|Application ||IHC, WB|
|Calculated MW||20472 Da|
|Other Names||Caveolin-1, CAV1, CAV|
|Target/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.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Caveolin-1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)- mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3- dependent manner. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway. Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (PubMed:25893292).|
|Cellular Location||Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein Membrane, caveola; Peripheral membrane protein. Membrane raft. Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane Membrane protein of caveolae|
|Tissue Location||Expressed in muscle and lung, less so in liver, brain and kidney|
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Provided below are standard protocols that you may find useful for product applications.
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).
1. Glenney, Jr., J.R. The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles. FEBS Lett. 314: 45
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
3. Smart, E.J., et al. Caveolins, liquid-ordered domains, and signal transduction. Mol. Cell. Biol. 19: 7289
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
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