Caveolin (pTyr14) antibody
Western Blotting (WB), Immunocytochemistry (ICC)
|6 references available|
|Quantity||50 µg (250 µg/ml) (Variants)|
|Price||Product not available in this region.|
|Immunogen||Phosphorylated Human Caveolin-1 (Y14) Peptide|
|Cross-Reactivity||Mouse (Murine), Rat (Rattus)|
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 alpha 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 .
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
3. 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.
4. Please refer to us for technical protocols.
|Molecular Weight||21-24 kDa|
Related Products: ABIN967389, ABIN968534
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution containing BSA, glycerol.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at -20°C.|
|Restrictions||For Research Use only|
Glenney, Soppet: "Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-transformed fibroblasts." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, Issue 21, pp. 10517-21, 1992 (PubMed).
Lee, Volonte, Galbiati 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." in: Molecular endocrinology (Baltimore, Md.), Vol. 14, Issue 11, pp. 1750-75, 2001 (PubMed).
Volonté, Galbiati, Pestell et al.: "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 stres" in: The Journal of biological chemistry, Vol. 276, Issue 11, pp. 8094-103, 2001 (PubMed).
Ushio-Fukai, Hilenski, Santanam 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." in: The Journal of biological chemistry, Vol. 276, Issue 51, pp. 48269-75, 2001 (PubMed).
Labrecque, Royal, Surprenant et al.: "Regulation of vascular endothelial growth factor receptor-2 activity by caveolin-1 and plasma membrane cholesterol." in: Molecular biology of the cell, Vol. 14, Issue 1, pp. 334-47, 2003 (PubMed).
Hill, Scherbakov, Schiefermeier et al.: "Reassessing the role of phosphocaveolin-1 in cell adhesion and migration." in: Traffic (Copenhagen, Denmark), Vol. 8, Issue 12, pp. 1695-705, 2007 (PubMed).