet D. Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-transformed fibroblasts. Proc Natl Acad Sci U S A. 1992; 89(21):10517-10521. (Biology). View Reference
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Hill M, Scherbakov N, Schiefermeier N, et al. Reassessing the role of phosphocaveolin-1 in cell adhesion and migration. Traffic. 2007; 8:1695-1705. (Clone-specific).
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Labrecque L, Royal I, Surprenant DS, Patterson C, Gingras D, Béliveau R. Regulation of vascular endothelial growth factor receptor-2 activity by caveolin-1 and plasma membrane cholesterol. Mol Biol Cell. 2003; 14(1):334-347. (Biology: Western blot). View Reference
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Lee H, Volonte D, Galbiati F, et al. Constitutive and growth factor-regulated phosphorylation of caveolin-1 occurs at the same site (Tyr-14) in vivo: identification of a c-Src/Cav-1/Grb7 signaling cassette. Mol Endocrinol. 2000; 14(11):1750-1775. (Biology: Immunofluorescence, Western blot). View Reference
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Ushio-Fukai M, Hilenski L, Santanam N, et al. Cholesterol depletion inhibits epidermal growth factor receptor transactivation by angiotensin II in vascular smooth muscle cells: role of cholesterol-rich microdomains and focal adhesions in angiotensin II signaling. J Biol Chem. 2001; 276(51):48269-48275. (Biology: Immunofluorescence, Western blot). View Reference
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Volonté D, Galbiati F, Pestell RG, Lisanti MP. Cellular stress induces the tyrosine phosphorylation of caveolin-1 (Tyr(14)) via activation of p38 mitogen-activated protein kinase and c-Src kinase. Evidence for caveolae, the actin cytoskeleton, and focal adhesions as mechanical sensors of osmotic stress. J Biol Chem. 2001; 276(11):8094-8103. (Biology: Immunofluorescence, Western blot). View Reference
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