| CatalogCode: | NB110-55670 |
| ProductName: | Caveolin-1 (C-term) Antibody |
| Product Description: | Rabbit Monoclonal anti-Caveolin-1 (C-term) (E249) |
| Clone: | E249 |
| Clonality: | Monoclonal |
| Specificity: | A synthetic peptide corresponding to residues near C-terminus of human Caveolin-1 was used as immunogen. The antibody should recognize both alpha and beta form of Caveolin-1. |
| CrossReactivity: | Reacts in Human and Mouse. Does not react in Rat. Not tested in other species. |
| Packaging: | 0.1 ml Rabbit ascites. |
| Uses: | WB: 1:20,000IHC: 1:250 (antigen retrieval required)ICC: 1:100 |
| Background: | 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). |
| Storage: | Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles. |
| Isotype: | IgG |
| Host_Name: | Rabbit |
| Buffer: | 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, and 0.05% BSA. |
| ListPrice: | 325 |
| AppSummary: | IHC, WB, ICC |
| SpeciesSummary: | Hu, Mu, Rt(-) |
| ALTnames: | anti-CAV 1 antibody, anti-CAV antibody, anti-CAV1 antibody, anti-Caveolin 1 caveolae protein 22kDa antibody, anti-Caveolin1 antibody, anti-MSTP085 antibody, anti-VIP 21 antibody, anti-VIP21 antibody |
| PackageSize: | 0.1 ml |
| GeneralRef: | 1. Glenney, Jr., J.R. The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles. FEBS Lett. 314: 45-8 (1992). 2. Okamoto, T., et al. Caveolins, a family of scaffolding proteins for organizing preassembled signaling complexes at the plasma membrane. J. Biol. Chem. 273: 5419-5422 (1998). 3. Smart, E.J., et al. Caveolins, liquid-ordered domains, and signal transduction. Mol. Cell. Biol. 19: 7289-7304 (1999). 4. Lee, H., et al. Caveolin-1 mutations (P132L and null) and the pathogenesis of breast cancer: caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia. Am J Pathol. 161: 1357-69 (2002). |
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